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红链霉菌产生的溶菌酶的纯化及特性研究

Purification and characterization of lysozyme produced by Streptomyces erythraeus.

作者信息

Morita T, Hara S, Matsushima Y

出版信息

J Biochem. 1978 Mar;83(3):893-903. doi: 10.1093/oxfordjournals.jbchem.a131987.

Abstract

A species of lysozyme (SE lysozyme) was purified from culture filtrate of Streptomyces erythraeus. The enzyme has a molecular weight of 18,500 as determined by ultracentrifugation. Its isoelectric point is 9.5, and it shows optimal activity at pH 4.0 with an optimal ionic strength of 0.1. Investigation of the substrate specificity showed SE lysozyme to be an N-acetyl-muramidase. The simplest product in the digest of cell walls of Micrococcus lysodeikticus was identified as a disaccharide, [GlcNAcbeta(1 leads to 4) MurNAc]. While S. aureus as well as M. lysodeikticus was lysed by this lysozyme, chitin and its derivatives were not.

摘要

从红霉素链霉菌的培养滤液中纯化出了一种溶菌酶(SE溶菌酶)。通过超速离心测定,该酶的分子量为18,500。其等电点为9.5,在pH 4.0、最佳离子强度为0.1时表现出最佳活性。对底物特异性的研究表明,SE溶菌酶是一种N - 乙酰胞壁质酶。在溶壁微球菌细胞壁消化过程中,最简单的产物被鉴定为二糖,[GlcNAcbeta(1→4)MurNAc]。虽然金黄色葡萄球菌和溶壁微球菌都能被这种溶菌酶裂解,但几丁质及其衍生物则不能。

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