一种对甘油二酯有区分作用的青霉菌脂肪酶的纯化与特性研究
Purification and characterization of a Penicillium sp. lipase which discriminates against diglycerides.
作者信息
Gulomova K, Ziomek E, Schrag J D, Davranov K, Cygler M
机构信息
Institute of Microbiology, Uzbek Academy of Sciences, Tashkent, Uzbekistan.
出版信息
Lipids. 1996 Apr;31(4):379-84. doi: 10.1007/BF02522923.
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).
从青霉菌株UZLM-4中分离并鉴定了一种脂肪酶。这种脂肪酶的分子量为27344（通过质谱法测定），优先水解甘油三酯而非甘油单酯和甘油二酯底物。在各种甘油三酯底物中，三丁酸甘油酯的水解速度比其他任何测试底物快约四倍。该脂肪酶倾向于在脂质的1,3位进行水解，并且对S对映体表现出较弱的立体选择性。与大多数其他脂肪酶不同，这种脂肪酶在低表面压力（5-10 mN/m）下稳定且具有高活性。
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