Effect of glycation degree on the structure and digestion properties of ovalbumin: A study of amino acids and peptides release after in vitro gastrointestinal simulated digestion

[Display omitted] •The structure of ovalbumin was changed by different glycation degree.•Glycation reduced protein digestibility, leading to the presence of large fragments after in vitro simulated digestion.•The content of EAA and TAA released after digestion decreased, especially in the intestinal...

Full description

Saved in:
Bibliographic Details
Published in:Food chemistry 2022-03, Vol.373 (Pt B), p.131331-131331, Article 131331
Main Authors: Yang, Qi, Wang, Ying, Yang, Meng, Liu, Xuanting, Lyu, Siwen, Liu, Boqun, Liu, Jingbo, Zhang, Ting
Format: Article
Language:English
Subjects:
Amino acid
Amino Acids
Animals
Digestibility
Digestion
Glycation
Glycosylation
Ovalbumin
Ovalbumin - metabolism
Peptide
Peptides - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:[Display omitted] •The structure of ovalbumin was changed by different glycation degree.•Glycation reduced protein digestibility, leading to the presence of large fragments after in vitro simulated digestion.•The content of EAA and TAA released after digestion decreased, especially in the intestinal phase after adding trypsin.•Peptide release and the distribution of peptide segments cleaved by trypsin were greatly influenced by glycation. Glycation can improve the functional properties of protein. However, in vitro and animal studies have shown that glycation induced lysine blockage and impaired protein digestibility. This study aimed to explore the effects of different glycation degree on the structure and digestive characteristics of ovalbumin. The results showed that glycation decreased the turbidity and hydrophobicity of the protein and changed the protein structure. Moreover, the results of in vitro simulated digestion revealed that glycation reduced the contents of essential amino acids and total amino acids after digestion. Glycation changed the amino acids and peptides release from the protein by resisting the digestion of digestive enzymes, especially trypsin. In conclusion, this work links glycation, protein digestibility, and the release of amino acids and peptides. This emphasizes the importance of the balance between improving properties and ensuring the digestibility of proteins during food processing.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2021.131331