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Keywords:

  • Bacillus licheniformis;
  • protease;
  • casein;
  • whey protein

ABSTRACT

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.