A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates
Cross‐linked enzyme aggregates (CLEAs) were prepared from several enzymes (penicillin G acylase, hydroxynitrile lyase, alcohol dehydrogenase, and two different nitrilases) by precipitation and subsequent cross‐linking using dextran polyaldehyde. In most cases, higher immobilization yields were obtai...
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| Veröffentlicht in: | Biotechnology and bioengineering 2004-05, Vol.86 (3), p.273-276 |
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| container_title | Biotechnology and bioengineering |
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| creator | Mateo, Cesar Palomo, José M. van Langen, Luuk M. van Rantwijk, Fred Sheldon, Roger A. |
| description | Cross‐linked enzyme aggregates (CLEAs) were prepared from several enzymes (penicillin G acylase, hydroxynitrile lyase, alcohol dehydrogenase, and two different nitrilases) by precipitation and subsequent cross‐linking using dextran polyaldehyde. In most cases, higher immobilization yields were obtained using the latter cross‐linker as compared with the commonly used glutaraldehyde. Active site titration of penicillin acylase CLEAs showed that the higher activity originated from a significantly lower loss in active sites using dextran polyaldehyde as a cross‐linking agent. It is proposed that macromolecular cross‐linkers are too large to penetrate the protein active site and react with catalytically essential amino acid residues. © 2004 Wiley Periodicals, Inc. |
| doi_str_mv | 10.1002/bit.20033 |
| format | Article |
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In most cases, higher immobilization yields were obtained using the latter cross‐linker as compared with the commonly used glutaraldehyde. Active site titration of penicillin acylase CLEAs showed that the higher activity originated from a significantly lower loss in active sites using dextran polyaldehyde as a cross‐linking agent. It is proposed that macromolecular cross‐linkers are too large to penetrate the protein active site and react with catalytically essential amino acid residues. © 2004 Wiley Periodicals, Inc.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.20033</identifier><identifier>PMID: 15083507</identifier><identifier>CODEN: BIBIAU</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Alcohol dehydrogenase ; Amino acids ; Binding Sites ; Biological and medical sciences ; Biotechnology ; Catalysis ; cross-linked enzyme aggregates (CLEAs) ; cross-linker ; Cross-Linking Reagents - metabolism ; Dextran ; Dextrans - metabolism ; Enzymes, Immobilized - metabolism ; Fundamental and applied biological sciences. Psychology ; Glutaral - metabolism ; Glutaraldehyde ; Immobilization ; Immobilized enzymes ; Molecular Weight ; Nitrilase ; oxynitrilase ; Penicillin amidase ; Penicillin Amidase - metabolism ; penicillin G acylase ; Precipitation ; Q1 ; Titration</subject><ispartof>Biotechnology and bioengineering, 2004-05, Vol.86 (3), p.273-276</ispartof><rights>Copyright © 2004 Wiley Periodicals, Inc.</rights><rights>2004 INIST-CNRS</rights><rights>Copyright 2004 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5243-6b7c52c969914d6646107beea5b5458027d06b12e7e2b224f251d25ffebbee723</citedby><cites>FETCH-LOGICAL-c5243-6b7c52c969914d6646107beea5b5458027d06b12e7e2b224f251d25ffebbee723</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbit.20033$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbit.20033$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15673949$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15083507$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mateo, Cesar</creatorcontrib><creatorcontrib>Palomo, José M.</creatorcontrib><creatorcontrib>van Langen, Luuk M.</creatorcontrib><creatorcontrib>van Rantwijk, Fred</creatorcontrib><creatorcontrib>Sheldon, Roger A.</creatorcontrib><title>A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol. Bioeng</addtitle><description>Cross‐linked enzyme aggregates (CLEAs) were prepared from several enzymes (penicillin G acylase, hydroxynitrile lyase, alcohol dehydrogenase, and two different nitrilases) by precipitation and subsequent cross‐linking using dextran polyaldehyde. In most cases, higher immobilization yields were obtained using the latter cross‐linker as compared with the commonly used glutaraldehyde. Active site titration of penicillin acylase CLEAs showed that the higher activity originated from a significantly lower loss in active sites using dextran polyaldehyde as a cross‐linking agent. It is proposed that macromolecular cross‐linkers are too large to penetrate the protein active site and react with catalytically essential amino acid residues. © 2004 Wiley Periodicals, Inc.