These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: A thermophilic β-mannanase from Neosartorya fischeri P1 with broad pH stability and significant hydrolysis ability of various mannan polymers.
    Author: Yang H, Shi P, Lu H, Wang H, Luo H, Huang H, Yang P, Yao B.
    Journal: Food Chem; 2015 Apr 15; 173():283-9. PubMed ID: 25466024.
    Abstract:
    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 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 °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.
    [Abstract] [Full Text] [Related] [New Search]