Hydrolysis of organophosphate insecticides by an immobilized-enzyme system
An enzyme preparation that could detoxify parathion and eight other organophosphate pesticides was covalently bound to either porous glass or porous silica beads. This immobilized‐enzyme system was examined for its use in detoxification of pesticides in production wastewaters. The kinetics of parath...
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| Veröffentlicht in: | Biotechnology and bioengineering 1979-12, Vol.21 (12), p.2247-2261 |
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| container_title | Biotechnology and bioengineering |
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| creator | Munnecke, D.M |
| description | An enzyme preparation that could detoxify parathion and eight other organophosphate pesticides was covalently bound to either porous glass or porous silica beads. This immobilized‐enzyme system was examined for its use in detoxification of pesticides in production wastewaters. The kinetics of parathion hydrolysis were examined at flow rates up to 96 liter/hr and at influent substrate concentrations ranging from 10–250 mg/liter. The enzyme reactor was able to hydrolyze 95% o1r more of the parathion added to industrial wastewaters generated during its production, thus reducing the effluent parathion concentration to below 500 ppb. Laboratory continuous‐flow experiments were conducted for 70 days with industrial wastewater and indicated no loss in immobilized‐enzyme activity. The influence of pH, temperature, solvents, and detergents on enzyme stability and activity and enzyme reactor kinetics will be discussed. |
| doi_str_mv | 10.1002/bit.260211207 |
| format | Article |
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This immobilized‐enzyme system was examined for its use in detoxification of pesticides in production wastewaters. The kinetics of parathion hydrolysis were examined at flow rates up to 96 liter/hr and at influent substrate concentrations ranging from 10–250 mg/liter. The enzyme reactor was able to hydrolyze 95% o1r more of the parathion added to industrial wastewaters generated during its production, thus reducing the effluent parathion concentration to below 500 ppb. Laboratory continuous‐flow experiments were conducted for 70 days with industrial wastewater and indicated no loss in immobilized‐enzyme activity. The influence of pH, temperature, solvents, and detergents on enzyme stability and activity and enzyme reactor kinetics will be discussed.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.260211207</identifier><identifier>PMID: 42449</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Enzymes, Immobilized ; Glass ; Hydrogen-Ion Concentration ; Hydrolysis ; Insecticides ; Kinetics ; Organophosphorus Compounds ; Phosphoric Monoester Hydrolases - antagonists & inhibitors ; Silicon Dioxide ; Temperature</subject><ispartof>Biotechnology and bioengineering, 1979-12, Vol.21 (12), p.2247-2261</ispartof><rights>Copyright © 1979 John Wiley & Sons, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4277-4d73cc7a35e0f6a8326d0d52ad0abd6b4ef6ba67c32ad24dcd42ef4e1efc5e663</citedby><cites>FETCH-LOGICAL-c4277-4d73cc7a35e0f6a8326d0d52ad0abd6b4ef6ba67c32ad24dcd42ef4e1efc5e663</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.260211207$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbit.260211207$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/42449$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Munnecke, D.M</creatorcontrib><title>Hydrolysis of organophosphate insecticides by an immobilized-enzyme system</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol. 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The influence of pH, temperature, solvents, and detergents on enzyme stability and activity and enzyme reactor kinetics will be discussed.</description><subject>Enzymes, Immobilized</subject><subject>Glass</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolysis</subject><subject>Insecticides</subject><subject>Kinetics</subject><subject>Organophosphorus Compounds</subject><subject>Phosphoric Monoester Hydrolases - antagonists & inhibitors</subject><subject>Silicon Dioxide</subject><subject>Temperature</subject><issn>0006-3592</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1P3DAQhq2qq3a77bGX9pITt8D4I_bmWFZ8CoFEQSAulmNPwCWJFzurEn49aXe14sRpNDPPvBo9hHynsEsB2F7l-10mgVHKQH0gUwqlyoGV8JFMAUDmvCjZZ_IlpT9jq-ZSfiITwYQop-T0eHAxNEPyKQt1FuK96cLyIaTlg-kx811C23vrHaasGjLTZb5tQ-Ub_4Iux-5laDFLQ-qx_UomtWkSftvUGbk-PLhaHOdnF0cni19nuRVMqVw4xa1VhhcItTRzzqQDVzDjwFROVgJrWRmpLB9HTDjrBMNaIMXaFigln5Gdde4yhqcVpl63PllsGtNhWCVNeUkFiPkI5mvQxpBSxFovo29NHDQF_c-cHs3prbmR_7kJXlUtui39X9W4VevtX9_g8H6U3j-5epu7-cOPmp63lyY-aqm4KvTN-ZE-vby9u9uXl3ox8j_WfG2CNvfRJ339W5W8AKr4K-xRkwI</recordid><startdate>197912</startdate><enddate>197912</enddate><creator>Munnecke, D.M</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>FBQ</scope><scope>BSCLL</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>7QH</scope></search><sort><creationdate>197912</creationdate><title>Hydrolysis of organophosphate insecticides by an immobilized-enzyme system</title><author>Munnecke, D.M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4277-4d73cc7a35e0f6a8326d0d52ad0abd6b4ef6ba67c32ad24dcd42ef4e1efc5e663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Enzymes, Immobilized</topic><topic>Glass</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolysis</topic><topic>Insecticides</topic><topic>Kinetics</topic><topic>Organophosphorus Compounds</topic><topic>Phosphoric Monoester Hydrolases - antagonists & inhibitors</topic><topic>Silicon Dioxide</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Munnecke, D.M</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aqualine</collection><jtitle>Biotechnology and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Munnecke, D.M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hydrolysis of organophosphate insecticides by an immobilized-enzyme system</atitle><jtitle>Biotechnology and bioengineering</jtitle><addtitle>Biotechnol. Bioeng</addtitle><date>1979-12</date><risdate>1979</risdate><volume>21</volume><issue>12</issue><spage>2247</spage><epage>2261</epage><pages>2247-2261</pages><issn>0006-3592</issn><eissn>1097-0290</eissn><abstract>An enzyme preparation that could detoxify parathion and eight other organophosphate pesticides was covalently bound to either porous glass or porous silica beads. This immobilized‐enzyme system was examined for its use in detoxification of pesticides in production wastewaters. The kinetics of parathion hydrolysis were examined at flow rates up to 96 liter/hr and at influent substrate concentrations ranging from 10–250 mg/liter. The enzyme reactor was able to hydrolyze 95% o1r more of the parathion added to industrial wastewaters generated during its production, thus reducing the effluent parathion concentration to below 500 ppb. Laboratory continuous‐flow experiments were conducted for 70 days with industrial wastewater and indicated no loss in immobilized‐enzyme activity. The influence of pH, temperature, solvents, and detergents on enzyme stability and activity and enzyme reactor kinetics will be discussed.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>42449</pmid><doi>10.1002/bit.260211207</doi><tpages>15</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3592 |
| ispartof | Biotechnology and bioengineering, 1979-12, Vol.21 (12), p.2247-2261 |
| issn | 0006-3592 1097-0290 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Enzymes, Immobilized Glass Hydrogen-Ion Concentration Hydrolysis Insecticides Kinetics Organophosphorus Compounds Phosphoric Monoester Hydrolases - antagonists & inhibitors Silicon Dioxide Temperature |
| title | Hydrolysis of organophosphate insecticides by an immobilized-enzyme system |
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