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Medin J, Kyriakidou M, Santoso B, Gupta P, Järlebark J, Schaefer A, Ferrand-Drake Del Castillo G, Cans AS, Dahlin A. Enzymatic Polymer Brush Interfaces for Electrochemical Sensing in Biofluids. ACS APPLIED BIO MATERIALS 2025; 8:4008-4019. [PMID: 40269558 DOI: 10.1021/acsabm.5c00146] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 04/25/2025]
Abstract
Electrochemical sensors enable specific and sensitive detection of biological markers. However, most small molecule analytes are not electroactive. Therefore, enzymes are widely used for selective breakdown of the markers into electro-active species. However, it has proven difficult to design a sensor interface where any enzyme can be controllably immobilized in high amounts with preserved activity. In addition, most interfaces cease to function in biofluids due to "fouling" of the sensor surface. Here we present a generic strategy employting polymer brushes for enzymatic electrochemical sensing which resolves these issues. Generic conjugation chemistry is used to covalently bind large amounts of enzymes (>1 μg/cm2). Remarkably, despite this enzyme load, the (∼200 nm thick) brushes remain highly hydrated and practically invisible by electrochemical methods: Small molecules freely access the underlying electrode and the charge transfer resistance increment is exceptionally low (<10 Ω). The enzymatic polymer brush interfaces enable specific detection of the biomarkers glucose and glutamate by simple chronoamperometry. Furthermore, by sequential immobilization of several enzymes, cascade reactions can be performed, as illustrated by detection of acetylcholine. Finally, the sensor interface still functions in cerebrospinal fluid (10× diluted, unfiltered). In conclusion, polymer brushes provide extended possibilities for enzymatic catalysis and electrochemical sensing.
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Affiliation(s)
- Jesper Medin
- Department of Chemistry and Chemical Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden
| | - Maria Kyriakidou
- Nyctea Technologies AB, AstraZeneca BioVentureHub, 431 83 Mölndal, Sweden
| | - Bagus Santoso
- Nyctea Technologies AB, AstraZeneca BioVentureHub, 431 83 Mölndal, Sweden
| | - Pankaj Gupta
- Department of Chemistry and Chemical Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden
| | - Julia Järlebark
- Department of Chemistry and Chemical Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden
| | - Andreas Schaefer
- Department of Chemistry and Chemical Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden
| | | | - Ann-Sofie Cans
- Department of Chemistry and Chemical Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden
| | - Andreas Dahlin
- Department of Chemistry and Chemical Engineering, Chalmers University of Technology, 41296 Gothenburg, Sweden
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2
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Sidhu AK, Patil SN, Gaikwad VB. Direct binding and characterization of laccase onto iron oxide nanoparticles. NANOTECHNOLOGY 2024; 35:235101. [PMID: 38364270 DOI: 10.1088/1361-6528/ad2a02] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Subscribe] [Scholar Register] [Received: 09/26/2023] [Accepted: 02/13/2024] [Indexed: 02/18/2024]
Abstract
Iron oxide nanoparticles (IONPs) exhibit unique magnetic properties and possess a high surface-to-volume ratio, making them ideal candidates for the conjugation of substances, including enzymes. Laccase (EC 1.10.3.2), an oxidative enzyme with diverse applications, presents an opportunity for enhancing stability and reusability through innovative immobilization techniques, thus reducing overall process costs. In this study, we employed a direct binding procedure via carbodiimide activation to conjugate laccase onto IONPs synthesized using thermal chemical coprecipitation. Stabilization of the nanoparticles was achieved using thioglycerol and polyvinyl alcohol (PVA) as capping agents. Characterization of the synthesized nanoparticles was conducted using UV-spectroscopy, Fourier transform infrared spectroscopy (FTIR), x-ray diffraction, scanning electron microscopy, and energy dispersive x-ray spectroscopy. FTIR spectroscopy analysis confirmed successful laccase binding to magnetic nanoparticles, with binding efficiencies of 90.65% and 73.02% observed for thioglycerol and PVA capped IONPs, respectively. Furthermore, the conjugated enzyme exhibited remarkable stability, retaining nearly 50% of its initial activity after 20 reuse cycles. This research demonstrates that immobilizing laccase onto IONPs enhances its activity, stability, and reusability, with the potential for significant cost savings and expanded applications in various fields.
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Affiliation(s)
- Amanpreet K Sidhu
- Assistant Professor, Department of Biotechnology, Khalsa College, Amritsar, Punjab, India
| | - Sucheta N Patil
- Professor, Department of Microbiology, K.T.H.M College, Nashik, Maharashtra, India
| | - Vishwas B Gaikwad
- Regional Director, Yashwantrao Chavan Maharashtra Open University, Nashik, Maharashtra, India
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3
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Czyzewska K, Trusek A. Critical Parameters in an Enzymatic Way to Obtain the Unsweet Lactose-Free Milk Using Catalase and Glucose Oxidase Co-Encapsulated into Hydrogel with Chemical Cross-Linking. Foods 2022; 12:113. [PMID: 36613329 PMCID: PMC9818303 DOI: 10.3390/foods12010113] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/03/2022] [Revised: 12/19/2022] [Accepted: 12/22/2022] [Indexed: 12/28/2022] Open
Abstract
The presented work involves obtaining and characterising a two-enzymatic one-pot bioreactor, including encapsulated (co-immobilised) glucose oxidase and catalase. The enzymatic capsules were applied to produce unsweet, lactose-free milk during low-temperature catalysis. Furthermore, operational conditions, like pH and aeration, were selected in the paper, which sorts out discrepancies in literature reports. All experiments were carried out at 12 °C, corresponding to milk storage and transportation temperature. Preliminary studies (for reasons of analytical accuracy) were carried out in a buffer (pH, concentration of sugars mimicking conditions in the lactose-free milk, the initial glucose concentration 27.5 g/L) verified by processes carried out in milk in the final stage of the study. The presented results showed the need for regulating pH and the aeration of the reaction mixture in the continuous mode during the process. The procedure of co-immobilisation was performed in an alginate matrix with the cross-linking of glutaraldehyde or carbodiimide while carbodiimide showed better enzymes retention inside alginate capsules. Co-encapsulated enzymes could be used for nine cycles, preserving finally about 40% of the initial activity.
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Affiliation(s)
| | - Anna Trusek
- Group of Micro, Nano and Bioengineering, Wroclaw University of Science and Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland
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Rusu AG, Chiriac AP, Nita LE, Balan V, Serban AM, Croitoriu A. Synthesis and Comparative Studies of Glucose Oxidase Immobilized on Fe 3O 4 Magnetic Nanoparticles Using Different Coupling Agents. NANOMATERIALS (BASEL, SWITZERLAND) 2022; 12:2445. [PMID: 35889669 PMCID: PMC9318457 DOI: 10.3390/nano12142445] [Citation(s) in RCA: 2] [Impact Index Per Article: 0.7] [Reference Citation Analysis] [Abstract] [Key Words] [Grants] [Track Full Text] [Download PDF] [Figures] [Subscribe] [Scholar Register] [Received: 06/20/2022] [Revised: 07/12/2022] [Accepted: 07/15/2022] [Indexed: 11/30/2022]
Abstract
Squaric acid (SA) is a compound with potential to crosslink biomacromolecules. Although SA has become over the last years a well-known crosslinking agent as a result of its good biocompatibility, glutaraldehyde (GA), a compound with proven cytotoxicity is still one of the most used crosslinkers to develop nanomaterials. In this regard, the novelty of the present study consists in determining whether it may be possible to substitute GA with a new bifunctional and biocompatible compound, such as SA, in the process of enzyme immobilization on the surface of magnetic nanoparticles (MNPs). Thus, a direct comparison between SA- and GA-functionalized magnetic nanoparticles was realized in terms of physico-chemical properties and ability to immobilize catalytic enzymes. The optimal conditions of the synthesis of the two types of GOx-immobilized MNPs were described, thus emphasizing the difference between the two reagents. Scanning Electron Microscopy and Dynamic Light Scattering were used for size, shape and colloidal stability characterization of the pristine MNPs and of those coupled with GOx. Binding of GOx to MNPs by using GA or SA was confirmed by FT-IR spectroscopy. The stability of the immobilized and free enzyme was investigated by measuring the enzymatic activity. The study confirmed that the resulting activity of the immobilized enzyme and the optimization of enzyme immobilization depended on the type of reagent used and duration of the process. The catalytic performance of immobilized enzyme was tested, revealing that the long-term colloidal stability of SA-functionalized MNPs was superior to those prepared with GA. In conclusion, the SA-functionalized bioconjugates have a better potential as compared to the GA-modified nanosystems to be regarded as catalytic nanodevices for biomedical purposes such as biosensors.
