PURIFICATION AND CHARACTERIZATION OF A XYLANASE AND AN ARABINOFURANOSIDASE FROM BACILLUS-POLYMYXA

被引：32

作者：

MORALES, P ^{[1
]}

MADARRO, A ^{[1
]}

FLORS, A ^{[1
]}

SENDRA, JM ^{[1
]}

PEREZGONZALEZ, JA ^{[1
]}

机构：

[1] CSIC,INST AGROQUIM & TECNOL ALIMENTOS,DEPT BIOTECNOL,E-46010 VALENCIA,SPAIN

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1995年 / 17卷 / 05期

关键词：

BACILLUS POLYMYXA; XYLANASE; ARABINOFURANOSIDASE; PURIFICATION; CHARACTERIZATION;

D O I：

10.1016/0141-0229(94)00062-V

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Two hemicellulases from Bacillus polymyxa were purified and characterized: a xylanase with a molecular mass of 61 kD and pI of 4.7 and an arabinofuranosidase with a molecular mass of 166 kD and pI of 4.7. The xylanase, which showed increased thermostability in the presence of MgCl2, showed a typical endo-action mode on xylans from several sources. The arabinofuranosidase was only active on (1-->5)-alpha-L-arabinooligosaccharides but not on linear (1-->5>)-alpha-L-arabinan, arabinogalactan, and arabinoxylan. Ho,wever, it was able to release arabinose from arabinoxylan when an active endoxylanase was also present in hydrolysis assays.

引用

页码：424 / 429

页数：6

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