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Lin YY, Huang SF, Liao KW, Ho CT, Hung WL. Quantitation of α-Dicarbonyls, Lysine- and Arginine-Derived Advanced Glycation End Products, in Commercial Canned Meat and Seafood Products. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 2023; 71:6727-6737. [PMID: 37088952 PMCID: PMC10161224 DOI: 10.1021/acs.jafc.3c01205] [Citation(s) in RCA: 3] [Impact Index Per Article: 1.5] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 05/03/2023]
Abstract
Commercial sterilization is a thermal processing method commonly used in low-acid canned food products. Meanwhile, heat treatment can significantly promote advanced glycation end product (AGE) formation in foodstuffs. In this research, the validated analytical methods have been developed to quantitate both lysine- and arginine-derived AGEs and their precursors, α-dicarbonyls, in various types of commercial canned meat and seafood products. Methylglyoxal-hydroimidazolone 1 was the most abundant AGEs found in the canned food products, followed by Nε-(carboxyethyl)lysine, Nε-(carboxymethyl)lysine, and glyoxal-hydroimidazolone 1. Correlation analysis revealed that methylglyoxal and glyoxal were only positively associated with the corresponding arginine-derived AGEs, while their correlations with the corresponding lysine-derived AGEs were not significant. Importantly, we demonstrated for the first time that total sugar and carbohydrate contents might serve as the potential markers for the prediction of total AGEs in canned meats and seafoods. Altogether, this study provided a more complete view of AGEs' occurrence in commercial canned food products.
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Affiliation(s)
- You-Yu Lin
- Master Program in Food Safety, College of Nutrition, Taipei Medical University, Taipei 11031, Taiwan
| | - Shih-Fang Huang
- Master Program in Food Safety, College of Nutrition, Taipei Medical University, Taipei 11031, Taiwan
| | - Kai-Wei Liao
- School of Food Safety, College of Nutrition, Taipei Medical University, Taipei 11031, Taiwan
| | - Chi-Tang Ho
- Department of Food Science, Rutgers University, New Brunswick, New Jersey 08901, United States
| | - Wei-Lun Hung
- School of Food Safety, College of Nutrition, Taipei Medical University, Taipei 11031, Taiwan
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Liu H, Mu L, Chen X, Wang J, Wang S, Sun B. Core-Shell Metal-Organic Frameworks/Molecularly Imprinted Nanoparticles as Absorbents for the Detection of Pyrraline in Milk and Milk Powder. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 2017; 65:986-992. [PMID: 28081599 DOI: 10.1021/acs.jafc.6b05429] [Citation(s) in RCA: 33] [Impact Index Per Article: 4.1] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 06/06/2023]
Abstract
A novel core-shell metal-organic framework coated with a dummy template molecularly imprinted polymer (MOF@DMIP) was synthesized by one-pot bulk polymerization for the detection of pyrraline in food samples. The pyrraline analogue pyrrolidine-3-carboxylic acid was used as the template because of its lower cost, and MIL-101 was used as the MOF core owing to its numerous inherent advantages, including high chemical and hydrothermal stabilities. MIL-101@DMIP was used to detect trace pyrraline in foods by solid-phase extraction combined with high-performance liquid chromatography. It exhibited the advantages of faster mass transport, excellent sensitivity, and selectivity. Under optimum conditions, the detection limit of this system was 40.7 μg L-1, and a linear range was from 5 × 10-7 to 2 × 10-3 mol L-1, within relative standard deviations of 4.46-6.87%. The recoveries ranged from 92.23 to 103.87%, indicating the excellent ability of the prepared MIL-101@DMIP to recognize pyrraline in complex food matrices and its potential for application in pyrraline detection.
