ArticleBMC biotechnology2015
Expression of the Thermobifida fusca xylanase Xyn11A in Pichia pastoris and its characterization.
Article in BMC biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 42 citations in OpenAlex.
- An impact of N-glycosylation on biochemical properties of a recombinant α-amylase fromHeliyon · 2024Article
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- A thermostable and CBM2-linked GH10 xylanase fromFrontiers in bioengineering and biotechnology · 2022Article
- The Effects of Carbon Source and Growth Temperature on the Fatty Acid Profiles ofFrontiers in molecular biosciences · 2022Article
- Cloning, expression, and characterization of a recombinant xylanase from Bacillus sonorensis T6.PloS one · 2022Article
- Heterologous Expression of Lignocellulose-Modifying Enzymes in Microorganisms: Current Status.Molecular biotechnology · 2021Review
- In silico screening and experimental analysis of family GH11 xylanases for applications under conditions of alkaline pH and high temperature.Biotechnology for biofuels · 2020Article
- Removal of N-terminal tail changes the thermostability of the low-temperature-active exo-inulinase InuAGN25.Bioengineered · 2020Article
- Improving low-temperature activity and thermostability of exo-inulinase InuAGN25 on the basis of increasing rigidity of the terminus and flexibility of the catalytic domain.Bioengineered · 2020Article
- Production and characterization of functional wheat bran hydrolysate rich in reducing sugars, xylooligosaccharides and phenolic acids.Biotechnology reports (Amsterdam, Netherlands) · 2020Article
- Genome analysis of cellulose and hemicellulose degrading3 Biotech · 2020Article
- Novel Synergistic Mechanism for Lignocellulose Degradation by a Thermophilic Filamentous Fungus and a Thermophilic Actinobacterium Based on Functional Proteomics.Frontiers in microbiology · 2020Article
- Characterization of Two Endo-β-1, 4-Xylanases fromFrontiers in microbiology · 2018Article
- Article
- Enhancement of thermoalkaliphilic xylanase production by Pichia pastoris through novel fed-batch strategy in high cell-density fermentation.BMC biotechnology · 2017Article
- Characterization of Full-Length and Truncated Recombinant κ-Carrageenase Expressed inFrontiers in microbiology · 2017Article
- Enzymatic Degradation of Aromatic and Aliphatic Polyesters byFrontiers in microbiology · 2017Article
- Production and Partial Characterization of an Alkaline Xylanase from a Novel Fungus Cladosporium oxysporum.BioMed research international · 2016Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundXylan is a major component of plant cells and the most abundant hemicellulose. Xylanases degrade xylan into monomers by randomly cleaving β-1,4-glycosidic bonds in the xylan backbone, and have widespread potential applications in various industries. The purpose of our study was to clone and express the endoxylanase gene xynA of Thermobifida fusca YX in its native form and with a C-terminal histidine (His) tag in Pichia pastoris X-33. We analyzed and compared these two forms of the protein and examined their potential applications in various industries.
resultsThe xynA gene from T. fusca YX was successfully cloned and expressed using P. pastoris X-33. We produced a recombinant native form of the protein (rXyn11A) and a C-terminal His-tagged form of the desired protein (rXyn11A-(His)6). The specific activities of rXyn11A and rXyn11A-(His)6 in culture supernatants approached 149.4 and 133.4 U/mg, respectively. These activities were approximately 4- and 3.5-fold higher than those for the non-recombinant wild-type Xyn11A (29.3 U/mg). Following purification, the specific activities of rXyn11A and rXyn11A-(His)6 were 557.35 and 515.84 U/mg, respectively. The specific activity of rXyn11A was 8% higher than that of rXyn11A-(His)6. Both recombinant xylanases were optimally active at 80°C and pH 8.0, and exhibited greater than 60% activity between pH 6-9 and 60-80°C. They exhibited similar pH stability, while rXyn11A exhibited better thermostability; N-glycosylation enhanced the thermostability of both recombinant xylanases. The products of beechwood xylan hydrolyzed by both xylanases included xylobiose, xylotriose, xylotetraose and xylopentaose.
conclusionsThe C-terminal His tag had adverse effects when added to the Xyn11A protein. The thermostability of both recombinant xylanases was enhanced by N-glycosylation. Their stabilities at a high pH and temperature indicate their potential for application in various industries.
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