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An improved method for the colorimetric assay of lipase activity using an optically clear medium
Author(s) -
Renard G.,
Grimaud J.,
El Zanf A.,
Pina M.,
Gralle J.
Publication year - 1987
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02540372
Subject(s) - rhizopus arrhizus , lipase , chemistry , chromatography , bovine serum albumin , clinical chemistry , optically active , enzyme , biochemistry , organic chemistry
Lipase activity can be spectrophometrically measured in an optically clear medium using long chain fatty thioesters of 1‐mercapto‐2,3‐propanediol or 2‐mercaptoethanol as substrates. With hexamethylphosphoric triamide solutions of these thiosubstrates, the Michaëlis‐Menten constants of lipase from Rhizopus arrhizus were determined. The effects of calcium chloride and of bovine serum albumin on the enzyme activity were established.