Biosensor for the determination of phenols based on Cross-Linked Enzyme Crystals (CLEC) of laccase
Cross-linked enzyme crystals (CLECs) are a versatile form of biocatalyst that can also be used for biosensor application. Laccase from Trametes versicolor (E.C.1.10.3.2) was crystallized, cross-linked and lyophilized with β-cyclodextrin. The CLEC laccase was found to be highly active towards phenols...
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Veröffentlicht in: | Biosensors & bioelectronics 2005-07, Vol.21 (1), p.206-211 |
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creator | Roy, J. Jegan Abraham, T. Emilia Abhijith, K.S. Kumar, P.V. Sujith Thakur, M.S. |
description | Cross-linked enzyme crystals (CLECs) are a versatile form of biocatalyst that can also be used for biosensor application. Laccase from
Trametes versicolor (E.C.1.10.3.2) was crystallized, cross-linked and lyophilized with β-cyclodextrin. The CLEC laccase was found to be highly active towards phenols like 2-amino phenol, guaiacol, catechol, pyrogallol, catechin and ABTS (non-phenolic). The CLEC laccase was embedded in 30% polyvinylpropylidone (PVP) gel and mounted into an electrode to make the sensor. The biosensor was used to detect the phenols in 50–1000
μmol concentration level. Phenols with lower molecular weight such as 2-amino phenol, catechol and pyrogallol gave a short response time where as the higher molecular weight substrates like catechin and ABTS had comparatively a long response time. The optimum pH of the analyte was 5.5–6.0 when catechol was used as substrate. The CLEC laccase retained good activity for over 3 months. |
doi_str_mv | 10.1016/j.bios.2004.08.024 |
format | Article |
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Trametes versicolor (E.C.1.10.3.2) was crystallized, cross-linked and lyophilized with β-cyclodextrin. The CLEC laccase was found to be highly active towards phenols like 2-amino phenol, guaiacol, catechol, pyrogallol, catechin and ABTS (non-phenolic). The CLEC laccase was embedded in 30% polyvinylpropylidone (PVP) gel and mounted into an electrode to make the sensor. The biosensor was used to detect the phenols in 50–1000
μmol concentration level. Phenols with lower molecular weight such as 2-amino phenol, catechol and pyrogallol gave a short response time where as the higher molecular weight substrates like catechin and ABTS had comparatively a long response time. The optimum pH of the analyte was 5.5–6.0 when catechol was used as substrate. The CLEC laccase retained good activity for over 3 months.</description><identifier>ISSN: 0956-5663</identifier><identifier>EISSN: 1873-4235</identifier><identifier>DOI: 10.1016/j.bios.2004.08.024</identifier><identifier>PMID: 15967371</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Biological and medical sciences ; Biosensing Techniques - instrumentation ; Biosensing Techniques - methods ; Biosensor ; Biosensors ; Biotechnology ; Calibration ; CLEC ; Cross-linking ; Cross-Linking Reagents ; Crystallization ; Fundamental and applied biological sciences. Psychology ; Glutaraldehyde ; Kinetics ; Laccase ; Laccase - chemistry ; Methods. Procedures. Technologies ; Phenols - analysis ; Polyporales - enzymology ; Polyvinyls ; Trametes versicolor ; Various methods and equipments</subject><ispartof>Biosensors & bioelectronics, 2005-07, Vol.21 (1), p.206-211</ispartof><rights>2004 Elsevier B.V.</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-221d9923e3bc3a0e0bbf16d86955eebab82e91841635d24f2016ed4a4efa2dab3</citedby><cites>FETCH-LOGICAL-c415t-221d9923e3bc3a0e0bbf16d86955eebab82e91841635d24f2016ed4a4efa2dab3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0956566304003902$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17120688$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15967371$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Roy, J. Jegan</creatorcontrib><creatorcontrib>Abraham, T. Emilia</creatorcontrib><creatorcontrib>Abhijith, K.S.</creatorcontrib><creatorcontrib>Kumar, P.V. Sujith</creatorcontrib><creatorcontrib>Thakur, M.S.</creatorcontrib><title>Biosensor for the determination of phenols based on Cross-Linked Enzyme Crystals (CLEC) of laccase</title><title>Biosensors & bioelectronics</title><addtitle>Biosens Bioelectron</addtitle><description>Cross-linked enzyme crystals (CLECs) are a versatile form of biocatalyst that can also be used for biosensor application. Laccase from
Trametes versicolor (E.C.1.10.3.2) was crystallized, cross-linked and lyophilized with β-cyclodextrin. The CLEC laccase was found to be highly active towards phenols like 2-amino phenol, guaiacol, catechol, pyrogallol, catechin and ABTS (non-phenolic). The CLEC laccase was embedded in 30% polyvinylpropylidone (PVP) gel and mounted into an electrode to make the sensor. The biosensor was used to detect the phenols in 50–1000
