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Heterologous expression of endo-1,4-β-xylanase a from Schizophyllum commune in Pichia pastoris and functional characterization of the recombinant enzyme

Song, Y.; Lee, Y.G.; Choi, I.S.; Lee, K.H.; Cho, E.J.; Bae, H.-J.

Enzyme and Microbial Technology 52(3): 170-176

2013


ISSN/ISBN: 1879-0909
PMID: 23410928
DOI: 10.1016/j.enzmictec.2012.12.012
Accession: 036708083

Endo-1,4-β-xylanase A (XynA) from Schizophyllum commune was cloned into pPCZαA and expressed in Pichia pastoris GS115. The open reading frame of the xynA gene is composed of 684 bp, encoding 278 amino acids with a molecular weight of 26 kDa. Based on sequence similarity, XynA belongs to the CAZy glycoside hydrolase family 11. The optimal activity of XynA was at pH 5 and 50 °C on beechwood xylan. Under these conditions, the K(m), V(max) and specific activity of XynA were 5768 units mg(-1), 4 mg ml(-1) and 9000 μmol min(-1)mg(-1), respectively. XynA activity was enhanced in the presence of cations, such as K(+), Na(+), Li(2+), Cd(2+), and Co(2+). However, in the presence of EDTA, Hg(2+) and Fe(3+), xylanase activity was significantly inhibited. This enzyme effectively degraded approximately 45% of unsubstituted xylans in the cell wall from poplar stems. The high level of XynA activity might increase the yield of enzyme hydrolysis from biomass. Thus, XynA could be used as a major component of a lignocellulosic degrading enzyme cocktail.

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