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Affiliation(s)
- Alina Gabriela Rusu
- Natural Polymers, Bioactive and Biocompatible Materials Department, Petru Poni Institute of Macromolecular Chemistry, 41A Gr. Ghica–Voda Alley, 700487 Iasi, Romania; (A.P.C.); (L.E.N.); (A.M.S.); (A.C.)
| | - Aurica P. Chiriac
- Natural Polymers, Bioactive and Biocompatible Materials Department, Petru Poni Institute of Macromolecular Chemistry, 41A Gr. Ghica–Voda Alley, 700487 Iasi, Romania; (A.P.C.); (L.E.N.); (A.M.S.); (A.C.)
| | - Loredana Elena Nita
- Natural Polymers, Bioactive and Biocompatible Materials Department, Petru Poni Institute of Macromolecular Chemistry, 41A Gr. Ghica–Voda Alley, 700487 Iasi, Romania; (A.P.C.); (L.E.N.); (A.M.S.); (A.C.)
| | - Vera Balan
- Faculty of Medical Bioengineering, Grigore T. Popa University of Medicine and Pharmacy of Iasi, 700115 Iasi, Romania;
| | - Alexandru Mihail Serban
- Natural Polymers, Bioactive and Biocompatible Materials Department, Petru Poni Institute of Macromolecular Chemistry, 41A Gr. Ghica–Voda Alley, 700487 Iasi, Romania; (A.P.C.); (L.E.N.); (A.M.S.); (A.C.)
| | - Alexandra Croitoriu
- Natural Polymers, Bioactive and Biocompatible Materials Department, Petru Poni Institute of Macromolecular Chemistry, 41A Gr. Ghica–Voda Alley, 700487 Iasi, Romania; (A.P.C.); (L.E.N.); (A.M.S.); (A.C.)
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5
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Characteristics of glucose oxidase immobilized on carbon-encapsulated iron nanoparticles decorated with polyethyleneimine. Polym Bull (Berl) 2022. [DOI: 10.1007/s00289-022-04125-1] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/19/2022]
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6
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Kaur J, Yogalakshmi KN. Degradation of n-hexanoyl homoserine lactone with quorum quenching bacteria immobilised magnetic nanocomposite beads. ENVIRONMENTAL TECHNOLOGY 2022; 43:885-892. [PMID: 32814501 DOI: 10.1080/09593330.2020.1811389] [Citation(s) in RCA: 3] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Received: 12/02/2019] [Accepted: 08/09/2020] [Indexed: 06/11/2023]
Abstract
N-acyl homoserine lactones (AHLs) based quorum sensing controls various phenotype expressions, including biofilm formation, hence its interruption is considered to be an ideal option for membrane biofouling control. Bead entrapped quorum quenching bacteria was reported to be an efficient approach for degradation of signal molecules in recent years. In the present study, we investigated the potential of quorum quenching (QQ) bacteria immobilised magnetic nanocomposite beads (IMN) in degradation of signalling molecule, n-hexanoyl homoserine lactone (C6-HSL). Three QQ bacteria, named Acinetobacter baumannii JYQ2, Pseudomonas nitroreducens JYQ3 and Pseudomonas JYQ4 isolated from dairy industry waste activated sludge (WAS) were immobilised in the magnetic nanocomposite (IMN) beads. The scanning electron microscopy (SEM) of the IMN beads has indicated the successful entrapment of QQ bacteria within the alginate matrix. The GC-MS analysis showed that all the QQ bacteria immobilised magnetic nanocomposite (IMN) beads degraded the signalling molecule, n-hexanoyl homoserine lactone (C6-HSL) within 72 h of incubation. The nanocomposite beads containing the QQ bacteria Pseudomonas JYQ4 showed the maximum degradation percentage of 97 ± 0.13% leaving a residual HSL of 0.7 mg/L. All the other isolates showed C6-HSL degradation percentage in the range of 87% to 95%. The data suggest the potential of C6-HSL degradation by QQ bacteria IMN beads. Hence, the study offers possibilities of controlling biofilm developed on the membrane surface during wastewater treatment processes.
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Affiliation(s)
- Jaskiran Kaur
- Centre for Environmental Sciences and Technology, School of Environment and Earth Sciences, Central University of Punjab, Bathinda, India
| | - K N Yogalakshmi
- Centre for Environmental Sciences and Technology, School of Environment and Earth Sciences, Central University of Punjab, Bathinda, India
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7
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Razzaghi M, Homaei A, Vianello F, Azad T, Sharma T, Nadda AK, Stevanato R, Bilal M, Iqbal HMN. Industrial applications of immobilized nano-biocatalysts. Bioprocess Biosyst Eng 2022; 45:237-256. [PMID: 34596787 DOI: 10.1007/s00449-021-02647-y] [Citation(s) in RCA: 24] [Impact Index Per Article: 8.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 07/07/2021] [Accepted: 09/24/2021] [Indexed: 02/05/2023]
Abstract
Immobilized enzyme-based catalytic constructs could greatly improve various industrial processes due to their extraordinary catalytic activity and reaction specificity. In recent decades, nano-enzymes, defined as enzyme immobilized on nanomaterials, gained popularity for the enzymes' improved stability, reusability, and ease of separation from the biocatalytic process. Thus, enzymes can be strategically incorporated into nanostructured materials to engineer nano-enzymes, such as nanoporous particles, nanofibers, nanoflowers, nanogels, nanomembranes, metal-organic frameworks, multi-walled or single-walled carbon nanotubes, and nanoparticles with tuned shape and size. Surface-area-to-volume ratio, pore-volume, chemical compositions, electrical charge or conductivity of nanomaterials, protein charge, hydrophobicity, and amino acid composition on protein surface play fundamental roles in the nano-enzyme preparation and catalytic properties. With proper understanding, the optimization of the above-mentioned factors will lead to favorable micro-environments for biocatalysts of industrial relevance. Thus, the application of nano-enzymes promise to further strengthen the advances in catalysis, biotransformation, biosensing, and biomarker discovery. Herein, this review article spotlights recent progress in nano-enzyme development and their possible implementation in different areas, including biomedicine, biosensors, bioremediation of industrial pollutants, biofuel production, textile, leather, detergent, food industries and antifouling.
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Affiliation(s)
- Mozhgan Razzaghi
- Department of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, P.O. Box 3995, Bandar Abbas, Iran
| | - Ahmad Homaei
- Department of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, P.O. Box 3995, Bandar Abbas, Iran.
| | - Fabio Vianello
- Department of Comparative Biomedicine and Food Science, University of Padova, Legnaro, PD, Italy
| | - Taha Azad
- Ottawa Hospital Research Institute, Ottawa, ON, K1H 8L6, Canada
- Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON, K1H 8M5, Canada
| | - Tanvi Sharma
- Department of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Solan, Waknaghat, India
| | - Ashok Kumar Nadda
- Department of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Solan, Waknaghat, India
| | - Roberto Stevanato
- Department of Molecular Sciences and Nanosystems, University Ca' Foscari of Venice, Venice, Italy
| | - Muhammad Bilal
- School of Life Science and Food Engineering, Huaiyin Institute of Technology, Huaian, 223003, China
| | - Hafiz M N Iqbal
- School of Engineering and Sciences, Tecnologico de Monterrey, 64849, Monterrey, Mexico
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8
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Zhai M, Gong P, Li H, Peng J, Xu W, Song S, Liu X, Liu J, Liu J, Liu Z. Metastable interface biomimetic synthesis of a smart nanosystem for enhanced starvation/gas therapy. J Colloid Interface Sci 2021; 599:149-157. [PMID: 33940438 DOI: 10.1016/j.jcis.2021.04.042] [Citation(s) in RCA: 15] [Impact Index Per Article: 3.8] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 01/22/2021] [Revised: 03/26/2021] [Accepted: 04/09/2021] [Indexed: 12/12/2022]
Abstract
Glucose oxidase (GOx)-mediated starvation therapy holds great promise in cancer treatment. However, the worse hypoxia conditions result into low therapeutic efficiency, and undegradability of carriers poses potential threats to living bodies. To address this, herein a bioinspired MnO2 nanosystem with controllable surface was developed for highly efficient starvation/gas synergistic enhanced therapy. Biomimetic design and further surface modification unprecedentedly endowed the nanosystem with ultrahigh loading capacity for GOx and l-Arginine (l-Arg) and special selectivity toward cancer cells. Especially, the dissipative O2 during starvation therapy was well replenished by a positive cycle formed by the nanosystem, which continuously reproduced O2 and accelerated glucose consumption. The abundant H2O2 was further used to oxidize l-Arg into nitric oxide to realize gas therapy. In vitro and in vivo testing confirmed that this new treatment effectively blocked the nutrition and energy sources of cells to obtain excellent therapeutic effect. We reported the first experimental item of this nanosystem for inhibiting cancer cell migration. Considering the novel design concept with facile biomimetic methods, effective co-loading of endogenous substances, and good anti-tumor and anti-migration effects, this work provided new theoretical and experimental basis for starvation therapy and inspired people to design more delicate platform for cancer treatment.