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Affiliation(s)
- Huilin Liu
- Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU) , 11 Fucheng Road, Beijing 100048, China
| | - Lin Mu
- Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU) , 11 Fucheng Road, Beijing 100048, China
| | - Xiaomo Chen
- Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU) , 11 Fucheng Road, Beijing 100048, China
| | - Jing Wang
- Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU) , 11 Fucheng Road, Beijing 100048, China
| | - Shuo Wang
- Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU) , 11 Fucheng Road, Beijing 100048, China
- Key Laboratory of Food Nutrition and Safety, Ministry of Education of China, Tianjin University of Science and Technology , Tianjin 300457, China
| | - Baoguo Sun
- Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU) , 11 Fucheng Road, Beijing 100048, China
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3
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Liang Z, Li L, Fu Q, Zhang X, Xu Z, Li B. Formation and elimination of pyrraline in the Maillard reaction in a saccharide-lysine model system. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE 2016; 96:2555-2564. [PMID: 26260362 DOI: 10.1002/jsfa.7376] [Citation(s) in RCA: 18] [Impact Index Per Article: 2.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Received: 02/22/2015] [Revised: 07/21/2015] [Accepted: 08/06/2015] [Indexed: 06/04/2023]
Abstract
BACKGROUND Pyrraline, a causative factor for various kinds of disease, is also used as a food contaminant to evaluate the formation of advanced glycation end-products (AGEs) in diet foods. In this study, model systems consisting of lysine and different saccharides were heated at different times, temperatures and initial molar ratios of saccharide to lysine under microwave heating conditions in order to investigate the formation of pyrraline. RESULTS Increase in initial molar ratio of saccharide to lysine could significantly promote the formation of pyrraline. Specifically, the pyrraline formation rate was influenced by the structure of saccharides involved in the reaction, and decreased in the following order: lactose > fructose > glucose > sucrose; the highest pyrraline was generated in lactose-lysine models. The maximum pyrraline was formed at 140 °C. Moreover, saccharides and lysine had different effects on the stability of pyrraline. Among the reactants, lysine was the major factor for the instability of pyrraline; a dipyrraline and a crosslink by pyrraline reacting with lysine could be formed. CONCLUSION Pyrraline formation by the saccharide-lysine model system was a dynamic reaction, consisting not only of the pyrraline formation, but also pyrraline elimination with some formation of crosslinks. © 2015 Society of Chemical Industry.
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Affiliation(s)
- Zhili Liang
- College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, China
| | - Lin Li
- College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, China
- Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, South China University of Technology, Guangzhou, China
| | - Quanyi Fu
- College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, China
| | - Xia Zhang
- College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, China
- School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou, China
| | - Zhenbo Xu
- College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, China
- Department of Microbial Pathogenesis, Dental School, University of Maryland, Baltimore, MD, USA
| | - Bing Li
- College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, China
- Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, South China University of Technology, Guangzhou, China
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Formation of Peptide Bound Pyrraline in the Maillard Model Systems with Different Lys-Containing Dipeptides and Tripeptides. Molecules 2016; 21:463. [PMID: 27070556 PMCID: PMC6274133 DOI: 10.3390/molecules21040463] [Citation(s) in RCA: 13] [Impact Index Per Article: 1.4] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/06/2016] [Revised: 03/24/2016] [Accepted: 03/31/2016] [Indexed: 11/28/2022] Open
Abstract
Peptide-bound advanced glycation end-products (peptide-bound AGEs) can be formed when peptides are heated with reducing saccharides. Pyrraline is the one of most commonly studied AGEs in foods, but the relative importance of the precursor peptide structure is uncertain. In the present study, model systems were prepared by heating peptides with glucose from 60 °C to 220 °C for up to 65 min, and the amounts of peptide-bound pyrraline formed were monitored to evaluate the effect of the neighboring amino acids on the peptide-bound pyrraline formation. The physico-chemical properties were introduced to explore the quantitative structure-reactivity relationships between physicochemical properties and peptide bound formation. 3-DG content in dipeptide-glucose model system was higher than that in the corresponding tripeptide-glucose model systems. Dipeptides produced higher amounts of peptide-bound pyrraline than the corresponding tripeptides. The peptide-bound pyrraline and 3-DG production were influenced by the physico-chemical properties of the side chain of amino acids adjacent to Lys in the following order: Lys-Leu/glucose > Lys-Ile/glucose > Lys-Val/ glucose > Lys-Thr/glucose > Lys-Ser/glucose > Lys-Ala/ glucose > Lys-Gly/glucose; Lys-Leu-Gly/glucose > Lys-Ile-Gly/glucose > Lys-Val-Gly/glucose > Lys-Thr-Gly/glucose > Lys-Ser-Gly/glucose > Lys-Ala-Gly/glucose > Lys-Gly-Gly/glucose. For the side chain of amino acids adjacent to Lys in dipeptides, residue volume, polarizability, molecular volume and localized electrical effect were positively related to the yield of peptide bound pyrraline, while hydrophobicity and pKb were negatively related to the yield of peptide bound pyrraline. In terms of side chain of amino acid adjacent to Lys in tripeptides, a similar result was observed, except hydrophobicity was positively related to the yield of peptide bound pyrraline.
