A novel cold-active xylanase gene from the environmental DNA of goat rumen contents: direct cloning, expression and enzyme characterization.

@article{Wang2011ANC,
  title={A novel cold-active xylanase gene from the environmental DNA of goat rumen contents: direct cloning, expression and enzyme characterization.},
  author={Guozeng Wang and Huiying Luo and Yaru Wang and Huo-qing Huang and Pengjun Shi and Peilong Yang and Kun Meng and Yingguo Bai and Bin Yao},
  journal={Bioresource technology},
  year={2011},
  volume={102 3},
  pages={
          3330-6
        }
}

Molecular and biochemical characterization of a novel cold-active and metal ion-tolerant GH10 xylanase from frozen soil

TLDR
Xyn27 exhibited superior metal ion tolerance than other GH10 cold-active xylanases, being tolerant to most metal ions and organic solvents, and significantly enhanced by Ca2+, Mn2+ and Zn2+ metal ions.

Biochemical analysis of a highly specific, pH stable xylanase gene identified from a bovine rumen-derived metagenomic library

TLDR
An understanding of the mechanism and the substrate specificity of this enzyme is provided serving as a starting point for directed evolution of Xyn10N18 and subsequent downstream use in industry.

Characterization of a Novel Xylanase Gene from Rumen Content of Hu Sheep

TLDR
The novel xylanase gene, XYN-LXY, was cloned from a metagenomic fosmid library and exhibited deep degradation effects on the xylan substrate, which were rarely observed with endo-xylanase, making it a promising candidate for industrial application, especially in biofuel production.

A novel cold-active xylanase from the cellulolytic myxobacterium Sorangium cellulosum So9733-1: gene cloning, expression, and enzymatic characterization

The cellulolytic myxobacterium Sorangium cellulosum is able to efficiently degrade many kinds of polysaccharides, but none of the enzymes involved have been characterized. In this paper, a xylanase

Isolation of a Novel Cold-Active Family 11 Xylanase from the Filamentous Fungus Bispora antennata and Deletion of its N-Terminal Amino Acids on Thermostability

TLDR
A new factor affecting the thermostability of cold-active xylanase of family 11 was identified, and the coding gene (xyn11) was cloned and successfully expressed in Pichia pastoris.

Molecular and biochemical characterization of a novel intracellular low-temperature-active xylanase.

  • Junpei ZhouY. Dong Zunxi Huang
  • Biology, Engineering
    Journal of microbiology and biotechnology
  • 2012
TLDR
The above mechanism of structural adaptation for low-temperature activity of intracellular endoxylanase rXynAHJ2 is different from that of GH 10 extracellular low-Temperature-active endxylanases.

Molecular and Biochemical Characterization of a Novel Xylanase from Massilia sp. RBM26 Isolated from the Feces of Rhinopithecus bieti.

TLDR
This paper is the first to report a xylanase (XynRBM26) belonging to the glycosyl hydrolase family (GH10) from the genus Massilia with salt tolerance, which could maintain 86% activity in 5 M NaCl, and is applicable to high-salt food and seafood processing, as well as other high-Salt environmental biotechnological fields.

Cloning, expression and characterization of a novel cold-active and halophilic xylanase from Zunongwangia profunda

TLDR
This may be the first report concerning a cold-adapted xylanase from a non-halophilic species that displays the highest activity at a NaCl concentration range from 3 to 5 M and the features of cold activity and salt tolerance suggest the potential application of XynA in the food industry and bioethanol production from marine seaweeds.

Molecular and Biochemical Characterization of a Novel Multidomain Xylanase from Arthrobacter sp. GN16 Isolated from the Feces of Grus nigricollis

A novel glycosyl hydrolase family 10 (GH 10) xylanase (XynAGN16), consisting of five domains, was revealed from the genome sequence of Arthrobacter sp. GN16 isolated from the feces of Grus
...

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TLDR
XynA is a strict endo-β-1,4-xylanase with a demand of at least four sugar moieties for effective cleavage, suggesting its potential in xylo-oligosaccharides production and may be the first salt-tolerant xylanase reported.

Molecular and biochemical characterization of a novel xylanase from the symbiotic Sphingobacterium sp. TN19

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A xylanase-encoding gene, designated xynA19, was cloned from Sphingobacterium sp. TN19—a symbiotic bacterium isolated from the gut of Batocera horsfieldi larvae—and expressed in Escherichia coli BL21

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A soil-derived metagenomic library containing 24,000 transformants was constructed with an efficient strategy for cloning xylanase genes and a gene encoding of XynH able to hydrolyze xylan was obtained, revealing that this enzyme is a new member in the family 10 of xylanases.

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TLDR
The mature protein of XYLD showed high sequence similarity to both glycosyl hydrolase (GH) families 5 and 30 but was more homologous to members of GH 30 based on phylogenetic analysis.

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TLDR
A novel cold-adaptive xylanolytic Penicillium strain FS010 was isolated from Yellow sea sediments and secreted the cold-active xylanase (XYL) showing high hydrolytic activities at low temperature and high sensitivity to high temperature.

Cloning and characterization of a cold-active xylanase enzyme from an environmental DNA library

TLDR
Cloned a xylanase gene (xyn8) from an environmental genomic DNA library and purified enzyme was thermolabile, had an activity temperature optimum of 20°C on native xylan substrate, and retained significant activity at lower temperatures.

Cloning of a Bacillus sp. BP-23 gene encoding a xylanase with high activity against aryl xylosides.

TLDR
Xylanase B showed high specific activity on aryl xylosides, probably as a result of the transxylosidase activity detected, and xylobiose was not hydrolyzed by the enzyme.

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TLDR
This novel xylanase, isolated from the Antarctic bacterium Pseudoalteromonas haloplanktis, is not homologous to family 10 or 11 enzymes but has 20–30% identity with family 8 members and NMR analysis shows that this enzyme hydrolyzes with inversion of anomeric configuration, in contrast to other known xylanases which are retaining.

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TLDR
The structure of IXT6 was compared with the highly homologous extracellular xylanase XT6, revealing a number of structural differences between the active sites of the two enzymes, which may account for the significant differences in the substrate specificities of these otherwise very similar enzymes.