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Affiliation(s)
- Mingzhu Zhai
- The Key Laboratory of Life-Organic Analysis, School of Chemistry and Chemical Engineering, Qufu Normal University, Qufu 273165, PR China
| | - Peiwei Gong
- The Key Laboratory of Life-Organic Analysis, School of Chemistry and Chemical Engineering, Qufu Normal University, Qufu 273165, PR China; State Key Laboratory of Solidification Processing, Center of Advanced Lubrication, and Seal Materials, Northwestern Polytechnical University, 517, Xi'an 710072, PR China.
| | - Hui Li
- The Key Laboratory of Life-Organic Analysis, School of Chemistry and Chemical Engineering, Qufu Normal University, Qufu 273165, PR China
| | - Jingyi Peng
- The Key Laboratory of Life-Organic Analysis, School of Chemistry and Chemical Engineering, Qufu Normal University, Qufu 273165, PR China
| | - Wenyu Xu
- The Key Laboratory of Life-Organic Analysis, School of Chemistry and Chemical Engineering, Qufu Normal University, Qufu 273165, PR China
| | - Shaohua Song
- The Key Laboratory of Life-Organic Analysis, School of Chemistry and Chemical Engineering, Qufu Normal University, Qufu 273165, PR China
| | - Xicheng Liu
- The Key Laboratory of Life-Organic Analysis, School of Chemistry and Chemical Engineering, Qufu Normal University, Qufu 273165, PR China
| | - Jianxi Liu
- State Key Laboratory of Solidification Processing, Center of Advanced Lubrication, and Seal Materials, Northwestern Polytechnical University, 517, Xi'an 710072, PR China.
| | - Jinfeng Liu
- The Key Laboratory of Life-Organic Analysis, School of Chemistry and Chemical Engineering, Qufu Normal University, Qufu 273165, PR China
| | - Zhe Liu
- The Key Laboratory of Life-Organic Analysis, School of Chemistry and Chemical Engineering, Qufu Normal University, Qufu 273165, PR China.
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González-Díaz CA, Golberg A. Sensitivity analysis of electrical bioimpedance patterns of breast cancer cells labeled with magnetic nanoparticles: forming the foundation for a biosensor of circulating tumor cells. Physiol Meas 2020; 41:064001. [DOI: 10.1088/1361-6579/ab9377] [Citation(s) in RCA: 3] [Impact Index Per Article: 0.6] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/29/2022]
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10
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Long J, Pan T, Xie Z, Xu X, Jin Z. Co-immobilization of β-fructofuranosidase and glucose oxidase improves the stability of Bi-enzymes and the production of lactosucrose. Lebensm Wiss Technol 2020. [DOI: 10.1016/j.lwt.2020.109460] [Citation(s) in RCA: 15] [Impact Index Per Article: 3.0] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/21/2022]
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11
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Doraiswamy N, Sarathi M, Pennathur G. Improvement in biochemical characteristics of cross-linked enzyme aggregates (CLEAs) with magnetic nanoparticles as support matrix. Methods Enzymol 2020; 630:133-158. [PMID: 31931983 DOI: 10.1016/bs.mie.2019.10.019] [Citation(s) in RCA: 2] [Impact Index Per Article: 0.4] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 04/05/2023]
Abstract
Recent developments in novel carriers for enzyme immobilization have led to improvement in the stability and cost-effectiveness of the biocatalysts for their enhanced suitability in the industrial applications. Cross-linked enzyme aggregates (CLEAs), a recent technique developed in the carrier-free type of enzyme immobilization is a simple and straightforward method. Moreover, the magnetic property and the higher surface-to-volume ratio of the maghemite nanoparticles have also been utilized in the present immobilization technique as magnetic nanoparticle-supported CLEAs (Mgnp-CLEAs). The stability studies of the free and immobilized enzyme revealed the Mgnp-CLEAs to have enhanced enzyme stability with an increase in the reusability cycle. The physical characterization of the nanoparticles and immobilized enzymes by the Scanning Electron Microscopy (SEM), Fourier-Transform Infrared spectroscopy (FT-IR) and X-ray diffraction analysis (XRD) showed the successful immobilization of the enzyme for its improved stability.
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Affiliation(s)
| | | | - Gautam Pennathur
- Centre for Biotechnology, Anna University, Chennai, Tamil Nadu, India; AU-KBC Research Centre, Anna University, Chennai, Tamil Nadu, India.
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12
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Sasya M, Devi KSS, Babu JK, Balaguru Rayappan JB, Krishnan UM. Metabolic Syndrome-An Emerging Constellation of Risk Factors: Electrochemical Detection Strategies. SENSORS (BASEL, SWITZERLAND) 2019; 20:E103. [PMID: 31878023 PMCID: PMC6982738 DOI: 10.3390/s20010103] [Citation(s) in RCA: 6] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Abstract] [Key Words] [Grants] [Track Full Text] [Download PDF] [Figures] [Subscribe] [Scholar Register] [Received: 10/15/2019] [Revised: 11/15/2019] [Accepted: 12/11/2019] [Indexed: 02/07/2023]
Abstract
Metabolic syndrome is a condition that results from dysfunction of different metabolic pathways leading to increased risk of disorders such as hyperglycemia, atherosclerosis, cardiovascular diseases, cancer, neurodegenerative disorders etc. As this condition cannot be diagnosed based on a single marker, multiple markers need to be detected and quantified to assess the risk facing an individual of metabolic syndrome. In this context, chemical- and bio-sensors capable of detecting multiple analytes may provide an appropriate diagnostic strategy. Research in this field has resulted in the evolution of sensors from the first generation to a fourth generation of 'smart' sensors. A shift in the sensing paradigm involving the sensing element and transduction strategy has also resulted in remarkable advancements in biomedical diagnostics particularly in terms of higher sensitivity and selectivity towards analyte molecule and rapid response time. This review encapsulates the significant advancements reported so far in the field of sensors developed for biomarkers of metabolic syndrome.
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Affiliation(s)
- Madhurantakam Sasya
- Department of Molecular Physiology, School of Medicine, Niigata University, Niigata-9518510, Japan;
- Centre for Nanotechnology & Advanced Biomaterials (CeNTAB), SASTRA Deemed-to-be University, Thanjavur 613401, India; (K.S.S.D.); (J.K.B.); (J.B.B.R.)
- School of Chemical & Biotechnology, SASTRA Deemed-to-be University, Thanjavur 613401, India
| | - K. S. Shalini Devi
- Centre for Nanotechnology & Advanced Biomaterials (CeNTAB), SASTRA Deemed-to-be University, Thanjavur 613401, India; (K.S.S.D.); (J.K.B.); (J.B.B.R.)
- School of Chemical & Biotechnology, SASTRA Deemed-to-be University, Thanjavur 613401, India
| | - Jayanth K. Babu
- Centre for Nanotechnology & Advanced Biomaterials (CeNTAB), SASTRA Deemed-to-be University, Thanjavur 613401, India; (K.S.S.D.); (J.K.B.); (J.B.B.R.)
- School of Electrical & Electronics Engineering, SASTRA Deemed-to-be University, Thanjavur 613401, India
| | - John Bosco Balaguru Rayappan
- Centre for Nanotechnology & Advanced Biomaterials (CeNTAB), SASTRA Deemed-to-be University, Thanjavur 613401, India; (K.S.S.D.); (J.K.B.); (J.B.B.R.)
- School of Electrical & Electronics Engineering, SASTRA Deemed-to-be University, Thanjavur 613401, India
| | - Uma Maheswari Krishnan
- Department of Molecular Physiology, School of Medicine, Niigata University, Niigata-9518510, Japan;
- School of Chemical & Biotechnology, SASTRA Deemed-to-be University, Thanjavur 613401, India
- School of Arts, Science & Humanities, SASTRA Deemed-to-be University, Thanjavur 613401, India
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Abstract
We report the preparation, characterization and application of a novel magnetic four-enzyme nanobiocatalyst prepared by the simultaneous covalent co-immobilization of cellulase (CelDZ1), β-glucosidase (bgl), glucose oxidase (GOx) and horseradish peroxidase (HRP) onto the surface of amino-functionalized magnetic nanoparticles (MNPs). This nanobiocatalyst was characterized by various spectroscopic techniques. The co-immobilization process yielded maximum recovered enzymatic activity (CelDZ1: 42%, bgl: 66%, GOx: 94% and HRP: 78%) at a 10% v/v cross-linker concentration, after 2 h incubation time and at 1:1 mass ratio of MNPs to total enzyme content. The immobilization process leads to an increase of Km and a decrease of Vmax values of co-immobilized enzymes. The thermal stability studies of the co-immobilized enzymes indicated up to 2-fold increase in half-life time constants and up to 1.5-fold increase in their deactivation energies compared to the native enzymes. The enhanced thermodynamic parameters of the four-enzyme co-immobilized MNPs also suggested increment in their thermal stability. Furthermore, the co-immobilized enzymes retained a significant part of their activity (up to 50%) after 5 reaction cycles at 50 °C and remained active even after 24 d of incubation at 5 °C. The nanobiocatalyst was successfully applied in a four-step cascade reaction involving the hydrolysis of cellulose.
