ArticleBMC biotechnology2009
Expression of endo-1, 4-beta-xylanase from Trichoderma reesei in Pichia pastoris and functional characterization of the produced enzyme.
Article in BMC biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 72 citations in OpenAlex.
- Review of Xylanases: Sources, Engineering and Biotechnological Use.Microorganisms · 2026Review
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- Exploiting xylan as sugar donor for the synthesis of an antiproliferative xyloside using an enzyme cascade.Microbial cell factories · 2019Article
- Efficient Expression of Xylanase by Codon Optimization and Its Effects on the Growth Performance and Carcass Characteristics of Broiler.Animals : an open access journal from MDPI · 2019Article
- Characterization of novel lignocellulose-degrading enzymes from the porcupine microbiome using synthetic metagenomics.PloS one · 2019Article
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- Expression, Docking, and Molecular Dynamics of Endo-BioMed research international · 2017Article
- Expressing accessory proteins in cellulolyticBiotechnology for biofuels · 2017Article
- Codon Optimization of the "Bos Taurus Chymosin" Gene for the Production of Recombinant Chymosin in Pichia pastoris.Molecular biotechnology · 2016Article
- Expression of the Thermobifida fusca xylanase Xyn11A in Pichia pastoris and its characterization.BMC biotechnology · 2015Article
- Isolation and cultivation of xylanolytic and cellulolytic Sarocladium kiliense and Trichoderma virens from the gut of the termite Reticulitermes santonensis.Environmental science and pollution research international · 2015Article
- Highly Thermostable Xylanase Production from A Thermophilic Geobacillus sp. Strain WSUCF1 Utilizing Lignocellulosic Biomass.Frontiers in bioengineering and biotechnology · 2015Article
- Identification of an endo-1,4-beta-xylanase of Ustilago maydis.BMC biotechnology · 2013Article
- Insights into exo- and endoglucanase activities of family 6 glycoside hydrolases from Podospora anserina.Applied and environmental microbiology · 2013Article
- Characterization and pH-dependent substrate specificity of alkalophilic xylanase from Bacillus alcalophilus.Journal of industrial microbiology & biotechnology · 2012Article
- Achieving efficient protein expression in Trichoderma reesei by using strong constitutive promoters.Microbial cell factories · 2012Article
- Optimization of a synthetic mixture composed of major Trichoderma reesei enzymes for the hydrolysis of steam-exploded wheat straw.Biotechnology for biofuels · 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
- Biorefining of wood: combined production of ethanol and xylanase from waste fiber sludge.Journal of industrial microbiology & biotechnology · 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
backgroundIn recent years, xylanases have attracted considerable research interest because of their potential in various industrial applications. The yeast Pichia pastoris can neither utilize nor degrade xylan, but it possesses many attributes that render it an attractive host for the expression and production of industrial enzymes.
resultsThe Xyn2 gene, which encodes the main Trichoderma reesei Rut C-30 endo-beta-1, 4-xylanase was cloned into the pPICZalphaA vector and expressed in Pichia pastoris. The selected P. pastoris strains produced as 4,350 nkat/ml beta-xylanase under the control of the methanol inducible alcohol oxidase 1 (AOX1) promoter. The secreted recombinant Xyn2 was estimated by SDS-PAGE to be 21 kDa. The activity of the recombinant Xyn2 was highest at 60 degrees C and it was active over a broad range of pH (3.0-8.0) with maximal activity at pH 6.0. The enzyme was quite stable at 50 degrees C and retained more than 94% of its activity after 30 mins incubation at this temperature. Using Birchwood xylan, the determined apparent Km and kcat values were 2.1 mg/ml and 219.2 S-1, respectively. The enzyme was highly specific towards xylan and analysis of xylan hydrolysis products confirmed as expected that the enzyme functions as endo-xylanase with xylotriose as the main hydrolysis products. The produced xylanase was practically free of cellulolytic activity.
conclusionThe P. pastoris expression system allows a high level expression of xylanases. Xylanase was the main protein species in the culture supernatant, and the functional tests indicated that even the non-purified enzyme shows highly specific xylanase activity that is free of cellulolytic side acitivities. Therefore, P pastoris is a very useful expression system when the goal is highly specific and large scale production of glycosyl hydrolases.
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