μmol concentration level. Phenols with lower molecular weight such as 2-amino phenol, catechol and pyrogallol gave a short response time where as the higher molecular weight substrates like catechin and ABTS had comparatively a long response time. The optimum pH of the analyte was 5.5–6.0 when catechol was used as substrate. The CLEC laccase retained good activity for over 3 months.</description><subject>Biological and medical sciences</subject><subject>Biosensing Techniques - instrumentation</subject><subject>Biosensing Techniques - methods</subject><subject>Biosensor</subject><subject>Biosensors</subject><subject>Biotechnology</subject><subject>Calibration</subject><subject>CLEC</subject><subject>Cross-linking</subject><subject>Cross-Linking Reagents</subject><subject>Crystallization</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glutaraldehyde</subject><subject>Kinetics</subject><subject>Laccase</subject><subject>Laccase - chemistry</subject><subject>Methods. Procedures. Technologies</subject><subject>Phenols - analysis</subject><subject>Polyporales - enzymology</subject><subject>Polyvinyls</subject><subject>Trametes versicolor</subject><subject>Various methods and equipments</subject><issn>0956-5663</issn><issn>1873-4235</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2L1DAYxoMo7rj6D3iQXhQ9tOa7LexFy6gLA3vRc8jHWzZjm4xJR5j96zdlBvamhxDy5vc8JM-D0FuCG4KJ_LxvjI-5oRjzBncNpvwZ2pCuZTWnTDxHG9wLWQsp2RV6lfMeY9ySHr9EV0T0smUt2SDztVhAyDFVY1nLPVQOFkizD3rxMVRxrA73EOKUK6MzuKrMhhRzrnc-_C7nbXg4zVBmp7zoQn0cdtvh06qbtLVF8hq9GMsFvLns1-jXt-3P4Ue9u_t-O3zZ1ZYTsdSUEtf3lAEzlmkM2JiRSNfJXggAo01HoScdJ5IJR_lISwTguOYwauq0Ydfow9n3kOKfI-RFzT5bmCYdIB6zkm0vqBD8vyBpmRSMryA9g3b9cIJRHZKfdTopgtVagdqrtQK1VqBwp0oFRfTu4n40M7gnySXzAry_ADpbPY1JB-vzE9cSimXXFe7mzEEJ7a-HpLL1ECw4n8AuykX_r3c8AufzpF4</recordid><startdate>20050715</startdate><enddate>20050715</enddate><creator>Roy, J. Jegan</creator><creator>Abraham, T. Emilia</creator><creator>Abhijith, K.S.</creator><creator>Kumar, P.V. Sujith</creator><creator>Thakur, M.S.</creator><general>Elsevier B.V</general><general>Elsevier Science</general><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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20050715</creationdate><title>Biosensor for the determination of phenols based on Cross-Linked Enzyme Crystals (CLEC) of laccase</title><author>Roy, J. Jegan ; Abraham, T. Emilia ; Abhijith, K.S. ; Kumar, P.V. Sujith ; Thakur, M.S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-221d9923e3bc3a0e0bbf16d86955eebab82e91841635d24f2016ed4a4efa2dab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Biological and medical sciences</topic><topic>Biosensing Techniques - instrumentation</topic><topic>Biosensing Techniques - methods</topic><topic>Biosensor</topic><topic>Biosensors</topic><topic>Biotechnology</topic><topic>Calibration</topic><topic>CLEC</topic><topic>Cross-linking</topic><topic>Cross-Linking Reagents</topic><topic>Crystallization</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glutaraldehyde</topic><topic>Kinetics</topic><topic>Laccase</topic><topic>Laccase - chemistry</topic><topic>Methods. Procedures. Technologies</topic><topic>Phenols - analysis</topic><topic>Polyporales - enzymology</topic><topic>Polyvinyls</topic><topic>Trametes versicolor</topic><topic>Various methods and equipments</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roy, J. Jegan</creatorcontrib><creatorcontrib>Abraham, T. Emilia</creatorcontrib><creatorcontrib>Abhijith, K.S.</creatorcontrib><creatorcontrib>Kumar, P.V. Sujith</creatorcontrib><creatorcontrib>Thakur, M.S.</creatorcontrib><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>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biosensors & bioelectronics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Roy, J. Jegan</au><au>Abraham, T. Emilia</au><au>Abhijith, K.S.</au><au>Kumar, P.V. Sujith</au><au>Thakur, M.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biosensor for the determination of phenols based on Cross-Linked Enzyme Crystals (CLEC) of laccase</atitle><jtitle>Biosensors & bioelectronics</jtitle><addtitle>Biosens Bioelectron</addtitle><date>2005-07-15</date><risdate>2005</risdate><volume>21</volume><issue>1</issue><spage>206</spage><epage>211</epage><pages>206-211</pages><issn>0956-5663</issn><eissn>1873-4235</eissn><abstract>Cross-linked enzyme crystals (CLECs) are a versatile form of biocatalyst that can also be used for biosensor application. Laccase from
Trametes versicolor (E.C.1.10.3.2) was crystallized, cross-linked and lyophilized with β-cyclodextrin. The CLEC laccase was found to be highly active towards phenols like 2-amino phenol, guaiacol, catechol, pyrogallol, catechin and ABTS (non-phenolic). The CLEC laccase was embedded in 30% polyvinylpropylidone (PVP) gel and mounted into an electrode to make the sensor. The biosensor was used to detect the phenols in 50–1000
μmol concentration level. Phenols with lower molecular weight such as 2-amino phenol, catechol and pyrogallol gave a short response time where as the higher molecular weight substrates like catechin and ABTS had comparatively a long response time. The optimum pH of the analyte was 5.5–6.0 when catechol was used as substrate. The CLEC laccase retained good activity for over 3 months.</abstract><cop>Lausanne</cop><pub>Elsevier B.V</pub><pmid>15967371</pmid><doi>10.1016/j.bios.2004.08.024</doi><tpages>6</tpages></addata></record> |
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subjects | Biological and medical sciences Biosensing Techniques - instrumentation Biosensing Techniques - methods Biosensor Biosensors Biotechnology Calibration CLEC Cross-linking Cross-Linking Reagents Crystallization Fundamental and applied biological sciences. Psychology Glutaraldehyde Kinetics Laccase Laccase - chemistry Methods. Procedures. Technologies Phenols - analysis Polyporales - enzymology Polyvinyls Trametes versicolor Various methods and equipments |
title | Biosensor for the determination of phenols based on Cross-Linked Enzyme Crystals (CLEC) of laccase |
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