Debeche T, Cummings N, Connerton I, Debeire P, O'Donohue M J
INRA, Unité de Physicochimie et Biotechnologie des Polymères, 51687 Reims Cedex 02, France.
Appl Environ Microbiol. 2000 Apr;66(4):1734-6. doi: 10.1128/AEM.66.4.1734-1736.2000.
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.
从嗜热木聚糖分解芽孢杆菌D3（Thermobacillus xylanilyticus D3）中分离出编码α-L-阿拉伯呋喃糖苷酶的基因AbfD3。对在大肠杆菌中产生的纯化重组α-L-阿拉伯呋喃糖苷酶的特性进行表征后发现，它在温度（高达90摄氏度）和pH值（在pH 4至12范围内稳定）方面都具有高度稳定性。基于氨基酸序列相似性，这种56071道尔顿的酶可归类于糖基水解酶分类系统的第51家族。然而，底物特异性分析表明，与大多数第51家族成员不同，AbfD3在多糖存在的情况下表现出高活性。
