Wood cellulignin as an alternative matrix for enzyme immobilization
The objective of this work was to select an efficient methodology for preparing active samples of Candida rugosa lipase immobilized in wood cellulignin, to be applied in hydrolysis and ester reactions. For this purpose, lipase was immobilized in the matrix by physical adsorption (pure cellulignin) a...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2005, Vol.121 (1-3), p.255-268 |
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| creator | Gomes, F.M Silva, G.S Pinati, D.G Conte, R.A Castro, H.F. de |
| description | The objective of this work was to select an efficient methodology for preparing active samples of Candida rugosa lipase immobilized in wood cellulignin, to be applied in hydrolysis and ester reactions. For this purpose, lipase was immobilized in the matrix by physical adsorption (pure cellulignin) and covalent binding (activated cellulignin with glutaraldeyde or carbonyldiimidazole [CDI]) in the presence or absence of polyethylene glycol (PEG) (Molecular mass of 1500 Daltons) as stabilizing agent. The activating agent and the presence of PEG-1500 in the immobilization procedure showed a strong influence on enzyme retention in the support. The values for enzyme retention ranged from 20 to 68%, and the highest yield was obtained when the enzyme was immobilized in cellulignin activated with CDI in the presence of PEG-1500. This immobilized derivative presented high hydrolytic (193.27 micromolar/[mg . min]) and synthetic (522.92 micromolar/[g . min]) activities when compared with those obtained by other techniques. The superiority of this immobilized system was confirmed by additional analyses, such as infrared spectroscopy and elemental analysis, which demonstrated an appropriate enzyme fixation and the highest level of protein incorporation in the support. Further information on the immobilized derivative was obtained by assessing the recycle potential in both aqueous and nonaqueous media. |
| doi_str_mv | 10.1385/ABAB:121:1-3:0255 |
| format | Article |
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For this purpose, lipase was immobilized in the matrix by physical adsorption (pure cellulignin) and covalent binding (activated cellulignin with glutaraldeyde or carbonyldiimidazole [CDI]) in the presence or absence of polyethylene glycol (PEG) (Molecular mass of 1500 Daltons) as stabilizing agent. The activating agent and the presence of PEG-1500 in the immobilization procedure showed a strong influence on enzyme retention in the support. The values for enzyme retention ranged from 20 to 68%, and the highest yield was obtained when the enzyme was immobilized in cellulignin activated with CDI in the presence of PEG-1500. This immobilized derivative presented high hydrolytic (193.27 micromolar/[mg . min]) and synthetic (522.92 micromolar/[g . min]) activities when compared with those obtained by other techniques. The superiority of this immobilized system was confirmed by additional analyses, such as infrared spectroscopy and elemental analysis, which demonstrated an appropriate enzyme fixation and the highest level of protein incorporation in the support. Further information on the immobilized derivative was obtained by assessing the recycle potential in both aqueous and nonaqueous media.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>EISSN: 0273-2289</identifier><identifier>DOI: 10.1385/ABAB:121:1-3:0255</identifier><identifier>PMID: 15917604</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>Biochemistry ; Biomass ; Candida - enzymology ; Candida rugosa ; Cellulose - chemistry ; Enzyme Activation ; Enzyme Stability ; Enzymes ; Enzymes, Immobilized - analysis ; Enzymes, Immobilized - chemistry ; Enzymes, Immobilized - ultrastructure ; Eucalyptus - chemistry ; immobilized enzymes ; Infrared spectroscopy ; Lignin - chemistry ; Lipase - analysis ; Lipase - chemistry ; Membranes, Artificial ; Polyethylene Glycols - chemistry ; Retention ; Studies ; triacylglycerol lipase ; Wood ; Yeast</subject><ispartof>Applied biochemistry and biotechnology, 2005, Vol.121 (1-3), p.255-268</ispartof><rights>Humana Press Inc. 