Comparison of glycation and glycosylation level between bovine milk-based and goat milk-based infant formula through label-free proteomics techniques

Heat treatment is unavoidable in the processing of infant formula; however, heat treatment causes the proteins to undergo Maillard reaction and form glycation products, which can negatively affect the nutrition and function of the protein. At the same time, glycosylation is a broad post-translationa...

Full description

Saved in:
Bibliographic Details
Published inFood bioscience Vol. 59; p. 103857
Main Authors Han, Hongyang, Pei, Jingjing, Feng, Jianhui, Yao, Huifang, Han, Binsong, Hou, Yanmei, Xie, Kui, Zhong, Jinjing, Zhang, Lina, Hettinga, Kasper, Zhou, Peng
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 01.06.2024
Subjects
Online AccessGet full text
ISSN2212-4292
DOI10.1016/j.fbio.2024.103857

Cover

More Information
Summary:Heat treatment is unavoidable in the processing of infant formula; however, heat treatment causes the proteins to undergo Maillard reaction and form glycation products, which can negatively affect the nutrition and function of the protein. At the same time, glycosylation is a broad post-translational protein modification that is important in a variety of biological processes. However, glycated proteins as well as N-glycoprotein components in infant formula have not been well characterized. Here, a comprehensive comparative analysis of the glycated proteome as well as the N-glycosylated proteome was conducted in both bovine milk-based (BF) and goat milk-based (GF) infant formula. In total, 918 whey proteins were identified from the whey fraction, including 200 glycated proteins and 219 glycosylated proteins. Furthermore, 33 N-glycosylated proteins containing 101 N-glycosylation sites and 64 glycosylated peptides derived from 30 proteins were significantly different (p < 0.05) between BF and GF. Most of the significantly different proteins are associated with innate immunity as well as defense responses. With respect to the differences between BF and GF, ɑ-lactalbumin (LALBA) had higher glycation level in BF than GF; whereas β-lactoglobulin (LGB) had higher glycation level in GF than BF. For glycosylation level, transferin (TF) was highly glycosylated in GF than BF; while serum albumin (ALB) was highly glycosylated in BF than GF. Our results elucidated the proteome, glycated proteome, N-glycosylated proteome in bovine milk-based and goat milk-based infant formulas, which may be useful to researchers in related fields and provide guidance on the improvement of processing technology for infant formula.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:2212-4292
DOI:10.1016/j.fbio.2024.103857