Prediction of penicillin V acylase stability in water-organic co-solvent monophasic systems as a function of solvent composition
Hydrolytic activity of penicillin V acylase (EC 3.5.1.11) can be improved by using organic cosolvents in monophasic systems. However, the addition of these solvents may result in loss of stability of the enzyme. The thermal stability of penicillin V acylase from Streptomyces lavendulae in water–orga...
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| Veröffentlicht in: | Enzyme and microbial technology 2000-07, Vol.27 (1), p.122-126 |
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| creator | Arroyo, Miguel Torres-Guzmán, Raquel de la Mata, Isabel Castillón, M.Pilar Acebal, Carmen |
| description | Hydrolytic activity of penicillin V acylase (EC 3.5.1.11) can be improved by using organic cosolvents in monophasic systems. However, the addition of these solvents may result in loss of stability of the enzyme. The thermal stability of penicillin V acylase from
Streptomyces lavendulae in water–organic cosolvent monophasic systems depends on the nature of the organic solvent and its concentration in the media. The threshold solvent concentration (at which half enzymatic activity is displayed) is related to the denaturing capacity of the solvent. We found out linear correlations between the free energy of denaturation at 40°C and the concentration of the solvent in the media. On one hand, those solvents with logP values lower than −1.8 have a protective effect that is enhanced when its concentration is increased in the medium. On the other hand, those solvents with logP values higher than −1.8 have a denaturing effect: the higher this value and concentration, the more deleterious. Deactivation constants of PVA at 40°C can be predicted in any monophasic system containing a water-miscible solvent. |
| doi_str_mv | 10.1016/S0141-0229(00)00183-6 |
| format | Article |
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Streptomyces lavendulae in water–organic cosolvent monophasic systems depends on the nature of the organic solvent and its concentration in the media. The threshold solvent concentration (at which half enzymatic activity is displayed) is related to the denaturing capacity of the solvent. We found out linear correlations between the free energy of denaturation at 40°C and the concentration of the solvent in the media. On one hand, those solvents with logP values lower than −1.8 have a protective effect that is enhanced when its concentration is increased in the medium. On the other hand, those solvents with logP values higher than −1.8 have a denaturing effect: the higher this value and concentration, the more deleterious. Deactivation constants of PVA at 40°C can be predicted in any monophasic system containing a water-miscible solvent.</description><identifier>ISSN: 0141-0229</identifier><identifier>EISSN: 1879-0909</identifier><identifier>DOI: 10.1016/S0141-0229(00)00183-6</identifier><identifier>PMID: 10862911</identifier><identifier>CODEN: EMTED2</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>Bacteria ; Bioconversions. Hemisynthesis ; Biological and medical sciences ; Biotechnology ; Composition ; Enzyme kinetics ; Enzyme stability ; Fundamental and applied biological sciences. Psychology ; logP ; Methods. Procedures. Technologies ; Monophasic systems ; Organic solvents ; Penicillin V acylase ; Streptomyces lavendulae ; Thermodynamic stability ; Water</subject><ispartof>Enzyme and microbial technology, 2000-07, Vol.27 (1), p.122-126</ispartof><rights>2000 Elsevier Science Inc.</rights><rights>2000 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-7398351c40432013af61adf7de4042e145b9fa35e156abb7e168a9be9e6fc5673</citedby><cites>FETCH-LOGICAL-c454t-7398351c40432013af61adf7de4042e145b9fa35e156abb7e168a9be9e6fc5673</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0141-0229(00)00183-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1405518$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10862911$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Arroyo, Miguel</creatorcontrib><creatorcontrib>Torres-Guzmán, Raquel</creatorcontrib><creatorcontrib>de la Mata, Isabel</creatorcontrib><creatorcontrib>Castillón, M.Pilar</creatorcontrib><creatorcontrib>Acebal, Carmen</creatorcontrib><title>Prediction of penicillin V acylase stability in water-organic co-solvent monophasic systems as a function of solvent composition</title><title>Enzyme and microbial technology</title><addtitle>Enzyme Microb Technol</addtitle><description>Hydrolytic activity of penicillin V acylase (EC 3.5.1.11) can be improved by using organic cosolvents in monophasic systems. However, the addition of these solvents may result in loss of stability of the enzyme. The thermal stability of penicillin V acylase from
