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Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing
α‐Dicarbonyl compounds (α‐DCs) are a class of compounds generated during the thermal processing of food. Due to the high reactivity, α‐DCs were endowed with the ability to react with food components thus lowering nutrition value and even leading to a potential risk for food safety. In this study, me...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8020911/ https://www.ncbi.nlm.nih.gov/pubmed/33841846 http://dx.doi.org/10.1002/fsn3.2211 |
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author | Wu, Yuekun Dong, Lu Wu, Yajing Wu, Dongyan Zhang, Yan Wang, Shuo |
author_facet | Wu, Yuekun Dong, Lu Wu, Yajing Wu, Dongyan Zhang, Yan Wang, Shuo |
author_sort | Wu, Yuekun |
collection | PubMed |
description | α‐Dicarbonyl compounds (α‐DCs) are a class of compounds generated during the thermal processing of food. Due to the high reactivity, α‐DCs were endowed with the ability to react with food components thus lowering nutrition value and even leading to a potential risk for food safety. In this study, methylglyoxal (MG), the most abundant α‐DCs, was selected to investigate the alteration effects on the structure and digestibility of α‐lactalbumin (αLA) under thermal processing (60–100°C). The results showed that the modification degree of αLA by MG increased with the rise of processing temperature, accompanied by the significant changes in molecular weight, intrinsic fluorescence, and secondary structures of αLA. High‐resolution mass spectrometry analysis identified that lysine (Lys) and arginine (Arg) are the modification sites, and N(ε)‐(carboxyethyl)‐L‐lysine is the main modification type. Since the Lys and Arg are also the cleavage sites of trypsin, the digestibility of MG modified αLA (MG‐αLA) by trypsin correspondingly decreased with an increase of processing temperature. The reacted Lys and Arg residues, and the protein‐bound AGEs were quantified, and the contents were found to be highly dependent on the temperature. |
format | Online Article Text |
id | pubmed-8020911 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-80209112021-04-08 Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing Wu, Yuekun Dong, Lu Wu, Yajing Wu, Dongyan Zhang, Yan Wang, Shuo Food Sci Nutr Original Research α‐Dicarbonyl compounds (α‐DCs) are a class of compounds generated during the thermal processing of food. Due to the high reactivity, α‐DCs were endowed with the ability to react with food components thus lowering nutrition value and even leading to a potential risk for food safety. In this study, methylglyoxal (MG), the most abundant α‐DCs, was selected to investigate the alteration effects on the structure and digestibility of α‐lactalbumin (αLA) under thermal processing (60–100°C). The results showed that the modification degree of αLA by MG increased with the rise of processing temperature, accompanied by the significant changes in molecular weight, intrinsic fluorescence, and secondary structures of αLA. High‐resolution mass spectrometry analysis identified that lysine (Lys) and arginine (Arg) are the modification sites, and N(ε)‐(carboxyethyl)‐L‐lysine is the main modification type. Since the Lys and Arg are also the cleavage sites of trypsin, the digestibility of MG modified αLA (MG‐αLA) by trypsin correspondingly decreased with an increase of processing temperature. The reacted Lys and Arg residues, and the protein‐bound AGEs were quantified, and the contents were found to be highly dependent on the temperature. John Wiley and Sons Inc. 2021-02-28 /pmc/articles/PMC8020911/ /pubmed/33841846 http://dx.doi.org/10.1002/fsn3.2211 Text en © 2021 The Authors. Food Science & Nutrition published by Wiley Periodicals LLC This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Research Wu, Yuekun Dong, Lu Wu, Yajing Wu, Dongyan Zhang, Yan Wang, Shuo Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing |
title | Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing |
title_full | Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing |
title_fullStr | Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing |
title_full_unstemmed | Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing |
title_short | Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing |
title_sort | effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8020911/ https://www.ncbi.nlm.nih.gov/pubmed/33841846 http://dx.doi.org/10.1002/fsn3.2211 |
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