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Tsekovska R, Sredovska-Bozhinov A, Niwa T, Ivanov I, Mironova R. Maillard reaction and immunogenicity of protein therapeutics. World J Immunol 2016; 6:19-38. [DOI: 10.5411/wji.v6.i1.19] [Citation(s) in RCA: 2] [Impact Index Per Article: 0.2] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 06/27/2015] [Revised: 11/24/2015] [Accepted: 12/14/2015] [Indexed: 02/05/2023] Open
Abstract
The recombinant DNA technology enabled the production of a variety of human therapeutic proteins. Accumulated clinical experience, however, indicates that the formation of antibodies against such proteins is a general phenomenon rather than an exception. The immunogenicity of therapeutic proteins results in inefficient therapy and in the development of undesired, sometimes life-threatening, side reactions. The human proteins, designed for clinical application, usually have the same amino acid sequence as their native prototypes and it is not yet fully clear what the reasons for their immunogenicity are. In previous studies we have demonstrated for the first time that interferon-β (IFN-β) pharmaceuticals, used for treatment of patients with multiple sclerosis, do contain advanced glycation end products (AGEs) that contribute to IFN-β immunogenicity. AGEs are the final products of a chemical reaction known as the Maillard reaction or glycation, which implication in protein drugs’ immunogenicity has been overlooked so far. Therefore, the aim of the present article is to provide a comprehensive overview on the Maillard reaction with emphasis on experimental data and theoretical consideration telling us why the Maillard reaction warrants special attention in the context of the well-documented protein drugs’ immunogenicity.
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Hellwig M, Bunzel D, Huch M, Franz CMAP, Kulling SE, Henle T. Stability of Individual Maillard Reaction Products in the Presence of the Human Colonic Microbiota. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 2015; 63:6723-30. [PMID: 26186075 DOI: 10.1021/acs.jafc.5b01391] [Citation(s) in RCA: 87] [Impact Index Per Article: 8.7] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 05/09/2023]
Abstract
Maillard reaction products (MRPs) are taken up in substantial amounts with the daily diet, but the majority are not transported across the intestinal epithelium. The aim of this study was to obtain first insights into the stability of dietary MRPs in the presence of the intestinal microbiota. Four individual MRPs, namely, N-ε-fructosyllysine (FL), N-ε-carboxymethyllysine (CML), pyrraline (PYR), and maltosine (MAL), were anaerobically incubated with fecal suspensions from eight human volunteers at 37 °C for up to 72 h. The stability of the MRPs was measured by HPLC with UV and MS/MS detections. The Amadori product FL could no longer be detected after 4 h of incubation. Marked interindividual differences were observed for CML metabolism: Depending on the individual, at least 40.7 ± 1.5% of CML was degraded after 24 h of incubation, and the subjects could thus be tentatively grouped into fast and slow metabolizers of this compound. PYR was degraded by 20.3 ± 4.4% during 24 h by all subjects. The concentration of MAL was not significantly lowered in the presence of fecal suspensions. In no case could metabolites be identified and quantified by different mass spectrometric techniques. This is the first study showing that the human colonic microbiota is able to degrade selected glycated amino acids and possibly use them as a source of energy, carbon, and/or nitrogen.
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Affiliation(s)
- Michael Hellwig
- †Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany
- §Department of Safety and Quality of Fruits and Vegetables, Max Rubner-Institut, Federal Research Institute of Nutrition and Food, Haid-und-Neu-Straße 9, 76131 Karlsruhe, Germany
| | - Diana Bunzel
- §Department of Safety and Quality of Fruits and Vegetables, Max Rubner-Institut, Federal Research Institute of Nutrition and Food, Haid-und-Neu-Straße 9, 76131 Karlsruhe, Germany
| | - Melanie Huch
- §Department of Safety and Quality of Fruits and Vegetables, Max Rubner-Institut, Federal Research Institute of Nutrition and Food, Haid-und-Neu-Straße 9, 76131 Karlsruhe, Germany
| | - Charles M A P Franz
- §Department of Safety and Quality of Fruits and Vegetables, Max Rubner-Institut, Federal Research Institute of Nutrition and Food, Haid-und-Neu-Straße 9, 76131 Karlsruhe, Germany
| | - Sabine E Kulling
- §Department of Safety and Quality of Fruits and Vegetables, Max Rubner-Institut, Federal Research Institute of Nutrition and Food, Haid-und-Neu-Straße 9, 76131 Karlsruhe, Germany
| | - Thomas Henle
- †Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany
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7
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Abstract
In vivo modification of proteins by molecules with reactive carbonyl groups leads to intermediate and advanced glycation end products (AGE). Glucose is a significant glycation reagent due to its high physiological concentration and poorly controlled diabetics show increased albumin glycation. Increased levels of glycated and AGE-modified albumin have been linked to diabetic complications, neurodegeneration, and vascular disease. This review discusses glycated albumin formation, structural consequences of albumin glycation on drug binding, removal of circulating AGE by several scavenger receptors, as well as AGE-induced proinflammatory signaling through activation of the receptor for AGE. Analytical methods for quantitative detection of protein glycation and AGE formation are compared. Finally, the use of glycated albumin as a novel clinical marker to monitor glycemic control is discussed and compared to glycated hemoglobin (HbA1c) as long-term indicator of glycemic status.