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14
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Zhong Y, Gong WJ, Gao XH, Li YN, Liu K, Hu YG, Qi JS. Synthesis and evaluation of a novel nanoparticle carrying urokinase used in targeted thrombolysis. J Biomed Mater Res A 2019; 108:193-200. [DOI: 10.1002/jbm.a.36803] [Citation(s) in RCA: 4] [Impact Index Per Article: 0.7] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 02/04/2019] [Revised: 06/05/2019] [Accepted: 09/16/2019] [Indexed: 01/30/2023]
Affiliation(s)
- Yan Zhong
- Department of Biochemistry Hebei Medical University Shijiazhuang China
| | - Wen J. Gong
- Department of Biochemistry Hebei Medical University Shijiazhuang China
| | - Xue H. Gao
- Department of Biochemistry Hebei Medical University Shijiazhuang China
| | - Yan N. Li
- Department of Biochemistry Hebei Medical University Shijiazhuang China
| | - Kun Liu
- Department of Biochemistry Hebei Medical University Shijiazhuang China
| | - Yong G. Hu
- State Key Laboratory of Agricultural Microbiology Huazhong Agricultural University Wuhan China
| | - Jin S. Qi
- Department of Biochemistry Hebei Medical University Shijiazhuang China
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15
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Song Y, Wang C. High-power biofuel cells based on three-dimensional reduced graphene oxide/carbon nanotube micro-arrays. MICROSYSTEMS & NANOENGINEERING 2019; 5:46. [PMID: 31636935 PMCID: PMC6799826 DOI: 10.1038/s41378-019-0081-2] [Citation(s) in RCA: 11] [Impact Index Per Article: 1.8] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Subscribe] [Scholar Register] [Received: 03/16/2019] [Revised: 06/05/2019] [Accepted: 06/20/2019] [Indexed: 06/01/2023]
Abstract
Miniaturized enzymatic biofuel cells (EBFCs) with high cell performance are promising candidates for powering next-generation implantable medical devices. Here, we report a closed-loop theoretical and experimental study on a micro EBFC system based on three-dimensional (3D) carbon micropillar arrays coated with reduced graphene oxide (rGO), carbon nanotubes (CNTs), and a biocatalyst composite. The fabrication process of this system combines the top-down carbon microelectromechanical systems (C-MEMS) technique to fabricate the 3D micropillar array platform and bottom-up electrophoretic deposition (EPD) to deposit the reduced rGO/CNTs/enzyme onto the electrode surface. The Michaelis-Menten constant KM of 2.1 mM for glucose oxidase (GOx) on the rGO/CNTs/GOx bioanode was obtained, which is close to the KM for free GOx. Theoretical modelling of the rGO/CNT-based EBFC system via finite element analysis was conducted to predict the cell performance and efficiency. The experimental results from the developed rGO/CNT-based EBFC showed a maximum power density of 196.04 µW cm-2 at 0.61 V, which is approximately twice the maximum power density obtained from the rGO-based EBFC. The experimental power density is noted to be 71.1% of the theoretical value.
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Affiliation(s)
- Yin Song
- Department of Mechanical and Materials Science Engineering, Florida International University, 10555 West Flagler Street, Miami, FL 33174 USA
| | - Chunlei Wang
- Department of Mechanical and Materials Science Engineering, Florida International University, 10555 West Flagler Street, Miami, FL 33174 USA
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Huerta-Nuñez LFE, Gutierrez-Iglesias G, Martinez-Cuazitl A, Mata-Miranda MM, Alvarez-Jiménez VD, Sánchez-Monroy V, Golberg A, González-Díaz CA. A biosensor capable of identifying low quantities of breast cancer cells by electrical impedance spectroscopy. Sci Rep 2019; 9:6419. [PMID: 31015522 PMCID: PMC6478841 DOI: 10.1038/s41598-019-42776-9] [Citation(s) in RCA: 34] [Impact Index Per Article: 5.7] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/30/2018] [Accepted: 03/28/2019] [Indexed: 12/29/2022] Open
Abstract
Breast cancer (BC) is a malignant disease with a high prevalence worldwide. The main cause of death is not the primary tumor, but instead the spread of tumor cells to distant sites. The aim of the present study was to examine a new method for the detection of cancer cells in aqueous medium using bioimpedance spectroscopy assisted with magnetic nanoparticles (MNP's) exposure to a constant magnetic field. The spectroscopic patterns were identified for three breast cancer cell lines. Each BC cell line represents a different pathologic stage: the early stage (MCF-7), invasive phase (MDA-MB-231) and metastasis (SK-BR-3). For this purpose, bioimpedance measurements were carried out at a certain frequency range with the aid of nanoprobes, consisting of magnetic nanoparticles (MNPs) coupled to a monoclonal antibody. The antibody was specific for the predominant cell surface protein for each cell line, which was identified by using RT-qPCR and flow cytometry. Accordingly, EpCAM corresponds to MCF-7, MUC-1 to MDA-MB-231, and HER-2 to SK-BR-3. Despite their low concentrations, BC cells could be detected by impedance spectroscopy. Hence, this methodology should permit the monitoring of circulating tumor cells (CTC) and therefore help to prevent recurrences and metastatic processes during BC treatment.
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Affiliation(s)
- L F E Huerta-Nuñez
- Escuela Militar de Graduados de Sanidad-Universidad del Ejército y Fuerza Aérea, México City, Mexico
- Escuela Superior de Medicina-Instituto Politécnico Nacional, México City, Mexico
| | - G Gutierrez-Iglesias
- Escuela Superior de Medicina-Instituto Politécnico Nacional, México City, Mexico
| | - A Martinez-Cuazitl
- Escuela Militar de Medicina-Universidad del Ejército y Fuerza Aérea, México City, Mexico
| | - M M Mata-Miranda
- Escuela Militar de Medicina-Universidad del Ejército y Fuerza Aérea, México City, Mexico
| | | | - V Sánchez-Monroy
- Escuela Nacional de Medicina y Homeopatía-Instituto Politécnico Nacional, México City, Mexico
| | - Alexander Golberg
- Porter School of Environmental and Earth Sciences, Tel Aviv University, Tel Aviv-Yafo, Israel
| | - C A González-Díaz
- Escuela Superior de Medicina-Instituto Politécnico Nacional, México City, Mexico.
- Porter School of Environmental and Earth Sciences, Tel Aviv University, Tel Aviv-Yafo, Israel.
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Xu Y, Fei J, Li G, Yuan T, Xu X, Li J. Nanozyme‐Catalyzed Cascade Reactions for Mitochondria‐Mimicking Oxidative Phosphorylation. Angew Chem Int Ed Engl 2019. [DOI: 10.1002/ange.201813771] [Citation(s) in RCA: 9] [Impact Index Per Article: 1.5] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/15/2022]
Affiliation(s)
- Youqian Xu
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
- University of Chinese Academy of Sciences Beijing 100049 China
| | - Jinbo Fei
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
| | - Guangle Li
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
- University of Chinese Academy of Sciences Beijing 100049 China
| | - Tingting Yuan
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
- University of Chinese Academy of Sciences Beijing 100049 China
| | - Xia Xu
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
- University of Chinese Academy of Sciences Beijing 100049 China
| | - Junbai Li
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
- University of Chinese Academy of Sciences Beijing 100049 China
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18
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Xu Y, Fei J, Li G, Yuan T, Xu X, Li J. Nanozyme‐Catalyzed Cascade Reactions for Mitochondria‐Mimicking Oxidative Phosphorylation. Angew Chem Int Ed Engl 2019; 58:5572-5576. [DOI: 10.1002/anie.201813771] [Citation(s) in RCA: 68] [Impact Index Per Article: 11.3] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/04/2018] [Indexed: 01/09/2023]
Affiliation(s)
- Youqian Xu
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
- University of Chinese Academy of Sciences Beijing 100049 China
| | - Jinbo Fei
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
| | - Guangle Li
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
- University of Chinese Academy of Sciences Beijing 100049 China
| | - Tingting Yuan
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
- University of Chinese Academy of Sciences Beijing 100049 China
| | - Xia Xu
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
- University of Chinese Academy of Sciences Beijing 100049 China
| | - Junbai Li
- Beijing National Laboratory for Molecular Sciences (BNLMS)CAS Key Lab of ColloidInterface and Chemical ThermodynamicsInstitute of ChemistryChinese Academy of Sciences Beijing 100190 China
- University of Chinese Academy of Sciences Beijing 100049 China
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Shawky SM, Awad AM, Abugable AA, El-Khamisy SF. Gold nanoparticles - an optical biosensor for RNA quantification for cancer and neurologic disorders diagnosis. Int J Nanomedicine 2018; 13:8137-8151. [PMID: 30555231 PMCID: PMC6278840 DOI: 10.2147/ijn.s181732] [Citation(s) in RCA: 10] [Impact Index Per Article: 1.4] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/23/2022] Open
Abstract
Purpose The objective of this study is to develop a facile tool for the absolute detection and quantification of nucleic acid transcripts, using a gold nanoparticle-based optical biosensor. Topoisomerase 1 (TOP1) and tyrosyl DNA phosphodiesterase 2 (TDP2) were among the nucleic acid transcripts of choice due to their role as genomic instability biomarkers and their implication in various cancers and neurologic disorders. This opens the door to develop a simple tool that can be used for diagnosing and monitoring treatment response for such diseases, overcoming the requirements for high cost, time, and complexity of the existing technologies for the absolute quantification of transcripts of interest. Materials and methods The TOP1 and TDP2 mRNA transcripts were first captured specifically using magnetic nanoparticles that were functionalized with TOP1- and TDP2-specific probes, respectively. The captured mRNA was then directly detected and quantified using the gold aggregating gold (GAG) assay, without the need for amplification as in existing technologies used for the quantification of transcripts. Results A linear correlation exists between the GAG assay and the qPCR for the quantification of the TOP1 and TDP2 mRNA transcripts (101–104 copies). The detection limit of the GAG assay in mRNA quantification was up to 10 copies per reaction. Wild-type and TDP2-deficient cell lines confirmed the assay specificity and reproducibility in distinguishing between different transcripts. Conclusion The GAG assay can be utilized as an inexpensive, rapid, simple, and sensitive tool for the absolute quantification of RNA for different applications, instead of the laborious, expensive, and sophisticated real-time PCR.
