Enzymatic digest of whey protein and wheylin-1, a dipeptide released in the digest, increase insulin sensitivity in an Akt phosphorylation-dependent manner

Food & Function
Maiko OgiwaraKousaku Ohinata

Abstract

We investigated the effects of the enzymatic digest of β-lactoglobulin, a major bovine milk whey protein, on glucose metabolism in KK-Ay mice, an animal model of type II diabetes. In the glucose tolerance test and insulin tolerance test (ITT), the thermolysin digest of β-lactoglobulin decreased blood glucose levels, suggesting that it increases insulin sensitivity in diabetic KK-Ay mice. The digest also increased phosphorylation of Akt, an intracellular factor activated in response to the insulin receptor activation, in the liver and skeletal muscle. Next, we searched for a bioactive peptide present in the digest that increased the insulin sensitivity. Wheylin-1 is an anxiolytic-like dipeptide (Met-His) isolated from the thermolysin digest of β-lactoglobulin. Wheylin-1 decreased blood glucose levels in the ITT test and increased hepatic Akt phosphorylation. Wheylin-1 also increased insulin-induced Akt phosphorylation in hepatic HepG2 cells and muscular C2C12 myotube cells. These results suggest that wheylin-1 increases insulin sensitivity in an Akt-dependent manner in vivo and in vitro. Taken together, we found that the thermolysin digest of bovine milk whey β-lactoglobulin and wheylin-1 increase insulin sensitivity in an Akt s...Continue Reading

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Citations

Oct 28, 2019·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Akitoshi NagaiKousaku Ohinata
Nov 27, 2020·International Journal of Molecular Sciences·Giovanni Tulipano

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Methods Mentioned

BETA
electrophoresis

Software Mentioned

ProteinSimple
Compass

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