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 a...

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Veröffentlicht in:	Lipids 1996-04, Vol.31 (4), p.379-384
Hauptverfasser:	Gulomova, K. (Uzbek Academy of Sciences, Tashkent, Uzbekistan.), Ziomek, E, Schrag, J.D, Davranov, K, Cygler, M
Format:	Artikel
Sprache:	eng
Schlagworte:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Amino Acid Sequence AMINO ACID SEQUENCES CHEMICAL COMPOSITION Chromatography, High Pressure Liquid Chromatography, Ion Exchange COMPOSICION QUIMICA COMPOSITION CHIMIQUE CULTURE MEDIA Diglycerides - metabolism ENZYMIC ACTIVITY Glycerides - metabolism Kinetics Lipase - chemistry Lipase - isolation & purification Lipase - metabolism Mass Spectrometry MEDIO DE CULTIVO MILIEU DE CULTURE MOLECULAR SEQUENCE DATA Molecular Weight PENICILLIUM Penicillium - enzymology Peptide Fragments - chemistry Peptide Fragments - isolation & purification Pressure PURIFICACION PURIFICATION Sequence Homology, Amino Acid Substrate Specificity SUBSTRATES Surface Properties TRIACILGLICEROL LIPASA TRIACYLGLYCEROL LIPASE Triglycerides - metabolism
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Zusammenfassung:	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).
ISSN:	0024-4201 1558-9307
DOI:	10.1007/BF02522923