ArticleMolecular biology reports2020
Cloning, expression and characterization of C. crescentus xynA2 gene and application of Xylanase II in the deconstruction of plant biomass.
Article in Molecular biology reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Cell-Surface and Periplasmic Deconstruction of Xylan by Oligotrophic Bacterium Caulobacter vibrioides.Environmental microbiology · 2026Article
- Cloning, heterologus expression and characterization of a thermophilic and salt tolerant GH11 xylanase from Allostreptomyces psammosilenae YIM DR4008Antonie van Leeuwenhoek · 2025Article
- BioengineeringMicroorganisms · 2025Article
- Biopolishing of denim by the recombinant xylanase II of Caulobacter crescentus.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Characterization of a novel GH10 alkali-thermostable xylanase from a termite microbiome.Bioresources and bioprocessing · 2022Article
- Targeted genome editing of plants and plant cells for biomanufacturing.Transgenic research · 2021Review
- Co-production of Xylooligosaccharides and Xylose From Poplar Sawdust by Recombinant Endo-1,4-β-Xylanase and β-Xylosidase Mixture Hydrolysis.Frontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Biotechnology offers innovative alternatives for industrial bioprocesses mainly because it uses enzymes that biodegrade the hemicellulose releasing fermentable sugars. Caulobacter crescentus (C. crescentus) has seven genes responsible for xylanolytic cleavage, 5 to β-xylosidases (EC 3.2.1.37) and 2 for endoxylanases, like xynA2 (CCNA_03137) that encodes Xylanase II (EC 3.2.1.8) of the glycohydrolases-GH10 group. The xynA2 gene was amplified by PCR, cloned into the pTrcHisA vector e efficiently overexpressed in E. coli providing a His-tag fusion protein. Recombinant xylanase (XynA2) was purified by affinity chromatography using a nickel sepharose column and exhibited a single 43 kDa band on SDS-PAGE gel. XynA2 showed an optimum alkaline pH (8) and stability at alkaline pH for 24 h. Although C. crescentus is mesophilic, XynA2 has optimum temperature of 60 °C and is thermo-resistance at 65 °C. XynA maintains 66% of the enzymatic activity at high temperatures (90 °C) without being denatured.The enzyme displayed a xylanolitic activity free of cellulase to xylan from beechwood and it was not inhibited in the presence of 50 μmol mL
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