基于胰蛋白酶图谱分析对VAPS-24来源的内切-1,4-β-木聚糖酶的结构洞察
Tryptic Mapping Based Structural Insights of Endo-1, 4-β-Xylanase from VAPS-24.
作者信息
Mathibe Brian N, Malgas Samkelo, Radosavljevic Layla, Kumar Vishal, Shukla Pratyoosh, Pletschke Brett I
机构信息
Enzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, Eastern Cape 6140 South Africa.
Enzyme Technology and Protein Bioinformatics Laboratory, Department of Microbiology, Maharshi Dayanand University, Rohtak, Haryana 124001 India.
出版信息
Indian J Microbiol. 2020 Sep;60(3):392-395. doi: 10.1007/s12088-020-00879-2. Epub 2020 May 11.
Abstract
An endo-1,4-β-xylanase, XynA, from 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 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.
摘要
从VAPS - 24中纯化得到一种内切 - 1,4 - β - 木聚糖酶XynA，纯化后的该酶达到了均一性，其分子量约为20 kDa。发现XynA的蛋白质序列与其他来源的木聚糖酶相似，因此，它可以作为一种模型酶，用于理解蛋白质结构 - 活性关系，并有助于蛋白质工程设计具有理想特性的酶变体。因此，这种木聚糖酶将是生物燃料和精细化工行业中用于降解蒸汽预处理生物质中木聚糖的有吸引力的候选酶。
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