The Complete Genome Sequence of a Bacterial Strain with High Alkalic Xylanase Activity Isolated from the Sludge Near a P
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The Complete Genome Sequence of a Bacterial Strain with High Alkalic Xylanase Activity Isolated from the Sludge Near a Papermill Si Chen1 · Hao Feng2 · Xin Li1 · Hong‑jun Chao1 · Jing Wu1 · Jun Liu1 · Wen‑jun Zhu1 · Da‑zhong Yan1 Received: 30 June 2020 / Accepted: 23 September 2020 © Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract Many organisms secrete xylanase, an import group of proteins hydrolyzing xylan, and thus are able to use xylan as their carbon source. In this study, we sequenced the whole genome of a bacterial strain, YD01, which was isolated from the sludge near the sewage discharge outlet of a papermill and showed high alkalic xylanase activity. Its genome consists of a chromosome and two plasmids. Six rRNA genes, 46 tRNA genes, 3136 CDSs as well as 955 repetitive sequences were predicted. 3046 CDSs were functionally annotated. Phylogenetic analysis on 16S rRNA shows that YD01 is a new species in Microbacterium genus and is taxonomically close to M. jejuense THG-C31T and M. kyungheense THG-C26T. A comparative study on phylogenetic trees of 16S rRNA and xylanase genes suggests that xylanase genes in YD01 may originate from horizontal gene transfer instead of ancestral gene duplication.
Introduction Xylanase is a group of enzymes that hydrolyze xylan, a polysaccharide. Xylan comes from multiple sources and thus has multiplicity and complexity in its structure. For xylan to be thoroughly degraded, various enzymes are needed to work cooperatively. Xylanase mainly consists of the following three categories. (1) endo-β-1,4-d-xylanase (EC 3.2.1.8). This enzyme is the key xylanase that hydrolyzes the glycosidic bonds in xylan’s main chain and produces oligosaccharides. (2) β-d-xylosidase (EC 3.2.1.37). This enzyme acts on xylooligosaccharides and releases xylose. (3) Other glycoside hydrolases including α-l-arabinofuranosidases (EC 3.2.1.55, EC 3.2.1.99), α- d -glucuronidases (EC 3.2.239), acetylxylan esterases (EC 3.2.72), and phenol aid esterases (EC 3.2.73) [1]. Enzymes classified as Xylanase belong to several glycoside hydrolase families [2]. Family Electronic supplementary material The online version of this article (https://doi.org/10.1007/s00284-020-02227-5) contains supplementary material, which is available to authorized users. * Da‑zhong Yan [email protected] 1
School of Biology and Pharmaceutical Engineering, Wuhan Polytechnic University, Wuhan 430023, China
Jiangsu Yanghe Brewery Joint-Stock Co., Ltd., Suqian 223800, Jiangsu, China
2
10 xylanases have high molecular weight, complex structure, and low isoelectric points. They degrade xylan into oligosaccharides. Family 11 xylanases have low molecular weight and low isoelectric points. They act on highly specific substrates and produce xylose [3–5]. In addition, some enzymes are also found to have xylanase activities in glycoside hydrolase families 5, 7, 8, 16, 26, 43, 52, and 62 [2]. In structure, some xylanases consist of only catalytical domains [6], while other xylanases may have additional domains, su
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