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Affiliation(s)
- Sherif M Shawky
- Center for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt, .,Krebs Institute, Department of Molecular Biology and Biotechnology, Firth Court, University of Sheffield, Sheffield, UK, .,Biochemistry Department, Faculty of Pharmacy, Misr University for Science and Technology, Giza, Egypt
| | - Ahmed M Awad
- Center for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt, .,Department of Molecular Biology, Genetic Engineering and Biotechnology Research Institute, University of Sadat City, Sadat City, Egypt
| | - Arwa A Abugable
- Center for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt, .,Krebs Institute, Department of Molecular Biology and Biotechnology, Firth Court, University of Sheffield, Sheffield, UK,
| | - Sherif F El-Khamisy
- Center for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt, .,Krebs Institute, Department of Molecular Biology and Biotechnology, Firth Court, University of Sheffield, Sheffield, UK,
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Ultrasound assisted synthesis of guar gum-zero valent iron nanocomposites as a novel catalyst for the treatment of pollutants. Carbohydr Polym 2018; 199:41-50. [DOI: 10.1016/j.carbpol.2018.06.097] [Citation(s) in RCA: 28] [Impact Index Per Article: 4.0] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 02/07/2018] [Revised: 06/20/2018] [Accepted: 06/21/2018] [Indexed: 12/18/2022]
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Park HJ, Driscoll AJ, Johnson PA. The development and evaluation of β-glucosidase immobilized magnetic nanoparticles as recoverable biocatalysts. Biochem Eng J 2018. [DOI: 10.1016/j.bej.2018.01.017] [Citation(s) in RCA: 23] [Impact Index Per Article: 3.3] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/30/2022]
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Nikitin AA, Shchetinin IV, Tabachkova NY, Soldatov MA, Soldatov AV, Sviridenkova NV, Beloglazkina EK, Savchenko AG, Fedorova ND, Abakumov MA, Majouga AG. Synthesis of Iron Oxide Nanoclusters by Thermal Decomposition. LANGMUIR : THE ACS JOURNAL OF SURFACES AND COLLOIDS 2018; 34:4640-4650. [PMID: 29566327 DOI: 10.1021/acs.langmuir.8b00753] [Citation(s) in RCA: 16] [Impact Index Per Article: 2.3] [Reference Citation Analysis] [Abstract] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 05/17/2023]
Abstract
Herein, we report a novel one-step solvothermal synthesis of magnetite nanoclusters (MNCs). In this report, we discuss the synthesis, structure, and properties of MNCs and contrast enhancement in T2-weighted MR images using magnetite nanoclusters. The effect of different organic acids, used as surfactants, on the size and shape of MNCs was investigated. The structure and properties of samples were determined by magnetic measurements, TGA, TEM, HRTEM, XRD, FTIR, and MRI. Magnetic measurements show that obtained MNCs have relatively high saturation magnetization values (65.1-81.5 emu/g) and dependence of the coercive force on the average size of MNCs was established. MNCs were transferred into an aqueous medium by Pluronic F-127, and T2-relaxivity values were determined. T2-Weighted MR phantom images clearly demonstrated that such magnetite nanoclusters can be used as contrast agents for MRI.
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Affiliation(s)
- Aleksey A Nikitin
- National University of Science and Technology "MISIS" , Leninskiy prospect 4 , 119991 Moscow , Russian Federation
- Department of Chemistry , Lomonosov Moscow State University , Leninskiye gory 1-3, GSP-1 , 119991 Moscow , Russian Federation
| | - Igor V Shchetinin
- National University of Science and Technology "MISIS" , Leninskiy prospect 4 , 119991 Moscow , Russian Federation
| | - Natalya Yu Tabachkova
- National University of Science and Technology "MISIS" , Leninskiy prospect 4 , 119991 Moscow , Russian Federation
| | - Mikhail A Soldatov
- Southern Federal University , Bolshaya Sadovaya st., 105 , 344006 Rostov-on-Don , Russian Federation
| | - Alexander V Soldatov
- Southern Federal University , Bolshaya Sadovaya st., 105 , 344006 Rostov-on-Don , Russian Federation
| | - Natalya V Sviridenkova
- National University of Science and Technology "MISIS" , Leninskiy prospect 4 , 119991 Moscow , Russian Federation
| | - Elena K Beloglazkina
- Department of Chemistry , Lomonosov Moscow State University , Leninskiye gory 1-3, GSP-1 , 119991 Moscow , Russian Federation
| | - Alexander G Savchenko
- National University of Science and Technology "MISIS" , Leninskiy prospect 4 , 119991 Moscow , Russian Federation
| | - Natalya D Fedorova
- National University of Science and Technology "MISIS" , Leninskiy prospect 4 , 119991 Moscow , Russian Federation
| | - Maxim A Abakumov
- Department of Chemistry , Lomonosov Moscow State University , Leninskiye gory 1-3, GSP-1 , 119991 Moscow , Russian Federation
- The Russian National Research Medical University , Ostrovityanova 1 , 117997 Moscow , Russian Federation
| | - Alexander G Majouga
- National University of Science and Technology "MISIS" , Leninskiy prospect 4 , 119991 Moscow , Russian Federation
- Department of Chemistry , Lomonosov Moscow State University , Leninskiye gory 1-3, GSP-1 , 119991 Moscow , Russian Federation
- Dmitry Mendeleev University of Chemical Technology of Russia , Miusskaya 9 , 125047 Moscow , Russian Federation
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Mehta R. Synthesis of magnetic nanoparticles and their dispersions with special reference to applications in biomedicine and biotechnology. MATERIALS SCIENCE & ENGINEERING. C, MATERIALS FOR BIOLOGICAL APPLICATIONS 2017. [DOI: 10.1016/j.msec.2017.05.135] [Citation(s) in RCA: 48] [Impact Index Per Article: 6.0] [Reference Citation Analysis] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/25/2023]
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Klekotka U, Rogowska M, Satuła D, Kalska-Szostko B. Characterization of ferrite nanoparticles for preparation of biocomposites. BEILSTEIN JOURNAL OF NANOTECHNOLOGY 2017; 8:1257-1265. [PMID: 28685126 PMCID: PMC5480339 DOI: 10.3762/bjnano.8.127] [Citation(s) in RCA: 6] [Impact Index Per Article: 0.8] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Figures] [Subscribe] [Scholar Register] [Received: 12/09/2016] [Accepted: 04/07/2017] [Indexed: 06/07/2023]
Abstract
Ferrite nanoparticles with nominal composition Me0.5Fe2.5O4 (Me = Co, Fe, Ni or Mn) have been successfully prepared by the wet chemical method. The obtained particles have a mean diameter of 11-16 ± 2 nm and were modified to improve their magnetic properties and chemical activity. The surface of the pristine nanoparticles was functionalized afterwards with -COOH and -NH2 groups to obtain a bioactive layer. To achieve our goal, two different modification approaches were realized. In the first one, glutaraldehyde was attached to the nanoparticles as a linker. In the second one, direct bonding of such nanoparticles with a bioparticle was studied. In subsequent steps, the nanoparticles were immobilized with enzymes such as albumin, glucose oxidase, lipase and trypsin as a test bioparticles. The characterization of the nanoparticles was acheived by transmission electron microscopy, X-ray diffraction, energy dispersive X-ray and Mössbauer spectroscopy. The effect of the obtained biocomposites was monitored by Fourier transform infrared spectroscopy. The obtained results show that in some cases the use of glutaraldehyde was crucial (albumin).
