Cloning, expression and characterization of a novel acidic xylanase, XYL11B, from the acidophilic fungus Bispora sp MEY-1
Cloning, expression and characterization of a novel acidic xylanase, XYL11B, from the acidophilic fungus Bispora sp MEY-1
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DOI：
10.1016/j.enzmictec.2009.05.002
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发表时间：
2009-08-07
影响因子：
3.4
通讯作者：
Yao, Bin
中科院分区：
文献类型：
--
作者：
Luo, Huiying;Wang, Yaru;Yao, Bin
从毕赤酵母MEY-1中克隆出木聚糖酶基因xyl11B，并在毕赤酵母中表达。xyl11B含有一个66 bp的内含子，编码一个219个残基的成熟蛋白，与里氏木霉苷水解酶家族11的木聚糖酶具有最高的同源性（57.1%）。纯化后的重组酶XYL11B是嗜酸酶，在pH 2.6和65℃时表现出最大的活性。该酶还具有耐热性和pH稳定性，对胃蛋白酶和胰蛋白酶都具有高度的抗性，表明作为饲料添加剂在消化道中具有良好的性能，可以改善动物的营养。XYL11B的活性被大多数金属离子增强，但被Hg2+弱抑制。Pb2+和Cu2+。强烈抑制许多其他木聚糖酶。XYL11B对燕麦木聚糖底物的比活性为2049 U mg（-1）。木聚糖的主要水解产物为木糖和木糖二糖。(C) 2009爱思唯尔公司版权所有。
A xylanase gene (xyl11B) was cloned from Bispora sp. MEY-1 and expressed in Pichia pastons. xyl11B, with a 66-bp intron, encodes a mature protein of 219 residues with highest identity (57.1%) to the Trichoderma reesei xylanase of glycoside hydrolase family 11. The purified recombinant XYL11B was acidophilic, exhibiting maximum activity at pH 2.6 and 65 degrees C. The enzyme was also thermostable, pH stable, and was highly resistant to both pepsin and trypsin, suggesting good performance in the digestive tract as a feed supplement to improve animal nutrition. The activity of XYL11B was enhanced by most metal ions but was inhibited weakly by Hg2+. Pb2+ and Cu2+. which strongly inhibit many other xylanases. The specific activity of XYL11B for oat spelt xylan substrate was 2049 U mg(-1). The main hydrolysis products of xylan were xylose and xylobiose. (C) 2009 Elsevier Inc. All rights reserved.