</description><subject>Alcohol dehydrogenase</subject><subject>Amino acids</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Catalysis</subject><subject>cross-linked enzyme aggregates (CLEAs)</subject><subject>cross-linker</subject><subject>Cross-Linking Reagents - metabolism</subject><subject>Dextran</subject><subject>Dextrans - metabolism</subject><subject>Enzymes, Immobilized - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glutaral - metabolism</subject><subject>Glutaraldehyde</subject><subject>Immobilization</subject><subject>Immobilized enzymes</subject><subject>Molecular Weight</subject><subject>Nitrilase</subject><subject>oxynitrilase</subject><subject>Penicillin amidase</subject><subject>Penicillin Amidase - metabolism</subject><subject>penicillin G acylase</subject><subject>Precipitation</subject><subject>Q1</subject><subject>Titration</subject><issn>0006-3592</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90F1PFDEUBuDGYGRdveAPkLkBQ-LA6ffM5YqIGCIxWQN3TWfmzFCYj7WdDa6_3rq7Ajd61TZ53nPSl5A9CscUgJ0UbjxmAJy_IBMKuU6B5bBDJgCgUi5ztkteh3AXnzpT6hXZpRIyLkFPyNUs6fHhfdK5tkpKP4SQtq6_d32TdDjeDtXQDs0qGYdk4XFhPT5DWCXY_1p1mNim8djYEcMb8rK2bcC323NKvn86m59-Ti-vzi9OZ5dpKZngqSp0vJS5ynMqKqWEoqALRCsLKWQGTFegCspQIysYEzWTtGKyrrGISjM-Je82cxd--LHEMJrOhRLb1vY4LIPRQsVGBBdRHv5f0owppbMIjzZw_UOPtVl411m_MhTMn55N7Nmse452fzt0WXRYPcltsREcbIENpW1rb_vShWdOaZ6LPLqTjXtwLa7-vdF8uJj_XZ1uEi6M-PMxYf29iTO1NNdfz83NN_rlI8xjjP8GQ1aiGA</recordid><startdate>20040505</startdate><enddate>20040505</enddate><creator>Mateo, Cesar</creator><creator>Palomo, José M.</creator><creator>van Langen, Luuk M.</creator><creator>van Rantwijk, Fred</creator><creator>Sheldon, Roger A.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20040505</creationdate><title>A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates</title><author>Mateo, Cesar ; Palomo, José M. ; van Langen, Luuk M. ; van Rantwijk, Fred ; Sheldon, Roger A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5243-6b7c52c969914d6646107beea5b5458027d06b12e7e2b224f251d25ffebbee723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Alcohol dehydrogenase</topic><topic>Amino acids</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Catalysis</topic><topic>cross-linked enzyme aggregates (CLEAs)</topic><topic>cross-linker</topic><topic>Cross-Linking Reagents - metabolism</topic><topic>Dextran</topic><topic>Dextrans - metabolism</topic><topic>Enzymes, Immobilized - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glutaral - metabolism</topic><topic>Glutaraldehyde</topic><topic>Immobilization</topic><topic>Immobilized enzymes</topic><topic>Molecular Weight</topic><topic>Nitrilase</topic><topic>oxynitrilase</topic><topic>Penicillin amidase</topic><topic>Penicillin Amidase - metabolism</topic><topic>penicillin G acylase</topic><topic>Precipitation</topic><topic>Q1</topic><topic>Titration</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mateo, Cesar</creatorcontrib><creatorcontrib>Palomo, José M.</creatorcontrib><creatorcontrib>van Langen, Luuk M.</creatorcontrib><creatorcontrib>van Rantwijk, Fred</creatorcontrib><creatorcontrib>Sheldon, Roger A.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mateo, Cesar</au><au>Palomo, José M.</au><au>van Langen, Luuk M.</au><au>van Rantwijk, Fred</au><au>Sheldon, Roger A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates</atitle><jtitle>Biotechnology and bioengineering</jtitle><addtitle>Biotechnol. Bioeng</addtitle><date>2004-05-05</date><risdate>2004</risdate><volume>86</volume><issue>3</issue><spage>273</spage><epage>276</epage><pages>273-276</pages><issn>0006-3592</issn><eissn>1097-0290</eissn><coden>BIBIAU</coden><abstract>Cross‐linked enzyme aggregates (CLEAs) were prepared from several enzymes (penicillin G acylase, hydroxynitrile lyase, alcohol dehydrogenase, and two different nitrilases) by precipitation and subsequent cross‐linking using dextran polyaldehyde. In most cases, higher immobilization yields were obtained using the latter cross‐linker as compared with the commonly used glutaraldehyde. Active site titration of penicillin acylase CLEAs showed that the higher activity originated from a significantly lower loss in active sites using dextran polyaldehyde as a cross‐linking agent. It is proposed that macromolecular cross‐linkers are too large to penetrate the protein active site and react with catalytically essential amino acid residues. © 2004 Wiley Periodicals, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>15083507</pmid><doi>10.1002/bit.20033</doi><tpages>4</tpages></addata></record> |
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| subjects | Alcohol dehydrogenase Amino acids Binding Sites Biological and medical sciences Biotechnology Catalysis cross-linked enzyme aggregates (CLEAs) cross-linker Cross-Linking Reagents - metabolism Dextran Dextrans - metabolism Enzymes, Immobilized - metabolism Fundamental and applied biological sciences. Psychology Glutaral - metabolism Glutaraldehyde Immobilization Immobilized enzymes Molecular Weight Nitrilase oxynitrilase Penicillin amidase Penicillin Amidase - metabolism penicillin G acylase Precipitation Q1 Titration |
| title | A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates |
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