A family 5 beta-mannanase from the thermophilic fungus Thielavia arenaria XZ7 with typical thermophilic enzyme features
文献类型: 外文期刊
第一作者: Lu, Haiqiang
作者: Lu, Haiqiang;Shi, Pengjun;Luo, Huiying;Wang, Yaru;Yang, Peilong;Yao, Bin;Zhang, Huitu
作者机构:
关键词: Thielavia arenaria XZ7;beta-Mannanase;Thermophilic;Alkali-tolerant
期刊名称:APPLIED MICROBIOLOGY AND BIOTECHNOLOGY ( 影响因子:4.813; 五年影响因子:4.697 )
ISSN: 0175-7598
年卷期: 2013 年 97 卷 18 期
页码:
收录情况: SCI
摘要: A novel beta-mannanase gene, man5XZ7, was cloned from thermophilic fungus Thielavia arenaria XZ7, and successfully expressed in Pichia pastoris. The gene (1,110 bp) encodes a 369-amino acid polypeptide with a molecular mass of approximately 40.8 kDa. The deduced sequence of Man5XZ7 consists of a putative 17-residue signal peptide and a catalytic module belonging to glycoside hydrolase (GH) family 5, and displays 76 % identity with the experimentally verified GH 5 endo-beta-1,4-mannanase from Podospora anserina. Recombinant Man5XZ7 was optimally active at 75 A degrees C and pH 5.0 and exhibited high activity at a wide temperature range (> 50.0 % activity at 50-85 A degrees C). Moreover, it had good adaptability to acidic to basic pH (> 74.1 % activity at pH 4.0-7.0 and 25.6 % even at pH 9.0) and good stability from pH 3.0 to 10.0. These enzymatic properties showed that Man5XZ7 was a new thermophilic and alkali-tolerant beta-mannanase. Further amino acid composition analysis indicated that Man5XZ7 has several characteristic features of thermophilic enzymes.
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