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Affiliation(s)
- Urszula Klekotka
- Institute of Chemistry, University of Bialystok, Ciołkowskiego 1K, 15-245 Bialystok, Poland
| | - Magdalena Rogowska
- Institute of Chemistry, University of Bialystok, Ciołkowskiego 1K, 15-245 Bialystok, Poland
| | - Dariusz Satuła
- Faculty of Physics, University of Bialystok, Ciołkowskiego 1L, 15-245 Bialystok, Poland
| | - Beata Kalska-Szostko
- Institute of Chemistry, University of Bialystok, Ciołkowskiego 1K, 15-245 Bialystok, Poland
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Vranish JN, Ancona MG, Oh E, Susumu K, Medintz IL. Enhancing coupled enzymatic activity by conjugating one enzyme to a nanoparticle. NANOSCALE 2017; 9:5172-5187. [PMID: 28393943 DOI: 10.1039/c7nr00200a] [Citation(s) in RCA: 22] [Impact Index Per Article: 2.8] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 05/04/2023]
Abstract
Enzymes have long been a prime research target for the commercial production of commodity and specialty chemicals, design of sensing devices, and the development of therapeutics and new chemical processes. Industrial applications for enzymes can potentially be enhanced by enzyme immobilization which often allows for increased enzyme stability, facile product purification, and minimized substrate diffusion times in multienzymatic cascades, but this is usually at the cost of a significant decrease in catalytic rates. Recently, enzyme immobilization has been advanced by the discovery that nanoparticle surfaces are frequently able to enhance the activity of the bound enzyme. Here we extend this observation to a multienzymatic coupled system using semiconductor quantum dots (QDs) as a model nanoparticle material and the prototypical enzyme pair of glucose oxidase (GOX) and horseradish peroxidase (HRP). We first demonstrate that HRP binding to QDs has a significant beneficial effect on enzymatic activity, producing a >2-fold improvement in kcat. We argue that this enhancement is due to affinity of the QD surface for the substrate. Furthermore, we demonstrate that when the ratio of GOX to HRP is adjusted to allow HRP to be the rate-limiting step of the pathway, the QD-induced rate enhancement of HRP can be maintained in a multi-enzyme cascade. Kinetic analysis shows that the underlying processes can be simulated numerically and provide insight into the governing mechanisms. The potential of nanoparticle-based catalytic enhancement is then discussed in the context of multienzyme cascades and synthetic biology.
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Papain-functionalized gold nanoparticles as heterogeneous biocatalyst for bioanalysis and biopharmaceuticals analysis. Anal Chim Acta 2017; 963:33-43. [PMID: 28335973 DOI: 10.1016/j.aca.2017.02.009] [Citation(s) in RCA: 18] [Impact Index Per Article: 2.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/05/2016] [Revised: 02/06/2017] [Accepted: 02/09/2017] [Indexed: 01/30/2023]
Abstract
Surface-modified gold nanoparticles (GNPs) were synthesized via layer-by-layer process with alternating cationic polyallylamine and anionic poly(acrylic acid) polyelectrolyte layers leading to a highly hydrophilic biocompatible shell supporting colloidal stability. Afterwards, papain was covalently immobilized on the modified GNPs via amide coupling between the amino groups on papain and the terminal carboxylic groups of the modified GNPs by using N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide and N-hydroxysulfosuccinimide sodium as coupling agents. The resultant papain-functionalized gold nanoparticles were characterized by surface plasmon resonance, dynamic light scattering and zeta potential measurements. The new technology resonant mass measurement was applied for determining the average number of papain molecules immobilized per GNP by measurement of the single nanoparticle buoyant mass in the range of femtograms. The activity of the immobilized enzyme was estimated by determination of the kinetic parameters (Km, Vmax and kcat) with the standard chromogenic substrate Nα-benzoyl-dl-arginine-4-nitroanilide hydrochloride. It was found that Km of immobilized and free enzyme are in the same order of magnitude. On contrary, turnover numbers kcat were significantly higher for GNP-conjugated papain. Further, the gold nanobiocatalyst was applied for digestion of polyclonal human immunoglobulin G to yield protein fragments. The resultant fragment mixture was further analyzed by high-performance liquid chromatography-microelectrospray ionization-quadrupole-time-of-flight mass spectrometry, which demonstrated the applicability of the bioreactor based on papain functionalized GNPs. The immobilized papain not only has higher catalytic activity and better stability, but also can be easily isolated from the reaction medium by straightforward centrifugation steps for reuse.
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28
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An overview of holocellulose-degrading enzyme immobilization for use in bioethanol production. ACTA ACUST UNITED AC 2016. [DOI: 10.1016/j.molcatb.2016.08.006] [Citation(s) in RCA: 28] [Impact Index Per Article: 3.1] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/23/2022]
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Selvam K, Govarthanan M, Senbagam D, Kamala-Kannan S, Senthilkumar B, Selvankumar T. Activity and stability of bacterial cellulase immobilized on magnetic nanoparticles. CHINESE JOURNAL OF CATALYSIS 2016. [DOI: 10.1016/s1872-2067(16)62487-7] [Citation(s) in RCA: 13] [Impact Index Per Article: 1.4] [Reference Citation Analysis] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 10/20/2022]
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30
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Diffusion, adsorption and reaction of glucose in glucose oxidase enzyme immobilized mesoporous silica (SBA-15) particles: Experiments and modeling. Biochem Eng J 2016. [DOI: 10.1016/j.bej.2015.10.011] [Citation(s) in RCA: 20] [Impact Index Per Article: 2.2] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/23/2022]
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31
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Khan AY, Noronha SB, Bandyopadhyaya R. Superior performance of a carbon-paste electrode based glucose biosensor containing glucose oxidase enzyme in mesoporous silica powder. ADV POWDER TECHNOL 2016. [DOI: 10.1016/j.apt.2015.11.003] [Citation(s) in RCA: 13] [Impact Index Per Article: 1.4] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/25/2022]
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Rudakovskaya PG, Beloglazkina EK, Majouga AG, Klyachko NL, Kabanov AV, Zyk NV. Synthesis of magnetite-gold nanoparticles with core-shell structure. ACTA ACUST UNITED AC 2015. [DOI: 10.3103/s0027131415030104] [Citation(s) in RCA: 9] [Impact Index Per Article: 0.9] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/30/2022]
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Modulatory Effect of Citrate Reduced Gold and Biosynthesized Silver Nanoparticles on α-Amylase Activity. ACTA ACUST UNITED AC 2015. [DOI: 10.1155/2015/829718] [Citation(s) in RCA: 12] [Impact Index Per Article: 1.2] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/17/2022]
Abstract
Amylase is one of the important digestive enzymes involved in hydrolysis of starch. In this paper, we describe a novel approach to study the interaction of amylase enzyme with gold nanoparticles (AuNPs) and silver nanoparticles (AgNPs) and checked its catalytic function. AuNPs are synthesized using citrate reduction method and AgNPs were synthesized using biological route employing Ficus benghalensis and Ficus religiosa leaf extract as a reducing and stabilizing agent to reduce silver nitrate to silver atoms. A modulatory effect of nanoparticles on amylase activity was observed. Gold nanoparticles are excellent biocompatible surfaces for the immobilization of enzymes. Immobilized amylase showed 1- to 2-fold increase of activity compared to free enzyme. The biocatalytic activity of amylase in the bioconjugate was marginally enhanced relative to the free enzyme in solution. The bioconjugate material also showed significantly enhanced pH and temperature stability. The results indicate that the present study paves way for the modulator degradation of starch by the enzyme with AuNPs and biogenic AgNPs, which is a promising application in the medical and food industry.
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Eissa S, Azzazy HME, Matboli M, Shawky SM, Said H, Anous FA. The prognostic value of histidine-rich glycoprotein RNA in breast tissue using unmodified gold nanoparticles assay. Appl Biochem Biotechnol 2015; 174:751-61. [PMID: 25091325 DOI: 10.1007/s12010-014-1085-x] [Citation(s) in RCA: 5] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Abstract] [MESH Headings] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/28/2022]
Abstract
The aim of is this study is to explore the role of tissue histidine-rich glycoprotein (HRG) RNA as a promising clinically useful biomarker for breast cancer patients prognosis using nanogold assay. Expression of the HRG RNA was assessed by gold nanoparticles and conventional RT-PCR after purification by magnetic nanoparticles in breast tissue samples. The study included 120 patients, 60 of which were histologically proven breast carcinoma cases, 30 had benign breast lesions and 30 were healthy individuals who had undergone reductive plastic surgery. ER, PR and HER2 status were also investigated. The prognostic significance of tissue HRG RNA expression in breast cancer was explored. The magnetic nanoparticles coated with specific thiol modified oligonucleotide probe were used successfully in purification of HRG RNA from breast tissue total RNAs with satisfactory yield. The developed HRG AuNPs assay had a sensitivity and a specificity of 90 %, and a detection limit of 1.5 nmol/l. The concordance rate between the HRG AuNPs assay with RT-PCR after RNA purification using magnetic nanoparticles was 93.3 %. The median follow-up period was 60 months. Among traditional prognostic biomarkers, HRG was a significant independent prognostic marker in relapse-free survival (RFS). HRG RNA is an independent prognostic marker for breast cancer and can be detected using gold NPs assay, which is rapid, sensitive, specific, inexpensive to extend the value for breast cancer prognosis.
