κ-Casein as a source of short-chain bioactive peptides generated by Lactobacillus helveticus.

ABSTRACT: This paper explores the ability of Lactobacillus helveticus strains to release sequences of short biologically active peptides (containing 2-10 amino acid residues) from casein. The proteolytic enzymes of the tested strains exhibit different patterns of cleavage of CN fractions. The modification of κ-casein (κ-CN) with pyrrolidone carboxylic acid inhibits the proteolytic activity of strains L. helveticus 141 and the reference strain (DSMZ 20075), while the modification with phosphothreonine inhibits enzymes of all the tested bacteria. The peptide sequencing analysis indicated that the examined strains produced functional peptides very efficiently. κ-CN proved to be the main source of short peptides released by bacterial enzymes, and the hydrolysis of κ-CN yielded eighty-two bioactive pepti

SUBMITTER: Skrzypczak K 

PROVIDER: S-EPMC5629177 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature