Purification and characterization of a<i>Penicillium</i> sp. lipase which discriminates against diglycerides
Komola GulomovaInstitute of Microbiology Uzbek Academy of Sciences Tashkent UzbekistanEdmund ZiomekBiotechnology Research Institute National Research Council 6100 Royalmount Ave. Montreal Quebec H4P 2R2 CanadaJoseph D. SchragBiotechnology Research Institute National Research Council 6100 Royalmount Ave. Montreal Quebec H4P 2R2 CanadaKakhramon DavranovInstitute of Microbiology Uzbek Academy of Sciences Tashkent UzbekistanMirosław CyglerBiotechnology Research Institute National Research Council 6100 Royalmount Ave. Montreal Quebec H4P 2R2 Canada
ABI
Аннотация
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).
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