{"id":38919,"date":"2021-06-09T15:52:53","date_gmt":"2021-06-09T15:52:53","guid":{"rendered":"https:\/\/matis.is\/?p=38919"},"modified":"2021-06-09T15:52:55","modified_gmt":"2021-06-09T15:52:55","slug":"immobilization-of-a-recombinant-escherichia-coli-producing-a-thermostable-alpha-l-rhamnosidase-creation-of-a-bioreactor-for-hydrolyses-of-naringen","status":"publish","type":"post","link":"https:\/\/matis.is\/en\/greinar\/immobilization-of-a-recombinant-escherichia-coli-producing-a-thermostable-alpha-l-rhamnosidase-creation-of-a-bioreactor-for-hydrolyses-of-naringen\/","title":{"rendered":"Immobilization of a recombinant Escherichia coli producing a thermostable alpha-L-rhamnosidase; creation of a bioreactor for hydrolyses or naringen"},"content":{"rendered":"<p>An \u03b1-l-rhamnosidase (EC 3.2.1.40) from a newly discovered\u00a0<a href=\"https:\/\/www.sciencedirect.com\/topics\/biochemistry-genetics-and-molecular-biology\/thermophilic-bacterium\">thermophilic bacterium<\/a>\u00a0was expressed in\u00a0<em>Escherichia coli<\/em>\u00a0BL21 DE3 pRIL cells. The cells were immobilized in Ca<sup>2+<\/sup>-alginate beads. The temperature of 50 \u00b0 C used in reactions, appeared to be sufficient for making the mesophilic strain porous enough for the substrate to access the cloned thermostable enzyme. Pretreatment of cells with heat or\u00a0<a href=\"https:\/\/www.sciencedirect.com\/topics\/biochemistry-genetics-and-molecular-biology\/lysozyme\">lysozyme<\/a>\u00a0prior to bead formation did not improve the results. The best cell concentration (w \/ w) for bead preparation was found to be 0.0192 g ml<sup>\u22121<\/sup>\u00a0and stability of beads increased if CaCl<sub>2<\/sub>\u00a0concentration in buffers and substrate was kept at 50 mM. In a 60 min assay, the optimal pH of the entrapped cells was found to be 7.8 and the optimal temperature 60 \u00b0 C. By packing the beads in a column, a\u00a0<a href=\"https:\/\/www.sciencedirect.com\/topics\/immunology-and-microbiology\/bioreactor\">bioreactor<\/a>\u00a0for production of l-rhamnose from naringin was created. Full degradation of 7.9 mM naringin could be reached by running the reactor at 1 ml min<sup>\u22121<\/sup>\u00a0at 50 \u00b0 C. The optimal running temperature of the reactor was found to be 50 \u00b0 C and the reactor was fully stable over 3 days at that temperature. On the fourth day, substrate degradation capacity had decreased by 10\u201315%.<\/p>\n\n\n\n<p><strong><a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0141022906004534\">Link to article<\/a><\/strong><\/p>","protected":false},"excerpt":{"rendered":"<p>An \u03b1-l-rhamnosidase (E.C. 3.2.1.40) from a newly discovered\u00a0thermophilic bacterium\u00a0was expressed in\u00a0Escherichia coli\u00a0BL21 DE3 pRIL cells. The cells were immobilized in [&hellip;]<\/p>\n","protected":false},"author":1,"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-38919","post","type-post","status-publish","format-standard","hentry","category-greinar"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v27.4 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Immobilization of a recombinant\u00a0Escherichia coli\u00a0producing a thermostable alpha-L-rhamnosidase; creation of a bioreactor for hydrolyses of naringen - Mat\u00eds<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/matis.is\/en\/greinar\/immobilization-of-a-recombinant-escherichia-coli-producing-a-thermostable-alpha-l-rhamnosidase-creation-of-a-bioreactor-for-hydrolyses-of-naringen\/\" \/>\n<meta property=\"og:locale\" content=\"en_GB\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Immobilization of a recombinant\u00a0Escherichia coli\u00a0producing a thermostable alpha-L-rhamnosidase; creation of a bioreactor for hydrolyses of naringen - Mat\u00eds\" \/>\n<meta property=\"og:description\" content=\"An \u03b1-l-rhamnosidase (E.C. 3.2.1.40) from a newly discovered\u00a0thermophilic bacterium\u00a0was expressed in\u00a0Escherichia coli\u00a0BL21 DE3 pRIL cells. 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