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Hydrolysis of Milk Protein by a Bacillus licheniformis Protease Specific for Acidic Amino Acid Residues
Author(s) -
MADSEN J.S.,
QVIST K.B.
Publication year - 1997
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1997.tb04435.x
Subject(s) - bacillus licheniformis , chemistry , casein , hydrolysate , whey protein , protease , hydrolysis , biochemistry , peptide bond , hydrolyzed protein , enzyme , proteolysis , chromatography , beta lactoglobulin , peptide , substrate (aquarium) , serine protease , capillary electrophoresis , bacillus subtilis , bacteria , biology , ecology , genetics
A serine protease, which preferentially cleaves peptide bonds at the carboxylic site of Glu and Asp was evaluated with milk proteins as substrate. The enzyme hydrolyzed casein almost 10 times more efficiently than whey protein. In the casein assay, whey protein did not inhibit the protease, but the enzyme activity in a chromogenic assay was severely inhibited by one whey protein, β‐lactoglobulin. Capillary electrophoresis of β‐lactoglobulin hydrolysate revealed a peptide profile corresponding to the numbers of susceptible bonds, The enzyme may provide advantages in preparation of functional protein fractions and in cheese ripening.