Stabilization of Nocardia EH1 epoxide hydrolase by immobilization

A partially purified epoxide hydrolase from Nocardia EH1 was stabilized by immobilization through ionic binding onto DEAE-cellulose. This biocatalyst showed more than twice the activity (225 %) of that of the free enzyme albeit at a marginal reduction in enantioselectivity. The addition of the nonio...

Full description

Saved in:
Bibliographic Details
Published in:Biotechnology letters 1998-04, Vol.20 (4), p.373-377
Main Authors: KROUTIL, W, ORRU, R. V. A, FABER, K
Format: Article
Language:English
Subjects:
Binding sites
Biological and medical sciences
Biotechnology
Cellulose
Fundamental and applied biological sciences. Psychology
Immobilization of enzymes and other molecules
Immobilization techniques
Ions
Methods. Procedures. Technologies
Nocardia
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c323t-99bf00b369b69cc47a3945b53d55c1195f15b6ff02f318f35d6281a4befde893
cites
container_end_page 377
container_issue 4
container_start_page 373
container_title Biotechnology letters
container_volume 20
creator KROUTIL, W
ORRU, R. V. A
FABER, K
description A partially purified epoxide hydrolase from Nocardia EH1 was stabilized by immobilization through ionic binding onto DEAE-cellulose. This biocatalyst showed more than twice the activity (225 %) of that of the free enzyme albeit at a marginal reduction in enantioselectivity. The addition of the nonionic detergent Triton X-100 during the immobilization further enhanced the stability as indicated by a dramatic shift in the temperature optimum from 35 to 45°C. The stabilized immobilized biocatalyst could be successfully employed in repeated batch reactions (residual activity of 55% after five cycles), which was not the case for whole cell reactions (residual activity ≤10 %). © Rapid Science Ltd. 1998[PUBLICATION ABSTRACT]
doi_str_mv 10.1023/A:1005379314104
format article
fullrecord <record><control><sourceid>proquest_pasca</sourceid><recordid>TN_cdi_proquest_miscellaneous_17217473</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>17217473</sourcerecordid><originalsourceid>FETCH-LOGICAL-c323t-99bf00b369b69cc47a3945b53d55c1195f15b6ff02f318f35d6281a4befde893</originalsourceid><addsrcrecordid>eNpdzs1LAzEQBfAgCtbq2esi4m01k8nHxlsp1QpFD_a-JNkEU3abutmC9a93wYLgaeDxe48h5BroPVCGD7NHoFSg0ggcKD8hExAKS6mUPCUTOoal4Jqdk4ucN5RSraiakNn7YGxs47cZYtoWKRSvyZm-iaZYLKHwu_QVG198HJo-tSb7wh6K2HXpr3NJzoJps7863ilZPy3W82W5ent-mc9WpUOGQ6m1DZRalNpK7RxXBjUXVmAjhAPQIoCwMgTKAkIVUDSSVWC49aHxlcYpufud3fXpc-_zUHcxO9-2ZuvTPtegGCiucIQ3_-Am7fvt-FqtUFaMS6hGdHtEJjvTht5sXcz1ro-d6Q81YwyY5PgD1U5khw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>736824618</pqid></control><display><type>article</type><title>Stabilization of Nocardia EH1 epoxide hydrolase by immobilization</title><source>Springer Link</source><creator>KROUTIL, W ; ORRU, R. V. A ; FABER, K</creator><creatorcontrib>KROUTIL, W ; ORRU, R. V. A ; FABER, K</creatorcontrib><description>A partially purified epoxide hydrolase from Nocardia EH1 was stabilized by immobilization through ionic binding onto DEAE-cellulose. This biocatalyst showed more than twice the activity (225 %) of that of the free enzyme albeit at a marginal reduction in enantioselectivity. The addition of the nonionic detergent Triton X-100 during the immobilization further enhanced the stability as indicated by a dramatic shift in the temperature optimum from 35 to 45°C. The stabilized immobilized biocatalyst could be successfully employed in repeated batch reactions (residual activity of 55% after five cycles), which was not the case for whole cell reactions (residual activity ≤10 %). © Rapid Science Ltd. 1998[PUBLICATION ABSTRACT]</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1023/A:1005379314104</identifier><identifier>CODEN: BILED3</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Binding sites ; Biological and medical sciences ; Biotechnology ; Cellulose ; Fundamental and applied biological sciences. Psychology ; Immobilization of enzymes and other molecules ; Immobilization techniques ; Ions ; Methods. Procedures. Technologies ; Nocardia</subject><ispartof>Biotechnology letters, 1998-04, Vol.20 (4), p.373-377</ispartof><rights>1998 INIST-CNRS</rights><rights>Kluwer Academic Publishers 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c323t-99bf00b369b69cc47a3945b53d55c1195f15b6ff02f318f35d6281a4befde893</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=2221264$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>KROUTIL, W</creatorcontrib><creatorcontrib>ORRU, R. V. A</creatorcontrib><creatorcontrib>FABER, K</creatorcontrib><title>Stabilization of Nocardia EH1 epoxide hydrolase by immobilization</title><title>Biotechnology letters</title><description>A partially purified epoxide hydrolase from Nocardia EH1 was stabilized by immobilization through ionic binding onto DEAE-cellulose. This biocatalyst showed more than twice the activity (225 %) of that of the free enzyme albeit at a marginal reduction in enantioselectivity. The addition of the nonionic detergent