Research Grants 23/04462-0 - Peptídeos bioativos, Laticínios - BV FAPESP
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Effect of beta-casein genetic variant on protein hydrolysis and peptide profile formed during in vitro gastrointestinal digestion of different dairy matrices

Abstract

Milk is recognized for its nutritional quality and content of proteins of high biological value, which are source of bioactive peptides resulting from enzymatic hydrolysis that occurs during the processing or digestion of milk and dairy products. However, studies suggest that a specific peptide released from enzymatic hydrolysis of ²-casein, ²-casomorphine-7, may have adverse effects on the human body. The release of this protein fraction, resulting from hydrolysis of ²-casein at bond 66-67, is dependent on the genetic variant of ²-casein present in milk. The hypothesis that this peptide is formed only in the hydrolysis of ²-casein A1 and B genetic variants has motivated the production and commercialization of A2 milk, which has only ²-casein A2 in its composition. Several studies have evaluated the effect of different genetic variants of ²-casein on the release of ²-casomorphine-7 during gastrointestinal digestion, however, the effect of the dairy matrix on digestion of different genetic variants of ²-casein has not yet been clarified. Thus, this project aims to evaluate the effect of the genetic variant of ²-casein (A1 or A2) on the technological characteristics and peptide profile of fermented dairy products, as well as the kinetics of protein digestion during in vitro simulation of gastrointestinal digestion of different dairy matrices and peptides bioavailability. (AU)

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