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8
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Hellwig M, Henle T. Backen, Altern, Diabetes: eine kurze Geschichte der Maillard-Reaktion. Angew Chem Int Ed Engl 2014. [DOI: 10.1002/ange.201308808] [Citation(s) in RCA: 15] [Impact Index Per Article: 1.4] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/06/2023]
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Hellwig M, Henle T. Baking, ageing, diabetes: a short history of the Maillard reaction. Angew Chem Int Ed Engl 2014; 53:10316-29. [PMID: 25044982 DOI: 10.1002/anie.201308808] [Citation(s) in RCA: 325] [Impact Index Per Article: 29.5] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/09/2013] [Revised: 12/12/2013] [Indexed: 01/11/2023]
Abstract
The reaction of reducing carbohydrates with amino compounds described in 1912 by Louis-Camille Maillard is responsible for the aroma, taste, and appearance of thermally processed food. The discovery that non-enzymatic conversions also occur in organisms led to intensive investigation of the pathophysiological significance of the Maillard reaction in diabetes and ageing processes. Dietary Maillard products are discussed as "glycotoxins" and thus as a nutritional risk, but also increasingly with regard to positive effects in the human body. In this Review we give an overview of the most important discoveries in Maillard research since it was first described and show that the complex reaction, even after over one hundred years, has lost none of its interdisciplinary actuality.
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Affiliation(s)
- Michael Hellwig
- Chair of Food Chemistry, Technische Universität Dresden, D-01062 Dresden (Germany) http://www.chm.tu-dresden.de/lc1
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10
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Hammel YA, Dubois M, Delatour T, Stadler RH. N,N-dimethylpiperidinium (mepiquat): Part 1. Formation in model systems and relevance to roasted food products. Food Addit Contam Part A Chem Anal Control Expo Risk Assess 2014; 31:226-33. [DOI: 10.1080/19440049.2013.871584] [Citation(s) in RCA: 11] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/25/2022]
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Poulsen MW, Hedegaard RV, Andersen JM, de Courten B, Bügel S, Nielsen J, Skibsted LH, Dragsted LO. Advanced glycation endproducts in food and their effects on health. Food Chem Toxicol 2013; 60:10-37. [PMID: 23867544 DOI: 10.1016/j.fct.2013.06.052] [Citation(s) in RCA: 548] [Impact Index Per Article: 45.7] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 01/28/2013] [Revised: 06/23/2013] [Accepted: 06/26/2013] [Indexed: 12/27/2022]
Abstract
Advanced glycation endproducts (AGEs) form by Maillard-reactions after initial binding of aldehydes with amines or amides in heated foods or in living organisms. The mechanisms of formation may include ionic as well as oxidative and radical pathways. The reactions may proceed within proteins to form high-molecular weight (HMW) AGEs or among small molecules to form low-molecular weight (LMW) AGEs. All free amino acids form AGEs, but lysine or arginine side chains dominate AGE formation within proteins. The analysis of AGEs in foods and body fluids is most often performed by ELISA or LC-MS; however, none of the methodologies cover all HMW and LMW AGEs. Most research is, therefore, carried out using 'representative' AGE compounds, most often N(ε)-carboxymethyl-lysine (CML). Only LMW AGEs, including peptide-bound forms, and carbonyls may be absorbed from the gut and contribute to the body burden of AGEs. Some AGEs interact with specific pro- or anti-inflammatory receptors. Most studies on the biological effects of AGEs have been carried out by administering heated foods. The pro-inflammatory and deteriorating biological effects of AGEs in these studies, therefore, need further confirmation. The current review points out several research needs in order to address important questions on AGEs in foods and health.
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Affiliation(s)
- Malene W Poulsen
- Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Rolighedsvej 30, 1958 Frederiksberg C, Denmark
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Release of pyrraline in absorbable peptides during simulated digestion of casein glycated by 3-deoxyglucosone. Eur Food Res Technol 2013. [DOI: 10.1007/s00217-013-2027-5] [Citation(s) in RCA: 22] [Impact Index Per Article: 1.8] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/26/2022]
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Abstract
This is an introduction to a collection of review articles by leading investigators in the field of protein glycation research, see following articles in this issue. With this we launch a section of this journal now established for presentation of research results, reviews and commentaries on protein glycation and related topics. Glycation is the spontaneous, non-enzymatic reaction of protein with saccharides and saccharide derivatives. Although studied in the modern scientific era for over 100 years, its importance in the biology, medicine, food and nutrition, pharmacology and toxicology, and technological processing remains intriguingly undisclosed. In this section of amino acids, research on glycation is a qualifier for publication. Glycation research now has a place to call home.
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Affiliation(s)
- Naila Rabbani
- Clinical Sciences Research Institute, Warwick Medical School, University of Warwick, University Hospital, Clifford Bridge Road, Coventry, CV2 2DX, UK.