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Affiliation(s)
- Sanaa Eissa
- Oncology Diagnostic Unit, Medical Biochemistry and Molecular biology Department, Faculty of Medicine, Ain Shams University, P.O. Box 11381, Abbassia, Cairo, Egypt,
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Glucose oxidase enzyme immobilized porous silica for improved performance of a glucose biosensor. Biochem Eng J 2014. [DOI: 10.1016/j.bej.2014.07.011] [Citation(s) in RCA: 37] [Impact Index Per Article: 3.4] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/20/2022]
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Xu J, Sun J, Wang Y, Sheng J, Wang F, Sun M. Application of iron magnetic nanoparticles in protein immobilization. Molecules 2014; 19:11465-86. [PMID: 25093986 PMCID: PMC6270831 DOI: 10.3390/molecules190811465] [Citation(s) in RCA: 144] [Impact Index Per Article: 13.1] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/23/2014] [Revised: 07/09/2014] [Accepted: 07/09/2014] [Indexed: 12/18/2022] Open
Abstract
Due to their properties such as superparamagnetism, high surface area, large surface-to-volume ratio, easy separation under external magnetic fields, iron magnetic nanoparticles have attracted much attention in the past few decades. Various modification methods have been developed to produce biocompatible magnetic nanoparticles for protein immobilization. This review provides an updated and integrated focus on the fabrication and characterization of suitable magnetic iron nanoparticle-based nano-active materials for protein immobilization.
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Affiliation(s)
- Jiakun Xu
- Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China.
| | - Jingjing Sun
- Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China.
| | - Yuejun Wang
- Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China.
| | - Jun Sheng
- Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China.
| | - Fang Wang
- Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China.
| | - Mi Sun
- Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China.
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Modeling and Simulation of Enzymatic Biofuel Cells with Three-Dimensional Microelectrodes. ENERGIES 2014. [DOI: 10.3390/en7074694] [Citation(s) in RCA: 18] [Impact Index Per Article: 1.6] [Reference Citation Analysis] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 11/16/2022]
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Synthesis and characterization of cysteine functionalized silver nanoparticles for biomolecule immobilization. Bioprocess Biosyst Eng 2014; 37:2139-48. [PMID: 24760173 DOI: 10.1007/s00449-014-1191-8] [Citation(s) in RCA: 21] [Impact Index Per Article: 1.9] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/26/2013] [Accepted: 04/10/2014] [Indexed: 10/25/2022]
Abstract
A facile method for the aqueous phase synthesis of cysteine-functionalized silver nanoparticles by potato extract has been reported in the present work. These functionalized nanoparticles were then used for the covalent immobilization of a biomolecule, alkaline phosphatase, on its surface through carbodiimide coupling. Different reaction parameters such as cysteine concentration, reducing agent concentration, temperature, pH and reaction time were varied during the nanoparticles' formation, and their effects on plasmon resonance were studied using Ultraviolet-visible spectroscopy. Fourier transform infrared spectroscopy was used to confirm the surface modification of silver nanoparticles by cysteine and the particle size analysis was done using particle size analyzer, which showed the average nanoparticles' size of 61 nm for bare silver nanoparticles and 201 nm for the enzyme-immobilized nanoparticles. The synthesized nanoparticles were found to be highly efficient for the covalent immobilization of alkaline phosphatase on its surface and retained 67% of its initial enzyme activity (9.44 U/mg), with 75% binding efficiency. The shelf life of the enzyme-nanoparticle bioconjugates was found to be 60 days, with a 12% loss in the initial enzyme activity. With a simple synthesis strategy, high immobilization efficiency and enhanced stability, these enzyme-coated nanoparticles have the potential for further integration into the biosensor technology.
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Cho H, Jaworski J. A portable and chromogenic enzyme-based sensor for detection of abrin poisoning. Biosens Bioelectron 2013; 54:667-73. [PMID: 24334282 DOI: 10.1016/j.bios.2013.11.058] [Citation(s) in RCA: 9] [Impact Index Per Article: 0.8] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 09/04/2013] [Revised: 11/06/2013] [Accepted: 11/20/2013] [Indexed: 01/27/2023]
Abstract
A first of its kind portable, colorimetric detection system has been developed for the rapid diagnosis of abrin poisoning. Abrin, a natural biotoxin that is homologous to ricin yet more lethal, has high potential for becoming a weapon of bioterrorism given its ease of production. Using an immobilization strategy that implements non-natural amino acids for site-specific conjugation, we have created a reusable N-methyltryptophan oxidase based magnetic bead system that is capable of detecting L-abrine, a marker for abrin poisoning, at concentrations as low as 4 μM in mock urine. Furthermore, we propose that this detection strategy may be readily adaptable for sensing other targets of interest. This unique diagnostic test for abrin poisoning has demonstrated key benefits of portability and simple visual readout. These significant advantages can thus provide the potential for more rapid assessment and corresponding poison management if dedicated toxicology laboratories are not an option.
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Affiliation(s)
- Hwayoung Cho
- Department of Chemical Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul 133-791, Republic of Korea; Institute of Nanoscience and Technology, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul 133-791, Republic of Korea
| | - Justyn Jaworski
- Department of Chemical Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul 133-791, Republic of Korea; Institute of Nanoscience and Technology, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul 133-791, Republic of Korea.
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Eissa S, Matboli M. Integrated technologies in the post-genomic era for discovery of bladder cancer urinary markers. World J Clin Urol 2013; 2:20-31. [DOI: 10.5410/wjcu.v2.i3.20] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 09/29/2013] [Revised: 11/10/2013] [Accepted: 11/21/2013] [Indexed: 02/06/2023] Open
Abstract
The incidence of bladder cancer (BC) continues to rise with high recurrence and mortality rate, especially in the past three decades. The development of accurate and successful BC treatment relies mainly on early diagnosis. BC is a heterogeneous disease reflected by the presence of many potential biomarkers associated with different disease phenotypes. Nowadays, cystoscopy and urinary cytology are considered the gold standard diagnostic tools for BC. There are many limitations to cystoscopy including being invasive, labor-intensive and carcinoma in situ of the bladder may easily be missed. Urinary cytology is still a noninvasive technique with high accuracy in high-grade BC with a median sensitivity of 35%. Furthermore, the need for a sensitive, specific, non invasive, easily accessible BC biomarker is a major clinical need. The field of urinary BC biomarkers discovery is still a rapidly evolving discipline in which more recent technologies are evaluated and often optimized if they are not clinically significant to the urologists. Most of the current strategies for BC urinary biomarker detection depend on integration of information gleaned from the fields of genomics, transcriptomics, proteomics, epigenetics, metabolomics and bionanotechnology. Effort is currently being made to identify the most potentially beneficial urinary biomarkers. The purpose of this review is to summarize and explore the efficacy of gathering the information revealed from the cooperation of different omic strategies that paves the way towards various urinary markers discovery for screening, diagnosis and prognosis of human BC.
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Kamelipour N, Mohsenifar A, Tabatabaei M, Rahmani-Cherati T, Khoshnevisan K, Allameh A, Milani MM, Najavand S, Etemadikia B. Fluorometric determination of paraoxon in human serum using a gold nanoparticle-immobilized organophosphorus hydrolase and coumarin 1 as a competitive inhibitor. Mikrochim Acta 2013. [DOI: 10.1007/s00604-013-1103-7] [Citation(s) in RCA: 22] [Impact Index Per Article: 1.8] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/29/2022]
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Power-free chip enzyme immunoassay for detection of prostate specific antigen (PSA) in serum. Biosens Bioelectron 2013; 49:478-84. [DOI: 10.1016/j.bios.2013.05.058] [Citation(s) in RCA: 50] [Impact Index Per Article: 4.2] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 04/03/2013] [Revised: 05/21/2013] [Accepted: 05/31/2013] [Indexed: 11/22/2022]
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Eissa S, Shawky SM, Matboli M, Mohamed S, Azzazy HME. Direct detection of unamplified hepatoma upregulated protein RNA in urine using gold nanoparticles for bladder cancer diagnosis. Clin Biochem 2013; 47:104-10. [PMID: 24183881 DOI: 10.1016/j.clinbiochem.2013.10.022] [Citation(s) in RCA: 23] [Impact Index Per Article: 1.9] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 08/31/2013] [Revised: 10/16/2013] [Accepted: 10/21/2013] [Indexed: 12/13/2022]
Abstract
OBJECTIVE To develop a gold nanoparticle (AuNP) assay for direct detection of unamplified HURP RNA in urine. DESIGN AND METHODS HURP RNA was extracted from urine samples (50 bladder carcinoma patients, 25 benign bladder lesions, and 25 controls) and further purified using magnetic nanoparticles (MNPs), functionalized with HURP RNA-specific oligonucleotides, and then detected by RT-PCR or gold nanoparticles. RESULTS The developed HURP RNA AuNP assay has a sensitivity and a specificity of 88.5% and 94%, respectively, and a detection limit of 2.4 nmol/L. The concordance between the HURP AuNP assay with RT-PCR after RNA purification using functionalized MNPs was 97%. CONCLUSIONS The developed colorimetric HURP RNA AuNP assay is sensitive, simple, and can aid noninvasive diagnosis of bladder cancer.
