A thermophilic β-mannanase from Neosartorya fischeri P1 with broad pH stability and significant hydrolysis ability of various mannan polymers
作者： Hong Yang , Pengjun Shi , Haiqiang Lu , Huimin Wang , Huiying Luo
DOI: 10.1016/J.FOODCHEM.2014.10.022
关键词: Enzyme 、 Hydrolysis 、 Biochemistry 、 Glycoside hydrolase family 5 、 Pichia pastoris 、 Peptide sequence 、 Mannan 、 Biology 、 Thermophile 、 Glucomannan
摘要: A new β-mannanase gene, man5P1, was cloned from the thermophilic fungus Neosartorya fischeri P1, and successfully expressed in Pichia pastoris. The predicted amino acid sequence of man5P1 consists a putative 19-residue signal peptide at N-terminus catalytic domain glycoside hydrolase family 5. purified recombinant Man5P1 (rMan5P1) optimally active pH 4.0 80 °C, alkali tolerant, exhibiting >20% maximal activity 2.0 9.0. rMan5P1 had better stability over broad range 2.0-12.0, highly thermostable 60 °C below. enzyme towards galactomannan glucomannan, exhibited classic endo-activity producing mixture mannooligosaccharides (MOS). Moreover, it strong resistance to SDS Ag(+) proteases. superior properties make potential candidate for use various industrial applications.
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