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Hellwig M, Geissler S, Matthes R, Peto A, Silow C, Brandsch M, Henle T. Transport of Free and Peptide-Bound Glycated Amino Acids: Synthesis, Transepithelial Flux at Caco-2 Cell Monolayers, and Interaction with Apical Membrane Transport Proteins. Chembiochem 2011; 12:1270-9. [DOI: 10.1002/cbic.201000759] [Citation(s) in RCA: 137] [Impact Index Per Article: 9.8] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/16/2010] [Indexed: 02/02/2023]
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15
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Trends in advanced glycation end products research in diabetes mellitus and its complications. Mol Cell Biochem 2010; 341:33-41. [DOI: 10.1007/s11010-010-0434-5] [Citation(s) in RCA: 50] [Impact Index Per Article: 3.3] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 01/01/2010] [Accepted: 03/09/2010] [Indexed: 12/13/2022]
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Contreras-Calderón J, Guerra-Hernández E, García-Villanova B. Utility of some indicators related to the Maillard browning reaction during processing of infant formulas. Food Chem 2009. [DOI: 10.1016/j.foodchem.2008.11.004] [Citation(s) in RCA: 38] [Impact Index Per Article: 2.4] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/30/2022]
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17
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Delatour T, Hegele J, Parisod V, Richoz J, Maurer S, Steven M, Buetler T. Analysis of advanced glycation endproducts in dairy products by isotope dilution liquid chromatography-electrospray tandem mass spectrometry. The particular case of carboxymethyllysine. J Chromatogr A 2009; 1216:2371-81. [PMID: 19181321 DOI: 10.1016/j.chroma.2009.01.011] [Citation(s) in RCA: 72] [Impact Index Per Article: 4.5] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/27/2008] [Revised: 12/19/2008] [Accepted: 01/05/2009] [Indexed: 10/21/2022]
Abstract
A fully validated multiple-transition recording isotope dilution liquid chromatography-electrospray tandem mass spectrometry (LC-MS/MS) method for the simultaneous quantitative determination of N(epsilon)-carboxymethyllysine (CML) and lysine in dairy products is described. Internal standards were [N-1',2'-(13)C(2)]CML and [1,2,3,4,5,6-(13)C(6)-2,6-(15)N(2)]lysine, and the method was validated by evaluating the selectivity, linearity, precision (repeatability and reproducibility) and trueness, using both powder and liquid products. For liquid dairy products, the repeatability and reproducibility was 2.79% and 11.0%, while 4.85% and 4.92% were determined for powder dairy products, respectively. The trueness of the method ranged from -9.6% to -3.6% for powder and from -0.99% to 6.8% for liquid dairy products. The limit of detection for CML was estimated to be 8 ng CML per mg protein while the limit of quantification was 27 ng CML per mg protein. The method encompasses a proteolytic cleavage mediated by enzymatic digestion to reach a complete release of the amino acids prior to a sample cleanup based on solid phase extraction, and followed by LC-MS/MS analysis of CML and lysine residues. To ensure a suitable performance of the enzymatic digestion, CML measurements were compared to values obtained with an acid hydrolysis-mediated proteolysis. Finally, the method was employed for the analysis of CML in various dairy products. The values compare well to the data available in the literature when similar methods were used, even if some discrepancies were observed upon comparison with the results obtained by other techniques such as enzyme-linked immunosorbent assay and GC-MS.
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Affiliation(s)
- Thierry Delatour
- Nestlé Research Centre, Nestec Ltd, Vers-chez-les-Blanc, Lausanne, Switzerland.
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18
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Indicators of non-enzymatic browning in the evaluation of heat damage of ingredient proteins used in manufactured infant formulas. Eur Food Res Technol 2007. [DOI: 10.1007/s00217-007-0700-2] [Citation(s) in RCA: 23] [Impact Index Per Article: 1.3] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/23/2022]
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Erbersdobler HF, Somoza V. Forty years of furosine – Forty years of using Maillard reaction products as indicators of the nutritional quality of foods. Mol Nutr Food Res 2007; 51:423-30. [PMID: 17390403 DOI: 10.1002/mnfr.200600154] [Citation(s) in RCA: 169] [Impact Index Per Article: 9.4] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/08/2022]
Abstract
The Maillard reaction products (MRPs) most widely used as markers of the nutritional quality of foods are furosine, N(epsilon)-carboxymethyllysine (CML), hydroxymethylfurfural, pyrraline, pentosidine and pronyl-lysine. One of the MRPs identified first was furosine, which was quantified in foods 40 years ago as a chemical indicator of the Amadori compound N(epsilon)-fructoselysine. Since then, furosine has gained broad attention by food chemists and biomedical researchers, as its formation upon heat treatment is well characterised. Moreover, it represents the Amadori products from early Maillard reactions in which amino acids react with reducing carbohydrates, resulting in a loss of their availability. This is of importance for the essential amino acid lysine, which is also the limiting amino acid in many proteins. In order to evaluate the nutritional quality of a protein, the concomitant analysis of free - and nutritionally available - lysine and the amount of lysine reacted to form the respective MRP is essential, even for mildly processed foods. The other chemical markers of heat treatment such as CML, pyrraline, pentosidine or pronyl-lysine seem to be useful markers of the advanced stages of Maillard reactions. Compared to the conditions in which furosine is formed, these compounds are generated under more severe conditions of heat treatment. However, the concentrations analysed are significantly lower than those of furosine. Therefore, the nutritional evaluation of a food protein should include not only furosine, but also other chemical markers of heat treatment such as, for example, CML, pyrraline and pentosidine.
