Hydrolysis of sequenced beta-casein peptides provides new insight into peptidase activity from thermophilic lactic acid bacteria and highlights intrinsic resistance of phosphopeptides.

Abstract

The peptidases of thermophilic lactic acid bacteria have a key role in the proteolysis of Swiss cheeses during warm room ripening. To compare their peptidase activities toward a dairy substrate, a tryptic/chymotryptic hydrolysate of purified beta-casein was used. Thirty-four peptides from 3 to 35 amino acids, including three phosphorylated peptides… (More)

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@article{Deutsch2000HydrolysisOS, title={Hydrolysis of sequenced beta-casein peptides provides new insight into peptidase activity from thermophilic lactic acid bacteria and highlights intrinsic resistance of phosphopeptides.}, author={Sebastian Deutsch and Doroth{\'e}e Molle and Val{\'e}rie Gagnaire and Mich{\`e}le Piot and Dani{\'e}le Atlan and Sylvie Lortal}, journal={Applied and environmental microbiology}, year={2000}, volume={66 12}, pages={5360-7} }