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Affiliation(s)
- Sanaa Eissa
- Oncology Diagnostic Unit, Medical Biochemistry and Molecular Biology Department, Faculty of Medicine, Ain Shams University, Abbassia, Cairo 11381, Egypt
| | - Sherif M Shawky
- Youssef Jameel Science & Technology Research Center, The American University in Cairo, P.O. Box 74, New Cairo 11835, Egypt
| | - Marwa Matboli
- Oncology Diagnostic Unit, Medical Biochemistry and Molecular Biology Department, Faculty of Medicine, Ain Shams University, Abbassia, Cairo 11381, Egypt
| | - Shaymaa Mohamed
- Oncology Diagnostic Unit, Medical Biochemistry and Molecular Biology Department, Faculty of Medicine, Ain Shams University, Abbassia, Cairo 11381, Egypt
| | - Hassan M E Azzazy
- Youssef Jameel Science & Technology Research Center, The American University in Cairo, P.O. Box 74, New Cairo 11835, Egypt; Department of Chemistry, The American University in Cairo, P.O. Box 74, New Cairo 11835, Egypt.
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Tudorachi N, Chiriac A. Obtaining of new magnetic nanocomposites based on modified polysaccharide. Carbohydr Polym 2013; 98:451-9. [DOI: 10.1016/j.carbpol.2013.05.080] [Citation(s) in RCA: 4] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/27/2013] [Revised: 04/29/2013] [Accepted: 05/28/2013] [Indexed: 10/26/2022]
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45
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Homaei AA, Sariri R, Vianello F, Stevanato R. Enzyme immobilization: an update. J Chem Biol 2013; 6:185-205. [PMID: 24432134 DOI: 10.1007/s12154-013-0102-9] [Citation(s) in RCA: 512] [Impact Index Per Article: 42.7] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 06/05/2013] [Accepted: 07/31/2013] [Indexed: 11/25/2022] Open
Abstract
Compared to free enzymes in solution, immobilized enzymes are more robust and more resistant to environmental changes. More importantly, the heterogeneity of the immo-bilized enzyme systems allows an easy recovery of both enzymes and products, multiple re-use of enzymes, continuous operation of enzymatic processes, rapid termination of reactions, and greater variety of bioreactor designs. This paper is a review of the recent literatures on enzyme immobilization by various techniques, the need for immobilization and different applications in industry, covering the last two decades. The most recent papers, patents, and reviews on immobilization strategies and application are reviewed.
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Affiliation(s)
- Ahmad Abolpour Homaei
- Department of Biology, Faculty of Science, University of Hormozgan, Bandarabbas, Iran
| | - Reyhaneh Sariri
- Reyhaneh Sariri, Department of Microbiology, Lahijan Branch, Islamic Azad University, Lahijan, Iran
| | - Fabio Vianello
- Department of Comparative Biomedicine and Food Science, University of Padua, Padua, Italy
| | - Roberto Stevanato
- Department of Molecular Sciences and Nanosystems, University of Venice, Venice, Italy
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Greiner R, Konietzny U, Blackburn DM, Jorquera MA. Production of partially phosphorylated myo-inositol phosphates using phytases immobilised on magnetic nanoparticles. BIORESOURCE TECHNOLOGY 2013; 142:375-383. [PMID: 23747448 DOI: 10.1016/j.biortech.2013.05.056] [Citation(s) in RCA: 20] [Impact Index Per Article: 1.7] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Received: 04/05/2013] [Revised: 05/14/2013] [Accepted: 05/15/2013] [Indexed: 06/02/2023]
Abstract
Phytases of different origin were covalently bound onto Fe3O4 magnetic nanoparticles (12 nm). Binding efficiencies of all three phytases were well above 70% relative to the number of aldehyde groups available on the surface of the magnetic nanoparticles. Temperature stability for all three phytases was enhanced as a consequence of immobilisation, whereas pH dependence of enzyme activity was not affected. Maximum catalytic activity of the immobilised phytases was found at 60°C (rye), 65°C (Aspergillus niger) and 70°C (Escherichia albertii). The immobilised enzymes exhibited the same excellent substrate specificities and unique myo-inositol phosphate phosphatase activities as their soluble counterparts. However, the catalytic turnover number dropped drastically for the immobilised phytases. The amount of the desired partially phosphorylated myo-inositol phosphate isomer could be easily controlled by the contact time of substrate solution and immobilised enzymes. The immobilised phytases showed a high operational stability by retaining almost full activity even after fifty uses.
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Affiliation(s)
- Ralf Greiner
- Max Rubner-Institut, Department of Food Technology and Bioprocess Engineering, Haid-und-Neu-Strasse 9, 76131 Karlsruhe, Germany.
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Pečová M, Šebela M, Marková Z, Poláková K, Čuda J, Šafářová K, Zbořil R. Thermostable trypsin conjugates immobilized to biogenic magnetite show a high operational stability and remarkable reusability for protein digestion. NANOTECHNOLOGY 2013; 24:125102. [PMID: 23466477 DOI: 10.1088/0957-4484/24/12/125102] [Citation(s) in RCA: 12] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 06/01/2023]
Abstract
In this work, magnetosomes produced by microorganisms were chosen as a suitable magnetic carrier for covalent immobilization of thermostable trypsin conjugates with an expected applicability for efficient and rapid digestion of proteins at elevated temperatures. First, a biogenic magnetite was isolated from Magnetospirillum gryphiswaldense and its free surface was coated with the natural polysaccharide chitosan containing free amino and hydroxy groups. Prior to covalent immobilization, bovine trypsin was modified by conjugating with α-, β- and γ-cyclodextrin. Modified trypsin was bound to the magnetic carriers via amino groups using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide and N-hydroxysulfosuccinimide as coupling reagents. The magnetic biomaterial was characterized by magnetometric analysis and electron microscopy. With regard to their biochemical properties, the immobilized trypsin conjugates showed an increased resistance to elevated temperatures, eliminated autolysis, had an unchanged pH optimum and a significant storage stability and reusability. Considering these parameters, the presented enzymatic system exhibits properties that are superior to those of trypsin forms obtained by other frequently used approaches. The proteolytic performance was demonstrated during in-solution digestion of model proteins (horseradish peroxidase, bovine serum albumin and hen egg white lysozyme) followed by mass spectrometry. It is shown that both magnetic immobilization and chemical modification enhance the characteristics of trypsin making it a promising tool for protein digestion.
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Affiliation(s)
- M Pečová
- Department of Protein Biochemistry and Proteomics, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University, Šlechtitelů 11, 783 71 Olomouc, Czech Republic
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Figueira JA, Sato HH, Fernandes P. Establishing the feasibility of using β-glucosidase entrapped in Lentikats and in sol-gel supports for cellobiose hydrolysis. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 2013; 61:626-34. [PMID: 23294439 DOI: 10.1021/jf304594s] [Citation(s) in RCA: 15] [Impact Index Per Article: 1.3] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 05/02/2023]
Abstract
β-Glucosidases represent an important group of enzymes due to their pivotal role in various biotechnological processes. One of the most prominent is biomass degradation for the production of fuel ethanol from cellulosic agricultural residues and wastes, where the use of immobilized biocatalysts may prove advantageous. Within such scope, the present work aimed to evaluate the feasibility of entrapping β-glucosidase in either sol-gel or in Lentikats supports for application in cellobiose hydrolysis, and to perform the characterization of the resulting bioconversion systems. The activity and stability of the immobilized biocatalyst over given ranges of temperature and pH values were assessed, as well as kinetic data, and compared to the free form, and the operational stability was evaluated. Immobilization increased the thermal stability of the enzyme, with a 10 °C shift to an optimal temperature in the case of sol-gel support. Mass transfer hindrances as a result of immobilization were not significant, for sol-gel support. Lentikats-entrapped glucosidase was used in 19 consecutive batch runs for cellobiose hydrolysis, without noticeable decrease in product yield. Moreover, encouraging results were obtained for continuous operation. In the overall, the feasibility of using immobilized biocatalysts for cellobiose hydrolysis was established.
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Affiliation(s)
- Joelise A Figueira
- Department of Food Science, School of Food Engineering, University of Campinas-UNICAMP, Campinas, SP, Brazil
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Min D, Zhang X, He W, Zhang Y, Li P, Zhang M, Liu J, Liu S, Xu F, Du Y, Zhang Z. Direct immobilization of glucose oxidase in magnetic mesoporous bioactive glasses. J Mater Chem B 2013; 1:3295-3303. [DOI: 10.1039/c3tb20480d] [Citation(s) in RCA: 12] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/21/2022]
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50
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Evaluation of a silver-based electrocatalyst for the determination of hydrogen peroxide formed via enzymatic oxidation. Talanta 2012; 99:989-96. [DOI: 10.1016/j.talanta.2012.07.082] [Citation(s) in RCA: 9] [Impact Index Per Article: 0.7] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 06/15/2012] [Revised: 07/25/2012] [Accepted: 07/30/2012] [Indexed: 11/23/2022]
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