Structural highlights
FunctionPublication Abstract from PubMedXylanase (EC 3.2.1.8) is a kind of enzymes that degrade xylan into xylose, which has been widely used in a variety of industrial applications. Particularly, xylanases from thermophilic microorganisms show distinct advantages in the industries which need high temperature conditions. The CoXynA gene, which is identified from thermophilic bacterium Caldicellulosiruptor owensensis, encoding a glycoside hydrolase family 10 xylanase, was overexpressed in Escherichia coli. The recombinant CoXynA showed optimal activity at 90 degrees C and pH 7. Its half-life is about 1 h at 80 degrees C. The activity of CoXynA was not affected by most cations. CoXynA showed distinct substrate specificities for beech wood xylan and birch wood xylan. The crystal structure of CoXynA was solved and the molecular dynamics simulation was performed for CoXynA. The relatively high thermostability of CoXynA is proposed to be the increased overall protein rigidity resulted from the shortened length and reduced fluctuation of Loop 7. Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis.,Liu X, Liu T, Zhang Y, Xin F, Mi S, Wen B, Gu T, Shi X, Wang F, Sun L J Agric Food Chem. 2017 Dec 13. doi: 10.1021/acs.jafc.7b03607. PMID:29236500[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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