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来自淡紫拟青霉D218的聚(3-羟基丁酸酯)解聚酶的纯化及性质

Purification and properties of poly(3-hydroxybutyrate) depolymerase from the fungus Paecilomyces lilacinus D218.

作者信息

Oda Y, Osaka H, Urakami T, Tonomura K

机构信息

Department of Food Science and Technology, Fukuyama University, Fukuyama, Hiroshima 729-02, Japan.

出版信息

Curr Microbiol. 1997 Apr;34(4):230-2. doi: 10.1007/s002849900174.

DOI:10.1007/s002849900174
PMID:9058543
Abstract

Poly(3-hydroxybutyrate) depolymerase was purified to homogeneity from the culture filtrate of Paecilomyces lilacinus D218 by column chromatography on CM-Toyopearl 650M and hydroxylapatite. The molecular weight of the enzyme was estimated to be 48,000 by SDS-PAGE. Maximal activity was observed near pH 7.0 and 45 degrees C. The Km and Vmax values for PHB were 0.13(mg/ml) and 3750 (U/mg protein), respectively. The enzyme hydrolyzed PHB and p-nitrophenyl fatty acids but not polycaprolactone and triglycerides.

摘要

通过在CM-Toyopearl 650M和羟基磷灰石上进行柱色谱,从淡紫拟青霉D218的培养滤液中纯化出聚(3-羟基丁酸酯)解聚酶至同质。通过SDS-PAGE估计该酶的分子量为48,000。在pH 7.0和45℃附近观察到最大活性。PHB的Km和Vmax值分别为0.13(mg/ml)和3750(U/mg蛋白质)。该酶水解PHB和对硝基苯基脂肪酸,但不水解聚己内酯和甘油三酯。

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