ArticleWorld journal of microbiology & biotechnology2012
Molecular cloning and heterologous expression of an acid stable xylanase gene from Alternaria sp. HB186.
Article in World journal of microbiology & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- Multi-parameter optimization of recombinant protein secretion in Bacillus subtilis: a review.Microbial cell factories · 2026Review
- Tunnel engineering to accelerate product release for better biomass-degrading abilities in lignocellulolytic enzymes.Biotechnology for biofuels · 2019Article
- High copy and stable expression of the xylanase XynHB in Saccharomyces cerevisiae by rDNA-mediated integration.Scientific reports · 2017Article
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6 authors.
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Abstract
A new xylanase gene, named xyn186, was cloned by the genome-walking PCR method from the Alternaria sp. HB186. The sequence of xyn186 contains a 748 bp open reading frame separated by one intron with the size of 52 bp. The cDNA was obtained by DpnI-mediated intron deletion. The cDNA was cloned into pHBM905A and transformed into Pichia pastoris GS115 to screen xylanase-secreting transformants on RBB-xylan plates. The molecular mass of the enzyme was estimated to be 23 kDa on SDS-PAGE. The optimal pH and temperature of the purified enzyme is 6 and 50°C, respectively. The K (m) and V (max) valued for birchwood xylan are 1.404 mg ml(-1) and 0.2748 mmol min(-1) mg(-1), respectively. The inhibitory effects of various metal ions were investigated, Cu(2+) and Hg(2+) ions inhibited most of the enzyme activity. The gene copy number of xyn186 in the genome of P. pastoris was estimated as two by the Real-time PCR. To date, xyn186 gene is the first xylanase gene cloned from the genus Alternaria.
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