Genetic and biochemical characterization of a highly thermostable α-L-arabinofuranosidase from Thermobacillus xylanilyticus

被引:76
作者
Debeche, T
Cummings, S
Connerton, I
Debeire, P
O'Donohue, MJ
机构
[1] INRA, Unite Physico Chim & Biotechnol, F-51687 Reims 02, France
[2] Univ Nottingham, Sch Biol Sci, Div Food Sci, Loughborough LE12 5RD, Leics, England
关键词
D O I
10.1128/AEM.66.4.1734-1736.2000
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
The gene encoding an alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus D3, AbfD3, was isolated. Characterization of the purified recombinant alpha-L-arabinofuranosidase produced in Escherichia coli revealed that it is highly stable with respect to both temperature (up to 90 degrees C) and pH (stable in the pH range 4 to 12). On the basis of amino acid sequence similarities, this 56,071-Da enzyme could be assigned to family 51 of the glycosyl hydrolase classification system. However, substrate specificity analysis revealed that AbfD3, unlike the majority of F51 members, displays high activity in the presence of polysaccharides.
引用
收藏
页码:1734 / 1736
页数:3
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