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产紫青霉可产生多种木聚糖酶:两种酶的纯化及性质研究

Penicillium purpurogenum produces several xylanases: purification and properties of two of the enzymes.

作者信息

Belancic A, Scarpa J, Peirano A, Díaz R, Steiner J, Eyzaguirre J

机构信息

Laboratorio de Bioquímica, Pontificia Universidad Católica de Chile, Santiago.

出版信息

J Biotechnol. 1995 Jul 15;41(1):71-9. doi: 10.1016/0168-1656(95)00057-w.

Abstract

The fungus Penicillium purpurogenum produces several extracellular xylanases. The two major forms (xylanases A and B) have been purified and characterized. After ammonium sulfate precipitation and chromatography in Bio-Gel P 100, xylanase A was further purified by means of DEAE-cellulose, hydroxylapatite and CM-Sephadex, and xylanase B by DEAE-cellulose and CM-Sephadex. Both xylanases showed apparent homogeneity in SDS-polyacrylamide gel electrophoresis. Xylanase A (33 kDa) has an isoelectric point of 8.6, while xylanase B (23 kDa) is isoelectric at pH 5.9. Antisera against both enzymes do not cross-react. The amino terminal sequences of xylanases A and B show no homology. The results obtained suggest that the enzymes are produced by separate genes and they may perform different functions in xylan degradation.

摘要

产紫青霉可产生多种胞外木聚糖酶。已对两种主要形式(木聚糖酶A和B)进行了纯化和特性鉴定。经硫酸铵沉淀和在Bio-Gel P 100中进行层析后,木聚糖酶A通过DEAE-纤维素、羟基磷灰石和CM-葡聚糖凝胶进一步纯化,木聚糖酶B则通过DEAE-纤维素和CM-葡聚糖凝胶纯化。两种木聚糖酶在SDS-聚丙烯酰胺凝胶电泳中均显示出明显的均一性。木聚糖酶A(33 kDa)的等电点为8.6,而木聚糖酶B(23 kDa)在pH 5.9时达到等电点。针对这两种酶的抗血清不发生交叉反应。木聚糖酶A和B的氨基末端序列没有同源性。所得结果表明,这些酶由不同的基因产生,并且它们在木聚糖降解中可能发挥不同的功能。

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