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Silván JM, van de Lagemaat J, Olano A, Del Castillo MD. Analysis and biological properties of amino acid derivates formed by Maillard reaction in foods. J Pharm Biomed Anal 2006; 41:1543-51. [PMID: 16824722 DOI: 10.1016/j.jpba.2006.04.004] [Citation(s) in RCA: 111] [Impact Index Per Article: 5.8] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/19/2005] [Revised: 04/05/2006] [Accepted: 04/10/2006] [Indexed: 10/24/2022]
Abstract
Maillard reaction products (MRPs), especially early stage MRPs and melanoidins, are currently gaining a lot of attention due to their reported health-promoting properties and their potential to be used as functional food ingredients. It is often not clear which specific biological function is assigned to which MRP, due to the large amount of MRPs formed during the reaction and difficulties in their purification and identification. This paper provides an overview of amino acid derivatives such as Amadori compounds, carboxymethyllysine, pyrraline, cross-linking products and melanoidins, which can be formed by Maillard reaction in foods, their biological properties and the analytical tools commonly employed for their determination.
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Affiliation(s)
- José Manuel Silván
- Instituto de Fermentaciones Industriales (CSIC), C/Juan de la Cierva 3, 28006 Madrid, Spain
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Henle T. Protein-bound advanced glycation endproducts (AGEs) as bioactive amino acid derivatives in foods. Amino Acids 2005; 29:313-22. [PMID: 15997413 DOI: 10.1007/s00726-005-0200-2] [Citation(s) in RCA: 208] [Impact Index Per Article: 10.4] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/01/2004] [Accepted: 02/02/2005] [Indexed: 01/12/2023]
Abstract
The Maillard reaction or nonenzymatic browning is of outstanding importance for the formation of flavour and colour of heated foods. Corresponding reactions, also referred to as "glycation", are known from biological systems, where the formation of advanced glycation endproducts (AGEs) shall play an important pathophysiological role in diabetes and uremia. In this review, pathways leading to the formation of individual protein-bound lysine and arginine derivatives in foods are described and nutritional consequences resulting from this posttranslational modifications of food proteins are discussed.
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Affiliation(s)
- T Henle
- Institute of Food Chemistry, Technical University of Dresden, Germany.
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Kwak EJ, Lee YS, Murata M, Homma S. Effect of pH control on the intermediates and melanoidins of nonenzymatic browning reaction. Lebensm Wiss Technol 2005. [DOI: 10.1016/j.lwt.2003.09.011] [Citation(s) in RCA: 14] [Impact Index Per Article: 0.7] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/25/2022]
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23
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Méndez JD, Leal LI. Inhibition of in vitro pyrraline formation by l-arginine and polyamines. Biomed Pharmacother 2004; 58:598-604. [PMID: 15589069 DOI: 10.1016/j.biopha.2004.09.004] [Citation(s) in RCA: 31] [Impact Index Per Article: 1.5] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 08/02/2004] [Indexed: 11/30/2022] Open
Abstract
Glycation of biomolecules such as proteins, nucleic acids and lipids leading to the formation of advanced glycation end products (AGEs) may be a major contributor to the pathological manifestations of diabetes mellitus. Several studies have shown that the chemical inhibition of AGEs formation results in attenuation of diabetic complications. We tested the in vitro inhibition of pyrraline formation on bovine serum albumin and L-lysine by L-arginine and the polyamines putrescine, cadaverine, spermidine and spermine. Among the inhibitors, L-arginine and spermine potently inhibited pyrraline formation. This effect could be related to the presence of the guanidino group in L-arginine and four amino groups in spermine, but this inhibitory effect was also shown by putrescine, cadaverine and spermidine, suggesting that these natural compounds may have a novel therapeutic potential in preventing diabetic complications. A significant unexpected observation emerged when experiments were carried out with aminoguanidine. It showed increased absorbance produced by a non-identified compound whose peak appears at 285 nm, but this aspect remains to be investigated.
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Affiliation(s)
- José D Méndez
- Mexican Institute of Social Security (IMSS), Medical Research Unit in Metabolic Diseases, National Medical Center, Mexico City 06703, México.
