ArticleMolecular biology reports2011
Heterologous expression of a gene for thermostable xylanase from Chaetomium thermophilum in Pichia pastoris GS115.
Article in Molecular biology reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 35 citations in OpenAlex.
- Screening, Characterization and Comparison of Endoglucanases/Xylanases from Thermophilic Fungi: AInternational journal of molecular sciences · 2025Article
- Identification and Characterization of a Novel Hyperthermostable Bifunctional Cellobiohydrolase- Xylanase Enzyme for Synergistic Effect With Commercial Cellulase on Pretreated Wheat Straw Degradation.Frontiers in bioengineering and biotechnology · 2020Article
- Scl gene construction, expression and effect on hemangioma.Molecular biology reports · 2013Article
- Cloning, Expression, and Characterization of an GHF 11 Xylanase from Aspergillus niger XZ-3S.Indian journal of microbiology · 2012Article
- Cloning, expression, and characterization of an alkaline thermostable GH11 xylanase from Thermobifida halotolerans YIM 90462T.Journal of industrial microbiology & biotechnology · 2012Article
- Expression, purification and characterization of low-glycosylation influenza neuraminidase in α-1,6-mannosyltransferase defective Pichia pastoris.Molecular biology reports · 2012Article
- A novel apoptosis correlated molecule: expression and characterization of protein Latcripin-1 from Lentinula edodes C(91-3).International journal of molecular sciences · 2012Article
- High expression of recombinant Streptomyces sp. S38 xylanase in Pichia pastoris by codon optimization and analysis of its biochemical properties.Molecular biology reports · 2011Article
- Inducible expression of calreticulin-N58 in Pichia pastoris by high density cell culture.Molecular biology reports · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We studied heterologous expression of xylanase 11A gene of Chaetomium thermophilum in Pichia pastoris and characterized the thermostable nature of the purified gene product. For this purpose, the xylanase 11A gene of C. thermophilum was cloned in P. pastoris GS115 under the control of AOX1 promoter. The maximum extracellular activity of recombinant xylanase (xyn698: gene with intron) was 15.6 U ml(-1) while that of recombinant without intron (xyn669) was 1.26 U ml(-1) after 96 h growth. The gene product was purified apparently to homogeneity level. The optimum temperature of pure recombinant xylanase activity was 70°C and the enzyme retained its 40.57% activity after incubation at 80°C for 10 min. It exhibited quite lower demand of activation energy, enthalpy, Gibbs free energy, entropy, and xylan binding energy during substrate hydrolysis than that required by that of the donor, thus indicating its thermostable nature. pH-dependent catalysis showed that it was quite stable in a pH range of 5.5-8.5. This revealed that gene was successfully processed in P. pastoris and remained heat stable and may qualify for its potential use in paper and pulp and animal feed applications.
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