{"id":53289,"date":"2024-08-23T13:52:47","date_gmt":"2024-08-23T13:52:47","guid":{"rendered":"https:\/\/matis.is\/?p=53289"},"modified":"2024-08-23T13:52:48","modified_gmt":"2024-08-23T13:52:48","slug":"a-novel-glycoside-hydrolase-43-like-enzyme-from-clostridium-boliviensis-is-an-endo-xylanase-and-a-candidate-for-xylooligosaccharide-production-from-different-xylan-substrates","status":"publish","type":"post","link":"https:\/\/matis.is\/en\/greinar\/a-novel-glycoside-hydrolase-43-like-enzyme-from-clostridium-boliviensis-is-an-endo-xylanase-and-a-candidate-for-xylooligosaccharide-production-from-different-xylan-substrates\/","title":{"rendered":"A novel glycoside hydrolase 43-like enzyme from Clostridium boliviensis is an endo-xylanase and a candidate for xylooligosaccharide production from different xylan substrates"},"content":{"rendered":"<p>An uncharacterized gene encoding a glycoside hydrolase family 43-like enzyme from\u00a0<em>Clostridium boliviensis<\/em>\u00a0strain E-1 was identified from genomic sequence data, and the encoded enzyme,\u00a0<em>CbE1<\/em>Xyn43-l, was produced in\u00a0<em>Escherichia coli. CbE1<\/em>Xyn43-l (52.9 kDa) is a two-domain endo-\u03b2-xylanase consisting of a C-terminal CBM6 and a GH43-like catalytic domain. The positions of the catalytic dyad conserved in GH43, the catalytic base (Asp74), and proton donor (Glu240) were identified in alignments including GH43-enzymes of known 3D-structure from different subfamilies.\u00a0<em>CbE1<\/em>Xyn43-l is active at pH 7.0\u20139.0, with optimum temperature at 65\u00b0C, and a more than 7 days&#039; half-life in irreversible deactivation studies at this temperature. The enzyme hydrolyzed birchwood xylan, quinoa stalks glucuronoarabinoxylan, and wheat arabinoxylan with xylotriose and xylotetraose as major hydrolysis products.\u00a0<em>CbE1<\/em>Xyn43-l also released xylobiose from\u00a0<em>p<\/em>NPX<sub>2<\/sub>\u00a0with low turnover (<em>k<\/em><sub>cat<\/sub>\u00a0over 0.044 s<sup>\u22121<\/sup>) but was inactive on\u00a0<em>p<\/em>NPX, showing that a degree of polymerization of three (DP3) was the smallest hydrolyzable substrate. Divalent ions affected the specific activity on xylan substrates, which depending on the ion could be increased or decreased. In conclusion,\u00a0<em>CbE1<\/em>Xyn43-l from\u00a0<em>C. boliviensis<\/em>\u00a0strain E-1 is the first characterized member of a large group of homologous hypothetical proteins annotated as GH43-like and is a thermostable endo-xylanase, producing xylooligosaccharides of high DP (xylotriose and xylotetraose) producer.<\/p>","protected":false},"excerpt":{"rendered":"<p>An uncharacterized gene encoding a glycoside hydrolase family 43-like enzyme from\u00a0Clostridium boliviensis\u00a0strain E-1 was identified from genomic sequence data, and [&hellip;]<\/p>\n","protected":false},"author":3,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"template-greinar.php","format":"standard","meta":{"_acf_changed":false,"_uag_custom_page_level_css":"","site-sidebar-layout":"default","site-content-layout":"","ast-site-content-layout":"default","site-content-style":"default","site-sidebar-style":"default","ast-global-header-display":"","ast-banner-title-visibility":"","ast-main-header-display":"","ast-hfb-above-header-display":"","ast-hfb-below-header-display":"","ast-hfb-mobile-header-display":"","site-post-title":"","ast-breadcrumbs-content":"","ast-featured-img":"","footer-sml-layout":"","ast-disable-related-posts":"","theme-transparent-header-meta":"","adv-header-id-meta":"","stick-header-meta":"","header-above-stick-meta":"","header-main-stick-meta":"","header-below-stick-meta":"","astra-migrate-meta-layouts":"default","ast-page-background-enabled":"default","ast-page-background-meta":{"desktop":{"background-color":"var(--ast-global-color-5)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"tablet":{"background-color":"","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"mobile":{"background-color":"","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""}},"ast-content-background-meta":{"desktop":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"tablet":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"mobile":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""}},"footnotes":""},"categories":[2011],"tags":[],"class_list":["post-53289","post","type-post","status-publish","format-standard","hentry","category-greinar"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v27.4 - 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