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Abstract
The term "advanced glycation end products" (AGEs) stands for a heterogeneous group of amino acid derivatives that are formed via glycation processes between peptide-bound lysine or arginine derivatives and carbonyl compounds, processes originally known from food systems as "Maillard reactions." AGEs accumulate in plasma and tissues with advancing age, diabetes, and particular renal failure. In vivo and in vitro studies indicate that AGEs represent an important class of uremic toxins. This review focuses on the chemistry behind the formation of AGEs, possible mechanisms underlying the accumulation of AGEs in uremia, clinical and therapeutic implications, and possible nutritional consequences.
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Affiliation(s)
- Thomas Henle
- Institute of Food Chemistry, Technical University of Dresden, Germany
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Yoshihara K, Kiyonami R, Shimizu Y, Beppu M. Determination of urinary pyrraline by solid-phase extraction and high performance liquid chromatography. Biol Pharm Bull 2001; 24:863-6. [PMID: 11510474 DOI: 10.1248/bpb.24.863] [Citation(s) in RCA: 14] [Impact Index Per Article: 0.6] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/22/2022]
Abstract
Pyrraline is one of the advanced glycation end products formed under non-enzymatic and non-oxidative conditions in vivo. In this study, we developed a novel method for determination of urinary pyrraline using solid-phase extraction as a pretreatment procedure prior to determination by high performance liquid chromatography (HPLC). The Oasis HLB solid-phase extraction cartridge was used for pretreatment of urine samples without hydrolysis. The chromatogram obtained clearly revealed the peak for urinary pyrraline owing to prior removal of interfering substances in urine samples. The recovery rate of pyrraline was 97.2+/-3.3% (n=6). The mean excretion level of urinary pyrraline in healthy control (20-77 years old, n = 30) was 1.42+/-0.65 micromol/mmol creatinine, and the daily variation in the excretion level was considered to be insignificant. We propose the above procedure as a simple, rapid, and accurate method for determination of pyrraline levels in urine.
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Affiliation(s)
- K Yoshihara
- Laboratory of Public Health, School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Japan
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26
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HAYASE F. Recent Development of 3-Deoxyosone Related Maillard Reaction Products. FOOD SCIENCE AND TECHNOLOGY RESEARCH 2000. [DOI: 10.3136/fstr.6.79] [Citation(s) in RCA: 25] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 11/03/2022]
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27
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Rizzi GP. Chemical structure of colored maillard reaction products. FOOD REVIEWS INTERNATIONAL 1997. [DOI: 10.1080/87559129709541096] [Citation(s) in RCA: 80] [Impact Index Per Article: 2.9] [Reference Citation Analysis] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 10/20/2022]
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Portero-Otin M, Nagaraj RH, Monnier VM. Chromatographic evidence for pyrraline formation during protein glycation in vitro and in vivo. BIOCHIMICA ET BIOPHYSICA ACTA 1995; 1247:74-80. [PMID: 7873594 DOI: 10.1016/0167-4838(94)00209-y] [Citation(s) in RCA: 64] [Impact Index Per Article: 2.1] [Reference Citation Analysis] [Abstract] [MESH Headings] [Grants] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/27/2023]
Abstract
Pyrraline (epsilon-2-(formyl-5-hydroxymethyl-pyrrol-1-yl)-L-norleucine) is an advanced Maillard reaction product formed from 3-deoxyglucosone in the non-enzymatic reaction between glucose and the epsilon-amino group of lysine residues on proteins. Although its presence in vivo as well as in in vitro incubations of proteins with sugars has been documented by immunochemical methods using polyclonal and monoclonal antibodies, its formation in proteins has recently been questioned by similar methodology. To clarify this issue, we investigated pyrraline formation in proteins following alkaline hydrolysis and quantitation by high-performance liquid chromatography on a C18 reverse-phase column. Time- and sugar concentration-dependent increase in pyrraline formation was noted in serum albumin incubated with either 100 mM glucose or 50 mM 3-deoxyglucosone. Formation of pyrraline from 3-deoxyglucosone was rapid at slightly acidic pH, confirming its synthetic pathway through this Maillard reaction intermediate. Low levels of pyrraline (< 10 pmol/mg protein) were also detected in a pool of human skin collagen by this method, but no age effect was apparent. Using a slightly different approach, pyrraline-like material was detected in human plasma proteins following enzyme digestion and analysis by high performance liquid chromatography. Plasma from diabetic patients showed a significant increase in pyrraline-like material compared to controls. The levels in diabetic and normal individuals were 21.6 +/- 9.56 and 12.8 +/- 5.6 pmol per mg protein, respectively (P = 0.005), reflecting thereby the elevated levels of the immediate precursor of pyrraline, 3-deoxyglucosone, in diabetic plasma.
