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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Format: | Article |
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Elsevier
2022-01-01
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Series: | Current Research in Food Science |
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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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institution | Directory Open Access Journal |
issn | 2665-9271 |
language | English |
last_indexed | 2024-04-13T05:12:51Z |
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series | Current Research in Food Science |
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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