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Purification and characterization of a Penicillium sp. lipase which discriminates against diglycerides
Author(s) -
Gulomova Komola,
Ziomek Edmund,
Schrag Joseph D.,
Davranov Kahramon,
Cygler Miroslaw
Publication year - 1996
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/bf02522923
Subject(s) - tributyrin , lipase , hydrolysis , chemistry , diglyceride , triglyceride , triacylglycerol lipase , monoglyceride , chromatography , penicillium , enantiomer , enzyme , biochemistry , organic chemistry , food science , fatty acid , cholesterol
A lipase was isolated from Penicillium sp. strain UZLM‐4 and characterized. This lipase has a molecular weight of 27,344 (determined by mass spectrometry) and hydrolyzes triglycerides in preference to mono‐ and diglyceride substrates. Among various triglyceride substrates, tributyrin is hydrolyzed about four times faster than any other tested. The lipase has a preference for hydrolysis at the 1,3 positions of the lipids and shows a weak stereoselectivity for the S enantiomer. Unlike most other lipases, this lipase is stable and has a high activity at low surface pressures (5–10 mN/m).