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Affiliation(s)
- M Portero-Otin
- Institute of Pathology, Case Western Reserve University, Cleveland, OH 44106
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Wang CJ, Lin YL, Lin JK. Mutagenicity and cytotoxicity of nitropyrrole compounds derived from the reaction of 2-acetyl pyrrole with nitrite. Food Chem Toxicol 1994; 32:839-44. [PMID: 7927082 DOI: 10.1016/0278-6915(94)90161-9] [Citation(s) in RCA: 13] [Impact Index Per Article: 0.4] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/27/2023]
Abstract
2-Acetylpyrrole (AP) is a product of model browning systems, and has been isolated as a major flavour component of many foods. Reaction of AP with nitrite produces two N-nitropyrrole compounds, 1-nitro-2-acetyl-pyrrole (NAP) and 1,3,5-trinitro-2-acetylpyrrole (TNAP), the chemical structures of which have been confirmed by spectral studies, including UV mass, nuclear magnetic resonance, infra-red and elemental analysis (EA). NAP and TNAP are moderately mutagenic to the Salmonella strains TA98 and TA100 in the absence of a mammalian activation system and are markedly cytotoxic to mouse C3H10T1/2 cells. These results suggest that the formation of direct-acting mutagens of nitro-derivatives may take place in nitrite-containing food or in vivo by nitrosation following ingestion of AP.
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Affiliation(s)
- C J Wang
- Institute of Biochemistry, Chung Shan Medical and Dental College, Taichung, Taiwan, Republic of China
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Henle T, Klostermeyer H. Determination of protein-bound 2-amino-6-(2-formyl-1-pyrrolyl)-hexanoic acid (?pyrraline?) by ion exchange Chromatography and photodiode array detection. ACTA ACUST UNITED AC 1993. [DOI: 10.1007/bf01192975] [Citation(s) in RCA: 31] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/01/2022]
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31
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Sengl M, Ledl F, Severin T. [Maillard reaction of bovine serum albumin with glucose. Determination of 2-formyl-5-(hydroxymethyl)pyrrole-1-norleucine by high-performance liquid chromatography after alkaline hydrolysis]. J Chromatogr A 1989; 463:119-25. [PMID: 2715232 DOI: 10.1016/s0021-9673(01)84458-7] [Citation(s) in RCA: 24] [Impact Index Per Article: 0.7] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/02/2023]
Abstract
Reactions between glucose and bovine serum albumin proceed predominantly at the side chain amino groups of lysine residues. Among other products, protein-bound 2-formyl-5-(hydroxymethyl)pyrrole-1-norleucine is formed. After alkaline hydrolysis and fractionation of the protein hydrolysate on RP-18 material this substance can be separated by high-performance liquid chromatography. The identity of the norleucine derivative with a synthesized compound can be determined with fast atom bombardment-mass spectrometry spectral data. A colour reaction with thiobarbituric acid is also suitable for detection.
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Affiliation(s)
- M Sengl
- Institut für Pharmazie und Lebensmittelchemie, Universität München, F.R.G
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Njoroge FG, Fernandes AA, Monnier VM. 3-(D-Erythro-Trihydroxypropyl)-1-Neopentyl Pyrrole-2-Carboxaldehyde. A Novel Nonenzymatic Browning Product of Glucose. J Carbohydr Chem 1987. [DOI: 10.1080/07328308708058885] [Citation(s) in RCA: 19] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/23/2022]
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Oimomi M, Nishimoto S, Matsumoto S, Hatanaka H, Ishikawa K, Baba S. A specific method of glycosylated hemoglobin using furosine measurement. Diabetes Res Clin Pract 1985; 1:193-5. [PMID: 3939117 DOI: 10.1016/s0168-8227(85)80011-5] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Indexed: 01/08/2023]
Abstract
In order to get an accurately specific determination of glycosylated hemoglobin (GHb-f), the furosine assay method, which can detect epsilon-amino-lysine-bound glucose, was investigated. A good correlation was found between GHb-f values obtained by this method and HbA1 values by conventional ion exchange column chromatography. It was, therefore, considered that this technique would be a new useful method for determining glycosylated hemoglobin.
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Milić BL, Piletić MV. The mechanism of pyrrole, pyrazine and pyridine formation in non-enzymic browning reaction. Food Chem 1984. [DOI: 10.1016/0308-8146(84)90071-2] [Citation(s) in RCA: 22] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/01/2022]
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Westphal G, Cieślik E. Untersuchungen zur Maillard-Reaktion 5. Mitt. Produkt-Analyse der Reaktion von Glucose mit Phenylalanin in Wasser. ACTA ACUST UNITED AC 1982. [DOI: 10.1002/food.19820260913] [Citation(s) in RCA: 3] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/07/2022]
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