Purification and characterization of a Penicillium sp. lipase which discriminates against diglycerides.
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).
Gulomova
K
K
Institute of Microbiology, Uzbek Academy of Sciences, Tashkent, Uzbekistan.
Ziomek
E
E
Schrag
J D
JD
Davranov
K
K
Cygler
M
M
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004075:Diglycerides / Q000378:metabolism*; D005989:Glycerides / Q000378:metabolism; D007700:Kinetics; D008049:Lipase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D011312:Pressure; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013499:Surface Properties; D014280:Triglycerides / Q000378:metabolism
D004075:Diglycerides; D005989:Glycerides; D010446:Peptide Fragments; D014280:Triglycerides; D008049:Lipase; C005830:tributyrin