Triton X-100 during the immobilization further enhanced the stability as indicated by a dramatic shift in the temperature optimum from 35 to 45°C. The stabilized immobilized biocatalyst could be successfully employed in repeated batch reactions (residual activity of 55% after five cycles), which was not the case for whole cell reactions (residual activity ≤10 %). © Rapid Science Ltd. 1998[PUBLICATION ABSTRACT]</description><subject>Binding sites</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cellulose</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immobilization of enzymes and other molecules</subject><subject>Immobilization techniques</subject><subject>Ions</subject><subject>Methods. Procedures. Technologies</subject><subject>Nocardia</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNpdzs1LAzEQBfAgCtbq2esi4m01k8nHxlsp1QpFD_a-JNkEU3abutmC9a93wYLgaeDxe48h5BroPVCGD7NHoFSg0ggcKD8hExAKS6mUPCUTOoal4Jqdk4ucN5RSraiakNn7YGxs47cZYtoWKRSvyZm-iaZYLKHwu_QVG198HJo-tSb7wh6K2HXpr3NJzoJps7863ilZPy3W82W5ent-mc9WpUOGQ6m1DZRalNpK7RxXBjUXVmAjhAPQIoCwMgTKAkIVUDSSVWC49aHxlcYpufud3fXpc-_zUHcxO9-2ZuvTPtegGCiucIQ3_-Am7fvt-FqtUFaMS6hGdHtEJjvTht5sXcz1ro-d6Q81YwyY5PgD1U5khw</recordid><startdate>19980401</startdate><enddate>19980401</enddate><creator>KROUTIL, W</creator><creator>ORRU, R. V. A</creator><creator>FABER, K</creator><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7QO</scope></search><sort><creationdate>19980401</creationdate><title>Stabilization of Nocardia EH1 epoxide hydrolase by immobilization</title><author>KROUTIL, W ; ORRU, R. V. A ; FABER, K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c323t-99bf00b369b69cc47a3945b53d55c1195f15b6ff02f318f35d6281a4befde893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Binding sites</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cellulose</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immobilization of enzymes and other molecules</topic><topic>Immobilization techniques</topic><topic>Ions</topic><topic>Methods. Procedures. Technologies</topic><topic>Nocardia</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KROUTIL, W</creatorcontrib><creatorcontrib>ORRU, R. V. A</creatorcontrib><creatorcontrib>FABER, K</creatorcontrib><collection>Pascal-Francis</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical &amp; Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering collection</collection><collection>ProQuest Central Basic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KROUTIL, W</au><au>ORRU, R. V. A</au><au>FABER, K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stabilization of Nocardia EH1 epoxide hydrolase by immobilization</atitle><jtitle>Biotechnology letters</jtitle><date>1998-04-01</date><risdate>1998</risdate><volume>20</volume><issue>4</issue><spage>373</spage><epage>377</epage><pages>373-377</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><coden>BILED3</coden><abstract>A partially purified epoxide hydrolase from Nocardia EH1 was stabilized by immobilization through ionic binding onto DEAE-cellulose. This biocatalyst showed more than twice the activity (225 %) of that of the free enzyme albeit at a marginal reduction in enantioselectivity. The addition of the nonionic detergent Triton X-100 during the immobilization further enhanced the stability as indicated by a dramatic shift in the temperature optimum from 35 to 45°C. The stabilized immobilized biocatalyst could be successfully employed in repeated batch reactions (residual activity of 55% after five cycles), which was not the case for whole cell reactions (residual activity ≤10 %). © Rapid Science Ltd. 1998[PUBLICATION ABSTRACT]</abstract><cop>Dordrecht</cop><pub>Springer</pub><doi>10.1023/A:1005379314104</doi><tpages>5</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0141-5492
ispartof Biotechnology letters, 1998-04, Vol.20 (4), p.373-377
issn 0141-5492
1573-6776
language eng
recordid cdi_proquest_miscellaneous_17217473
source Springer Link
subjects Binding sites
Biological and medical sciences
Biotechnology
Cellulose
Fundamental and applied biological sciences. Psychology
Immobilization of enzymes and other molecules
Immobilization techniques
Ions
Methods. Procedures. Technologies
Nocardia
title Stabilization of Nocardia EH1 epoxide hydrolase by immobilization
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T03%3A11%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pasca&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Stabilization%20of%20Nocardia%20EH1%20epoxide%20hydrolase%20by%20immobilization&rft.jtitle=Biotechnology%20letters&rft.au=KROUTIL,%20W&rft.date=1998-04-01&rft.volume=20&rft.issue=4&rft.spage=373&rft.epage=377&rft.pages=373-377&rft.issn=0141-5492&rft.eissn=1573-6776&rft.coden=BILED3&rft_id=info:doi/10.1023/A:1005379314104&rft_dat=%3Cproquest_pasca%3E17217473%3C/proquest_pasca%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c323t-99bf00b369b69cc47a3945b53d55c1195f15b6ff02f318f35d6281a4befde893%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=736824618&rft_id=info:pmid/&rfr_iscdi=true