期刊
FOOD CHEMISTRY
卷 173, 期 -, 页码 283-289出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2014.10.022
关键词
Neosartorya fischeri; Pichia pastoris; beta-Mannanase; Thermophilic; Broad pH stability
资金
- National High Technology Research and Development Program of China [2012AA022208]
- National Science Foundation [31225026]
- National Science and Technology Support Program [2013BAD10B01-2]
- China Modern Agriculture Research System [CARS-42]
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.
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