Peculiarities of direct bioelectrocatalysis by laccase in aqueous–nonaqueous mixtures
The effect of concentration of ethanol and dimethyl sulfoxide on the catalytic activity of laccase is studied for the enzymatic reaction of catechol oxidation and bioelectrocatalytic reaction of oxygen reduction under the conditions of direct electron transfer. Laccase–Nafion composite is elaborated...
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| Veröffentlicht in: | Biosensors & bioelectronics 2002-12, Vol.17 (11), p.945-951 |
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| container_title | Biosensors & bioelectronics |
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| creator | Bogdanovskaya, V.A Tarasevich, M.R Kuznetsova, L.N Reznik, M.F Kasatkin, E.V |
| description | The effect of concentration of ethanol and dimethyl sulfoxide on the catalytic activity of laccase is studied for the enzymatic reaction of catechol oxidation and bioelectrocatalytic reaction of oxygen reduction under the conditions of direct electron transfer. Laccase–Nafion composite is elaborated ensuring the enzyme stability in a wide potential range and a content of organic solvents. Based on the STM measurements, the structure of composite layer is proposed. It is shown that the mechanism of oxygen reduction reaction by laccase in organo-aqueous mixtures is similar to that earlier proposed for aqueous solutions. A decrease in the electrocatalytic activity of laccase in the oxygen reduction correlates with a decrease in the laccase enzymatic activity in the substrate oxidation. However, a decrease in the laccase activity in the composite is observed at a higher content of organic solvent in the mixture. The mechanism of laccase inactivation by organic solvents is proposed. |
| doi_str_mv | 10.1016/S0956-5663(02)00086-6 |
| format | Article |
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Laccase–Nafion composite is elaborated ensuring the enzyme stability in a wide potential range and a content of organic solvents. Based on the STM measurements, the structure of composite layer is proposed. It is shown that the mechanism of oxygen reduction reaction by laccase in organo-aqueous mixtures is similar to that earlier proposed for aqueous solutions. A decrease in the electrocatalytic activity of laccase in the oxygen reduction correlates with a decrease in the laccase enzymatic activity in the substrate oxidation. However, a decrease in the laccase activity in the composite is observed at a higher content of organic solvent in the mixture. The mechanism of laccase inactivation by organic solvents is proposed.</description><identifier>ISSN: 0956-5663</identifier><identifier>EISSN: 1873-4235</identifier><identifier>DOI: 10.1016/S0956-5663(02)00086-6</identifier><identifier>PMID: 12392943</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Biosensing Techniques - instrumentation ; Biosensing Techniques - methods ; Catalysis ; Catechols - chemistry ; Composite ; Dimethyl Sulfoxide - chemistry ; Direct bioelectrocatalysis ; Electrochemistry - methods ; Electrodes ; Enzyme Activation ; Enzyme Inhibitors ; Enzyme Stability ; Enzymes, Immobilized - chemistry ; Ethanol - chemistry ; Fluorocarbon Polymers ; Laccase ; Organic Chemicals - chemistry ; Organic solvent ; Oxidation-Reduction ; Oxidoreductases - antagonists & inhibitors ; Oxidoreductases - chemistry ; Oxygen - chemistry ; Sensitivity and Specificity ; Solvents - chemistry ; Water - chemistry</subject><ispartof>Biosensors & bioelectronics, 2002-12, Vol.17 (11), p.945-951</ispartof><rights>2002 Elsevier Science B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-2b4ca2d0303792eb46be2481b0b05c33ff52cbe51f6349cd87608857c5c200ea3</citedby><cites>FETCH-LOGICAL-c427t-2b4ca2d0303792eb46be2481b0b05c33ff52cbe51f6349cd87608857c5c200ea3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0956566302000866$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12392943$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bogdanovskaya, V.A</creatorcontrib><creatorcontrib>Tarasevich, M.R</creatorcontrib><creatorcontrib>Kuznetsova, L.N</creatorcontrib><creatorcontrib>Reznik, M.F</creatorcontrib><creatorcontrib>Kasatkin, E.V</creatorcontrib><title>Peculiarities of direct bioelectrocatalysis by laccase in aqueous–nonaqueous mixtures</title><title>Biosensors & bioelectronics</title><addtitle>Biosens Bioelectron</addtitle><description>The effect of concentration of ethanol and dimethyl sulfoxide on the catalytic activity of laccase is studied for the enzymatic reaction of catechol oxidation and bioelectrocatalytic reaction of oxygen reduction under the conditions of direct electron transfer. Laccase–Nafion composite is elaborated ensuring the enzyme stability in a wide potential range and a content of organic solvents. Based on the STM measurements, the structure of composite layer is proposed. It is shown that the mechanism of oxygen reduction reaction by laccase in organo-aqueous mixtures is similar to that earlier proposed for aqueous solutions. A decrease in the electrocatalytic activity of laccase in the oxygen reduction correlates with a decrease in the laccase enzymatic activity in the substrate oxidation. However, a decrease in the laccase activity in the composite is observed at a higher content of organic solvent in the mixture. The mechanism of laccase inactivation by organic solvents is proposed.