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c343t-ec5cb1d068b6c03f36a54aed98bbf08dfcee114cae5944278e524dfb09013f713</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15917604$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gomes, F.M</creatorcontrib><creatorcontrib>Silva, G.S</creatorcontrib><creatorcontrib>Pinati, D.G</creatorcontrib><creatorcontrib>Conte, R.A</creatorcontrib><creatorcontrib>Castro, H.F. de</creatorcontrib><title>Wood cellulignin as an alternative matrix for enzyme immobilization</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><description>The objective of this work was to select an efficient methodology for preparing active samples of Candida rugosa lipase immobilized in wood cellulignin, to be applied in hydrolysis and ester reactions. For this purpose, lipase was immobilized in the matrix by physical adsorption (pure cellulignin) and covalent binding (activated cellulignin with glutaraldeyde or carbonyldiimidazole [CDI]) in the presence or absence of polyethylene glycol (PEG) (Molecular mass of 1500 Daltons) as stabilizing agent. The activating agent and the presence of PEG-1500 in the immobilization procedure showed a strong influence on enzyme retention in the support. The values for enzyme retention ranged from 20 to 68%, and the highest yield was obtained when the enzyme was immobilized in cellulignin activated with CDI in the presence of PEG-1500. This immobilized derivative presented high hydrolytic (193.27 micromolar/[mg . min]) and synthetic (522.92 micromolar/[g . min]) activities when compared with those obtained by other techniques. The superiority of this immobilized system was confirmed by additional analyses, such as infrared spectroscopy and elemental analysis, which demonstrated an appropriate enzyme fixation and the highest level of protein incorporation in the support. Further information on the immobilized derivative was obtained by assessing the recycle potential in both aqueous and nonaqueous media.</description><subject>Biochemistry</subject><subject>Biomass</subject><subject>Candida - enzymology</subject><subject>Candida rugosa</subject><subject>Cellulose - chemistry</subject><subject>Enzyme Activation</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized - analysis</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Enzymes, Immobilized - ultrastructure</subject><subject>Eucalyptus - chemistry</subject><subject>immobilized enzymes</subject><subject>Infrared spectroscopy</subject><subject>Lignin - chemistry</subject><subject>Lipase - analysis</subject><subject>Lipase - chemistry</subject><subject>Membranes, Artificial</subject><subject>Polyethylene Glycols - chemistry</subject><subject>Retention</subject><subject>Studies</subject><subject>triacylglycerol lipase</subject><subject>Wood</subject><subject>Yeast</subject><issn>0273-2289</issn><issn>1559-0291</issn><issn>0273-2289</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkU1P3DAQhq2qCLbAD-gFIg7tKeDxR2zvbVm1BQmph7LiaDmJvTJKYmonCPj1ONqVKvXQXmYuz8y8mgehz4AvgUp-tbpeXS-BwBJKusSE8w9oAZyrEhMFH9ECE0FLQqQ6Qp9SesQYiOTiEB0BVyAqzBZo_RBCWzS266bObwc_FCYVJtdutHEwo3-2RW_G6F8KF2Jhh7fX3ha-70PtO_-WgTCcoANnumRP9_0Ybb5_u1_flHc_f9yuV3dlQxkdS9vwpoYWV7KuGkwdrQxnxrZK1rXDsnWNtQCsMZYrxoiQlhPWuhorDNQJoMfo627vUwy_J5tG3fs0RzeDDVPSUihWKcJlJr_8k6yErISQ_wdBcEorRTN48Rf4GKb8oC4zSuTYDM8BYQc1MaQUrdNP0fcmvmrAejamZ2M6G9OgqZ6N5Zmz_eKp7m37Z2KvKAPnO8CZoM02-qQ3v0i-hiEXCYy-Ayrfmfk</recordid><startdate>2005</startdate><enddate>2005</enddate><creator>Gomes, F.M</creator><creator>Silva, G.S</creator><creator>Pinati, D.G</creator><creator>Conte, R.A</creator><creator>Castro, H.F. de</creator><general>Springer Nature B.V</general><scope>FBQ</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>3V.</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</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>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</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>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7QO</scope><scope>7X8</scope></search><sort><creationdate>2005</creationdate><title>Wood cellulignin as an alternative matrix for enzyme immobilization</title><author>Gomes, F.M ; Silva, G.S ; Pinati, D.G ; Conte, R.A ; Castro, H.F. de</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c343t-ec5cb1d068b6c03f36a54aed98bbf08dfcee114cae5944278e524dfb09013f713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Biochemistry</topic><topic>Biomass</topic><topic>Candida - enzymology</topic><topic>Candida rugosa</topic><topic>Cellulose - chemistry</topic><topic>Enzyme Activation</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Enzymes, Immobilized - analysis</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Enzymes, Immobilized - ultrastructure</topic><topic>Eucalyptus - chemistry</topic><topic>immobilized enzymes</topic><topic>Infrared spectroscopy</topic><topic>Lignin - chemistry</topic><topic>Lipase - analysis</topic><topic>Lipase - chemistry</topic><topic>Membranes, Artificial</topic><topic>Polyethylene Glycols - chemistry</topic><topic>Retention</topic><topic>Studies</topic><topic>triacylglycerol lipase</topic><topic>Wood</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gomes, F.M</creatorcontrib><creatorcontrib>Silva, G.S</creatorcontrib><creatorcontrib>Pinati, D.G</creatorcontrib><creatorcontrib>Conte, R.A</creatorcontrib><creatorcontrib>Castro, H.F. de</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & 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 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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</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 & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science 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>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gomes, F.M</au><au>Silva, G.S</au><au>Pinati, D.G</au><au>Conte, R.A</au><au>Castro, H.F. de</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Wood cellulignin as an alternative matrix for enzyme immobilization</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2005</date><risdate>2005</risdate><volume>121</volume><issue>1-3</issue><spage>255</spage><epage>268</epage><pages>255-268</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><eissn>0273-2289</eissn><abstract>The objective of this work was to select an efficient methodology for preparing active samples of Candida rugosa lipase immobilized in wood cellulignin, to be applied in hydrolysis and ester reactions. For this purpose, lipase was immobilized in the matrix by physical adsorption (pure cellulignin) and covalent binding (activated cellulignin with glutaraldeyde or carbonyldiimidazole [CDI]) in the presence or absence of polyethylene glycol (PEG) (Molecular mass of 1500 Daltons) as stabilizing agent. The activating agent and the presence of PEG-1500 in the immobilization procedure showed a strong influence on enzyme retention in the support. The values for enzyme retention ranged from 20 to 68%, and the highest yield was obtained when the enzyme was immobilized in cellulignin activated with CDI in the presence of PEG-1500. This immobilized derivative presented high hydrolytic (193.27 micromolar/[mg . min]) and synthetic (522.92 micromolar/[g . min]) activities when compared with those obtained by other techniques. The superiority of this immobilized system was confirmed by additional analyses, such as infrared spectroscopy and elemental analysis, which demonstrated an appropriate enzyme fixation and the highest level of protein incorporation in the support. Further information on the immobilized derivative was obtained by assessing the recycle potential in both aqueous and nonaqueous media.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>15917604</pmid><doi>10.1385/ABAB:121:1-3:0255</doi><tpages>14</tpages></addata></record> |
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| ispartof | Applied biochemistry and biotechnology, 2005, Vol.121 (1-3), p.255-268 |
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| subjects | Biochemistry Biomass Candida - enzymology Candida rugosa Cellulose - chemistry Enzyme Activation Enzyme Stability Enzymes Enzymes, Immobilized - analysis Enzymes, Immobilized - chemistry Enzymes, Immobilized - ultrastructure Eucalyptus - chemistry immobilized enzymes Infrared spectroscopy Lignin - chemistry Lipase - analysis Lipase - chemistry Membranes, Artificial Polyethylene Glycols - chemistry Retention Studies triacylglycerol lipase Wood Yeast |
| title | Wood cellulignin as an alternative matrix for enzyme immobilization |
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