Quantitative N-glycoproteome analysis of bovine milk and yogurt

Post-translational modification structure of food's proteins might be changed during processing, thereby affecting the nutritional characteristics of the food product. In this study, differences in protein N-glycosylation patterns between milk and yogurt were quantitatively compared based on gl...

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Main Authors: Jing Xiao, Jinqiu Wang, Renyou Gan, Di Wu, Yisha Xu, Lianxin Peng, Fang Geng
Format: Article
Language:English
Published: Elsevier 2022-01-01
Series:Current Research in Food Science
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S266592712200003X
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author Jing Xiao
Jinqiu Wang
Renyou Gan
Di Wu
Yisha Xu
Lianxin Peng
Fang Geng
author_facet Jing Xiao
Jinqiu Wang
Renyou Gan
Di Wu
Yisha Xu
Lianxin Peng
Fang Geng
author_sort Jing Xiao
collection DOAJ
description Post-translational modification structure of food's proteins might be changed during processing, thereby affecting the nutritional characteristics of the food product. In this study, differences in protein N-glycosylation patterns between milk and yogurt were quantitatively compared based on glycopeptide enrichment, liquid chromatography separation, and tandem mass spectrometry analysis. A total of 181 N-glycosites were identified, among which 142 were quantified in milk and yogurt. Significant alterations in the abundance of 13 of these N-glycosites were evident after the fermentation of milk into yogurt. Overall, the N-glycosylation status of the majority of milk proteins remained relatively unchanged in yogurt, suggesting that their conformations, activities, and functions were maintained despite the fermentation process. Among the main milk proteins, N241 of cathepsin D and N358 of lactoperoxidase were markedly reduced after undergoing lactic acid fermentation to produce yogurt. Furthermore, a comparative analysis of current and previously reported N-glycoproteomic data revealed heterogeneity in the N-glycosylation of milk proteins. To sum up, a quantitative comparison of the N-glycoproteomes of milk and yogurt was presented here for the first time, providing evidence that the fermentation process of yogurt could cause changes in the N-glycosylation of certain milk proteins.
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spelling doaj.art-58bf3631f4f149c6a47441e67ad8967f2022-12-22T03:00:59ZengElsevierCurrent Research in Food Science2665-92712022-01-015182190Quantitative N-glycoproteome analysis of bovine milk and yogurtJing Xiao0Jinqiu Wang1Renyou Gan2Di Wu3Yisha Xu4Lianxin Peng5Fang Geng6Key Laboratory of Coarse Cereal Processing (Ministry of Agriculture and Rural Affairs), School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, ChinaKey Laboratory of Coarse Cereal Processing (Ministry of Agriculture and Rural Affairs), School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, ChinaResearch Center for Plants and Human Health, Institute of Urban Agriculture, Chinese Academy of Agricultural Sciences, Chengdu, 610213, Sichuan, ChinaKey Laboratory of Coarse Cereal Processing (Ministry of Agriculture and Rural Affairs), School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, ChinaKey Laboratory of Coarse Cereal Processing (Ministry of Agriculture and Rural Affairs), School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, ChinaKey Laboratory of Coarse Cereal Processing (Ministry of Agriculture and Rural Affairs), School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, ChinaKey Laboratory of Coarse Cereal Processing (Ministry of Agriculture and Rural Affairs), School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, China; Corresponding author.Post-translational modification structure of food's proteins might be changed during processing, thereby affecting the nutritional characteristics of the food product. In this study, differences in protein N-glycosylation patterns between milk and yogurt were quantitatively compared based on glycopeptide enrichment, liquid chromatography separation, and tandem mass spectrometry analysis. A total of 181 N-glycosites were identified, among which 142 were quantified in milk and yogurt. Significant alterations in the abundance of 13 of these N-glycosites were evident after the fermentation of milk into yogurt. Overall, the N-glycosylation status of the majority of milk proteins remained relatively unchanged in yogurt, suggesting that their conformations, activities, and functions were maintained despite the fermentation process. Among the main milk proteins, N241 of cathepsin D and N358 of lactoperoxidase were markedly reduced after undergoing lactic acid fermentation to produce yogurt. Furthermore, a comparative analysis of current and previously reported N-glycoproteomic data revealed heterogeneity in the N-glycosylation of milk proteins. To sum up, a quantitative comparison of the N-glycoproteomes of milk and yogurt was presented here for the first time, providing evidence that the fermentation process of yogurt could cause changes in the N-glycosylation of certain milk proteins.http://www.sciencedirect.com/science/article/pii/S266592712200003XMilkYogurtN-glycoproteomeLactotransferrinLactoperoxidase
spellingShingle Jing Xiao
Jinqiu Wang
Renyou Gan
Di Wu
Yisha Xu
Lianxin Peng
Fang Geng
Quantitative N-glycoproteome analysis of bovine milk and yogurt
Current Research in Food Science
Milk
Yogurt
N-glycoproteome
Lactotransferrin
Lactoperoxidase
title Quantitative N-glycoproteome analysis of bovine milk and yogurt
title_full Quantitative N-glycoproteome analysis of bovine milk and yogurt
title_fullStr Quantitative N-glycoproteome analysis of bovine milk and yogurt
title_full_unstemmed Quantitative N-glycoproteome analysis of bovine milk and yogurt
title_short Quantitative N-glycoproteome analysis of bovine milk and yogurt
title_sort quantitative n glycoproteome analysis of bovine milk and yogurt
topic Milk
Yogurt
N-glycoproteome
Lactotransferrin
Lactoperoxidase
url http://www.sciencedirect.com/science/article/pii/S266592712200003X
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