THE EFFECTS OF SERUM-ALBUMIN AND RELATED AMINO-ACIDS ON PANCREATIC LIPASE AND BILE-SALTS INHIBITED MICROBIAL LIPASES

The activities of microbial lipases were inhibited by bile salts in a non-emulsifying assay system. To protect lipase activities from inactivation, the effects of proteins and amino acids were investigated. Bovine serum albumin (BSA) and alpha-lactalbumin (alpha-LA) stored the bile salts inhibited microbial lipases. Among N-end amino groups contained in BSA, L-histidine restored the activities of the bile salts inhibited microbial lipases. On the other hand, pancreatic lipase activity was stimulated by not only BSA, but L-histidine and L-aspartic acid as N-end amino groups of BSA and additionally accelerated it in combination with bile salts.