ArticleWorld journal of microbiology & biotechnology2013
Characterization and constitutive expression of an acidic mesophilic endo-1,4-β-D-xylanohydrolase with high thermotolerance and catalytic efficiency in Pichia pastoris.
Article in World journal of microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 17 citations in OpenAlex.
- Engineering Saccharomyces cerevisiae for targeted hydrolysis and fermentation of glucuronoxylan through CRISPR/Cas9 genome editing.Microbial cell factories · 2024Article
- Review
- Improvement in catalytic activity and thermostability of a GH10 xylanase and its synergistic degradation of biomass with cellulase.Biotechnology for biofuels · 2019Article
- Article
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5 authors at 1 institution in 1 country.
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Abstract
A putative endo-1,4-β-D-xylanohydrolase gene xyl11 from Aspergillus niger, encoding a 188-residue xylanase of glycosyl hydrolase family 11, was constitutively expressed in Pichia pastoris. The recombinant Xyl11 exhibited optimal activity at pH 5.0 and 50 °C, and displayed more than 68 % of the maximum activity over the temperature range 35-65 °C and 33 % over the pH range 2.2-7.0. It maintained more than 40 % of the original activity after incubation at 90 °C (pH 5.0) for 10 min and more than 75 % of the original activity after incubation at pH 2.2-11.0 (room temperature) for 2 h. The specific activity, K m and V max of purified Xyl11 were 22,253 U mg(-1), 6.57 mg ml(-1) and 51,546.4 μmol min(-1) mg(-1). It could degrade xylan to a series of xylooligosaccharides and no xylose was detected. The recombinant enzyme with high stability and catalytic efficiency could work over wide ranges of pH and temperature and thus has the potential for various industrial applications.
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