ArticleMolecular biology reports2011
High expression of recombinant Streptomyces sp. S38 xylanase in Pichia pastoris by codon optimization and analysis of its biochemical properties.
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 11 papers.
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11 citing papers in PubMed, 29 citations in OpenAlex.
- Cloning, expression, and characterization of a recombinant xylanase from Bacillus sonorensis T6.PloS one · 2022Article
- Pichia pastoris: A highly successful expression system for optimal synthesis of heterologous proteins.Journal of cellular physiology · 2020Review
- Trends in recombinant protein use in animal production.Microbial cell factories · 2017Review
- Homologous constitutive expression of Xyn III in Trichoderma reesei QM9414 and its characterization.Folia microbiologica · 2014Article
- A non-ionic surfactant reduces the induction time and enhances expression levels of bubaline somatotropin in Pichia pastoris.Molecular biology reports · 2014Article
- Identification of a novel fumarase C from Streptomyces lividans TK54 as a good candidate for L-malate production.Molecular biology reports · 2014Article
- Codon optimisation improves the expression of Trichoderma viride sp. endochitinase in Pichia pastoris.Scientific reports · 2013Article
- Purification, characterization of GH11 endo-β-1,4-xylanase from thermotolerant Streptomyces sp. SWU10 and overexpression in Pichia pastoris KM71H.Molecular biotechnology · 2013Article
- Purification and characterization of a novel laccase from Coprinus cinereus and decolorization of different chemically dyes.Molecular biology reports · 2013Article
- Secretory expression and characterization of a soluble laccase from the Ganoderma lucidum strain 7071-9 in Pichia pastoris.Molecular biology reports · 2012Article
- Synthetic biology: an emerging research field in China.Biotechnology advancesReview
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5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In recent years, the biotechnological use of xylanases has grown remarkably. To efficiently produce xylanase for food processing and other industry, a codon-optimized recombinant xylanase gene from Streptomyces sp. S38 was synthesized and extracellularly expressed in Pichia pastoris under the control of AOX1 promoter. SDS-PAGE and activity assay demonstrated that the molecular mass of the recombinant xylanase was estimated to be 25 kDa, the optimum pH and optimum temperature were 5.5 and 50°C, respectively. In shake flask culture, the specific activity of the xylanase activity was 5098.28 U/mg. The K ( m ) and V ( max ) values of recombinant xylanase were 11.0 mg/ml and 10000 μmol min(-1) mg(-1), respectively. In the presence of metal ions such as Ca(2+), Cu(2+), Cr(3+) and K(+), the activity of the enzyme increased. However, strong inhibition of the enzyme activity was observed in the presence of Hg(2+). This is the first report on the expression properties of a recombinant xylanase gene from the Streptomyces sp. S38 using Pichia pastoris. The attractive biochemical properties of the recombinant xylanase suggest that it may be a useful candidate for variety of commercial applications.
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