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环孢青霉M1部分甘油酯水解酶的纯化及性质

Purification and properties of partial glyceride hydrolase of Penicillium cyclopium M1.

作者信息

Okumura S, Iwai M, Tsujisaka Y

出版信息

J Biochem. 1980 Jan;87(1):205-11. doi: 10.1093/oxfordjournals.jbchem.a132726.

Abstract

A lipolytic enzyme which hydrolyzed monoacylglycerols more easily than triacylglycerols was found in the culture broth of Penicillium cyclopium M1. The enzyme was purified to homogeneity and its properties were investigated. Among various substrates used, monoacylglycerols, especially those of medium chain fatty acids, were hydrolyzed very rapidly. Although the rate was low, the enzyme hydrolyzed methyl esters of fatty acids, Span or triacylglycerols of medium chain fatty acids. Based on its substrate specificity, the enzyme was regarded as a partial glyceride hydrolase. When the partial glyceride hydrolase was used in conjunction with lipase on triacylglycerol, the degree of hydrolysis of triacylglycerol became extremely high.

摘要

在圆孤青霉M1的培养液中发现了一种脂解酶,该酶水解单酰甘油比水解三酰甘油更容易。该酶被纯化至同质,并对其性质进行了研究。在使用的各种底物中,单酰甘油,尤其是中链脂肪酸的单酰甘油,水解速度非常快。虽然水解速度较低,但该酶能水解脂肪酸甲酯、司盘或中链脂肪酸的三酰甘油。基于其底物特异性,该酶被视为一种甘油酯水解酶。当甘油酯水解酶与脂肪酶一起用于三酰甘油时,三酰甘油的水解程度变得极高。

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