An endo-1,4-β-xylanase, XynA, from Thermomyces lanuginosus VAPS-24, was purified to homogeneity and exhibited a molecular mass of approximately 20 kDa. The protein sequence of XynA was found to be similar to those of other Thermomyces lanuginosus derived xylanases and, as a result, could be used as a model enzyme for understanding the protein structure–activity relationship and facilitating protein engineering to design enzyme variants with desirable properties. Therefore, this xylanase will be an attractive candidate for applications in the biofuel and fine chemical industries for the degradation of xylans in steam pre-treated biomass.

中文翻译：

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基于胰蛋白酶定位的来自疏毛嗜热丝孢菌 VAPS-24 的 Endo-1, 4-β-木聚糖酶的结构洞察。

来自疏毛嗜热丝孢菌VAPS-24的内切 1,4-β-木聚糖酶 XynA被纯化至均一，分子量约为 20 kDa。发现 XynA 的蛋白质序列与其他疏毛型嗜热丝孢菌衍生的木聚糖酶的蛋白质序列相似，因此可用作模型酶以了解蛋白质结构-活性关系并促进蛋白质工程设计具有所需特性的酶变体. 因此，这种木聚糖酶将成为生物燃料和精细化工行业应用的有吸引力的候选者，用于降解蒸汽预处理生物质中的木聚糖。