Abstract
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).
MeSH terms
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Amino Acid Sequence
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Chromatography, High Pressure Liquid
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Chromatography, Ion Exchange
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Diglycerides / metabolism*
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Glycerides / metabolism
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Kinetics
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Lipase / chemistry
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Lipase / isolation & purification*
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Lipase / metabolism*
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Mass Spectrometry
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Molecular Sequence Data
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Molecular Weight
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Penicillium / enzymology*
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification
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Pressure
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Sequence Homology, Amino Acid
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Substrate Specificity
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Surface Properties
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Triglycerides / metabolism
Substances
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Diglycerides
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Glycerides
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Peptide Fragments
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Triglycerides
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Lipase
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tributyrin