Abstract
This work analyzed the antidiabetic activity of peptides from whey proteins after hydrolysis by Lactobacillus rhamnosus GG and Streptococcus thermophilus SY-102, emphasizing the differences between the proteolytic systems of both bacteria. Peptide fractions from whey proteins may have biological functions, such as antidiabetic functions, which inhibit the DPP-IV enzyme, and lactic acid bacteria could release them. A whey solution of 10% was fermented with selected lactic acid bacteria in monoculture and coculture, analyzing kinetic parameters and the proteolytic profile, using the 2,4,6-trinitrobenzene sulfonic acid technique for free amino groups’ determination and Tris-tricine polyacrylamide gel electrophoresis. An in vitro inhibition assay of the DPP-IV enzyme was used. The kinetic parameters showed a faster duplication rate in the monoculture with L. rhamnosus GG than in the co-culture, which was related to lactic acid production. Co-culture does not have the highest production of free amino groups and peptides. Still, peptide fractions with lower molecular weight (<2 kDa) were found and showed a high DPP-IV inhibitory capacity that was maintained from the middle of the fermentation to the end (55.4%). In comparison, the monoculture of L. rhamnosus GG increased from 0 to 63.3%. This demonstrates that the proteolytic capacity and the proteolytic system of each lactic acid bacteria determine the structure of the released peptides.
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