A thermophilic beta-mannanase from Neosartorya fischeri P1 with broad pH stability and significant hydrolysis ability of various mannan polymers

文献类型: 外文期刊

第一作者: Yang, Hong

作者: Yang, Hong;Shi, Pengjun;Lu, Haiqiang;Wang, Huimin;Luo, Huiying;Huang, Huoging;Yang, Peilong;Yao, Bin

作者机构:

关键词: Neosartorya fischeri;Pichia pastoris;beta-Mannanase;Thermophilic;Broad pH stability

期刊名称:FOOD CHEMISTRY ( 影响因子:7.514; 五年影响因子:7.516 )

ISSN:

年卷期:

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收录情况: SCI

摘要: A new beta-mannanase gene, mart5P1, was cloned from the thermophilic fungus Neosartorya fischeri P1, and successfully expressed in Pichia pastoris. The predicted amino acid sequence of man5P1 consists of a putative 19-residue signal peptide at the N-terminus and a catalytic domain of glycoside hydrolase family 5. The purified recombinant Man5P1 (rMan5P1) was optimally active at pH 4.0 and 80 degrees C, and was acid and alkali tolerant, exhibiting >20% of the maximal activity at pH 2.0 and 9.0. rMan5P1 had better stability over a broad pH range of 2.0-12.0, and was highly thermostable at 60 C and below. The enzyme was highly active towards galactomannan and glucomannan, and exhibited classic endo-activity producing a mixture of mannooligosaccharides (MOS). Moreover, it had strong resistance to SDS and Ag* and proteases. The superior properties make Man5P1 a potential candidate for use in various industrial applications. (C) 2014 Elsevier Ltd. All rights reserved.

分类号: TS2`TS201.2

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