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 α-lactalbumin (α-LA) stored the bile salts inhibited microbial...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1992, Vol.56 (7), p.1066-1070
Main Authors: Naka, Y. (Amano Pharmaceutical Co. Ltd., Nishiharu, Aichi (Japan)), Nakamura, T
Format: Article
Language:English
Subjects:
ACIDE AMINE
ALBUMINAS
ALBUMINE
ALBUMINS
AMINO ACIDS
AMINOACIDOS
Analytical, structural and metabolic biochemistry
BILE SALTS
Biological and medical sciences
BLOOD SERUM
ENZIMAS
ENZYME
ENZYMES
Enzymes and enzyme inhibitors
ESTIMULO
Fundamental and applied biological sciences. Psychology
Hydrolases
INHIBICION
INHIBITION
LIPOPROTEIN LIPASE
LIPOPROTEINA LIPASA
LIPOPROTEINE LIPASE
MUCOR
PANCREAS
SALES BILIARES
SEL BILIAIRE
SERUM SANGUIN
STIMULI
STIMULUS
SUERO SANGUINEO
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Summary: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 α-lactalbumin (α-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.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.56.1066