</description><subject>Biosensing Techniques - instrumentation</subject><subject>Biosensing Techniques - methods</subject><subject>Catalysis</subject><subject>Catechols - chemistry</subject><subject>Composite</subject><subject>Dimethyl Sulfoxide - chemistry</subject><subject>Direct bioelectrocatalysis</subject><subject>Electrochemistry - methods</subject><subject>Electrodes</subject><subject>Enzyme Activation</subject><subject>Enzyme Inhibitors</subject><subject>Enzyme Stability</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Ethanol - chemistry</subject><subject>Fluorocarbon Polymers</subject><subject>Laccase</subject><subject>Organic Chemicals - chemistry</subject><subject>Organic solvent</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - antagonists & inhibitors</subject><subject>Oxidoreductases - chemistry</subject><subject>Oxygen - chemistry</subject><subject>Sensitivity and Specificity</subject><subject>Solvents - chemistry</subject><subject>Water - chemistry</subject><issn>0956-5663</issn><issn>1873-4235</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1KxDAQgIMo7rr6CEpPoofqJGnS9iSy-AcLCioeQ5JOIdJt16QV9-Y7-IY-id3tokdPMwPf_H2EHFI4o0Dl-SPkQsZCSn4C7BQAMhnLLTKmWcrjhHGxTca_yIjshfDaQynNYZeMKOM5yxM-Ji8PaLvKae9ahyFqyqhwHm0bGddg1Se-sbrV1TK4EJllVGlrdcDI1ZF-67DpwvfnV93UmyKau4-28xj2yU6pq4AHmzghz9dXT9PbeHZ_cze9nMU2YWkbM5NYzQrgwNOcoUmkQZZk1IABYTkvS8GsQUFLyZPcFlkqIctEaoVlAKj5hBwPcxe-6U8IrZq7YLGqdL26R6VMMCYo7UExgNY3IXgs1cK7ufZLRUGtjKq1UbXSpYCptVEl-76jzYLOzLH469oo7IGLAcD-zXeHXgXrsLY4iFRF4_5Z8QOn2ogM</recordid><startdate>20021201</startdate><enddate>20021201</enddate><creator>Bogdanovskaya, V.A</creator><creator>Tarasevich, M.R</creator><creator>Kuznetsova, L.N</creator><creator>Reznik, M.F</creator><creator>Kasatkin, E.V</creator><general>Elsevier B.V</general><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>20021201</creationdate><title>Peculiarities of direct bioelectrocatalysis by laccase in aqueous–nonaqueous mixtures</title><author>Bogdanovskaya, V.A ; Tarasevich, M.R ; Kuznetsova, L.N ; Reznik, M.F ; Kasatkin, E.V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-2b4ca2d0303792eb46be2481b0b05c33ff52cbe51f6349cd87608857c5c200ea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Biosensing Techniques - instrumentation</topic><topic>Biosensing Techniques - methods</topic><topic>Catalysis</topic><topic>Catechols - chemistry</topic><topic>Composite</topic><topic>Dimethyl Sulfoxide - chemistry</topic><topic>Direct bioelectrocatalysis</topic><topic>Electrochemistry - methods</topic><topic>Electrodes</topic><topic>Enzyme Activation</topic><topic>Enzyme Inhibitors</topic><topic>Enzyme Stability</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Ethanol - chemistry</topic><topic>Fluorocarbon Polymers</topic><topic>Laccase</topic><topic>Organic Chemicals - chemistry</topic><topic>Organic solvent</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases - antagonists & inhibitors</topic><topic>Oxidoreductases - chemistry</topic><topic>Oxygen - chemistry</topic><topic>Sensitivity and Specificity</topic><topic>Solvents - chemistry</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bogdanovskaya, V.A</creatorcontrib><creatorcontrib>Tarasevich, M.R</creatorcontrib><creatorcontrib>Kuznetsova, L.N</creatorcontrib><creatorcontrib>Reznik, M.F</creatorcontrib><creatorcontrib>Kasatkin, E.V</creatorcontrib><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>Biosensors & bioelectronics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bogdanovskaya, V.A</au><au>Tarasevich, M.R</au><au>Kuznetsova, L.N</au><au>Reznik, M.F</au><au>Kasatkin, E.V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peculiarities of direct bioelectrocatalysis by laccase in aqueous–nonaqueous mixtures</atitle><jtitle>Biosensors & bioelectronics</jtitle><addtitle>Biosens Bioelectron</addtitle><date>2002-12-01</date><risdate>2002</risdate><volume>17</volume><issue>11</issue><spage>945</spage><epage>951</epage><pages>945-951</pages><issn>0956-5663</issn><eissn>1873-4235</eissn><abstract>The effect of concentration of ethanol and dimethyl sulfoxide on the catalytic activity of laccase is studied for the enzymatic reaction of catechol oxidation and bioelectrocatalytic reaction of oxygen reduction under the conditions of direct electron transfer. Laccase–Nafion composite is elaborated ensuring the enzyme stability in a wide potential range and a content of organic solvents. Based on the STM measurements, the structure of composite layer is proposed. It is shown that the mechanism of oxygen reduction reaction by laccase in organo-aqueous mixtures is similar to that earlier proposed for aqueous solutions. A decrease in the electrocatalytic activity of laccase in the oxygen reduction correlates with a decrease in the laccase enzymatic activity in the substrate oxidation. However, a decrease in the laccase activity in the composite is observed at a higher content of organic solvent in the mixture. The mechanism of laccase inactivation by organic solvents is proposed.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>12392943</pmid><doi>10.1016/S0956-5663(02)00086-6</doi><tpages>7</tpages></addata></record> |
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| subjects | Biosensing Techniques - instrumentation Biosensing Techniques - methods Catalysis Catechols - chemistry Composite Dimethyl Sulfoxide - chemistry Direct bioelectrocatalysis Electrochemistry - methods Electrodes Enzyme Activation Enzyme Inhibitors Enzyme Stability Enzymes, Immobilized - chemistry Ethanol - chemistry Fluorocarbon Polymers Laccase Organic Chemicals - chemistry Organic solvent Oxidation-Reduction Oxidoreductases - antagonists & inhibitors Oxidoreductases - chemistry Oxygen - chemistry Sensitivity and Specificity Solvents - chemistry Water - chemistry |
| title | Peculiarities of direct bioelectrocatalysis by laccase in aqueous–nonaqueous mixtures |
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