Effect of glycation derived from α-dicarbonyl compounds on the in vitro digestibility of ovalbumin: Tracing of advanced glycation end-products and immuno-active peptides
FOOD RESEARCH INTERNATIONAL(2023)
Abstract
•Glycation reduced protein digestibility by blocking cleavage sites and inducing steric hindrance.•AGEs masked IgE epitopes of OVA, counteracting the negative effects of reduced digestibility on antigenicity.•The formed AGEs survived protease hydrolysis and were additionally formed along digestion.•Substantial changes existed in peptide release pattern, including AGE-Ms within the sequences of protease-resistant epitopes of OVA.
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Key words
glycation,digestibility,peptides,ovalbumin,end-products,immuno-active
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