Streptomyces lavendulae in water–organic cosolvent monophasic systems depends on the nature of the organic solvent and its concentration in the media. The threshold solvent concentration (at which half enzymatic activity is displayed) is related to the denaturing capacity of the solvent. We found out linear correlations between the free energy of denaturation at 40°C and the concentration of the solvent in the media. On one hand, those solvents with logP values lower than −1.8 have a protective effect that is enhanced when its concentration is increased in the medium. On the other hand, those solvents with logP values higher than −1.8 have a denaturing effect: the higher this value and concentration, the more deleterious. Deactivation constants of PVA at 40°C can be predicted in any monophasic system containing a water-miscible solvent.</description><subject>Bacteria</subject><subject>Bioconversions. Hemisynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Composition</subject><subject>Enzyme kinetics</subject><subject>Enzyme stability</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>logP</subject><subject>Methods. Procedures. Technologies</subject><subject>Monophasic systems</subject><subject>Organic solvents</subject><subject>Penicillin V acylase</subject><subject>Streptomyces lavendulae</subject><subject>Thermodynamic stability</subject><subject>Water</subject><issn>0141-0229</issn><issn>1879-0909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNqFkU2LFDEQhoMo7uzoT1ByEFkPrVXpJN05iSyuCgsKflxDOl2tke7OmPSszM2fbmZnXD25EAi8PPUm1MPYI4TnCKhffASUWIEQ5gzgGQC2daXvsBW2janAgLnLVjfICTvN-TsUSkq4z04QWi0M4or9-pCoD34JceZx4Buagw_jGGb-hTu_G10mnhfXhTEsO17in26hVMX01RWS-1jlOF7RvPApznHzzeWS5l1eaMrclcOH7XxT_4f1cdrEHPbxA3ZvcGOmh8d7zT5fvP50_ra6fP_m3fmry8pLJZeqqU1bK_QSZC0AazdodP3Q9FQSQShVZwZXK0KlXdc1hLp1piNDevBKN_WaPT30blL8saW82ClkT-PoZorbbEVZTWPEHjz7L4itMrXQEm7vxKZBLbQooDqAPsWcEw12k8Lk0s4i2L1Oe63T7l1ZAHut0-oy9_j4wLabqP9n6uCvAE-OgMvejUNysw_5LydBqVK1Zi8PGJUNXwVKNvtAsy_qE_nF9jHc8pPfVPe9RQ</recordid><startdate>20000701</startdate><enddate>20000701</enddate><creator>Arroyo, Miguel</creator><creator>Torres-Guzmán, Raquel</creator><creator>de la Mata, Isabel</creator><creator>Castillón, M.Pilar</creator><creator>Acebal, Carmen</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20000701</creationdate><title>Prediction of penicillin V acylase stability in water-organic co-solvent monophasic systems as a function of solvent composition</title><author>Arroyo, Miguel ; Torres-Guzmán, Raquel ; de la Mata, Isabel ; Castillón, M.Pilar ; Acebal, Carmen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c454t-7398351c40432013af61adf7de4042e145b9fa35e156abb7e168a9be9e6fc5673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Bacteria</topic><topic>Bioconversions. Hemisynthesis</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Composition</topic><topic>Enzyme kinetics</topic><topic>Enzyme stability</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>logP</topic><topic>Methods. Procedures. 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However, the addition of these solvents may result in loss of stability of the enzyme. The thermal stability of penicillin V acylase from
Streptomyces lavendulae in water–organic cosolvent monophasic systems depends on the nature of the organic solvent and its concentration in the media. The threshold solvent concentration (at which half enzymatic activity is displayed) is related to the denaturing capacity of the solvent. We found out linear correlations between the free energy of denaturation at 40°C and the concentration of the solvent in the media. On one hand, those solvents with logP values lower than −1.8 have a protective effect that is enhanced when its concentration is increased in the medium. On the other hand, those solvents with logP values higher than −1.8 have a denaturing effect: the higher this value and concentration, the more deleterious. Deactivation constants of PVA at 40°C can be predicted in any monophasic system containing a water-miscible solvent.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><pmid>10862911</pmid><doi>10.1016/S0141-0229(00)00183-6</doi><tpages>5</tpages></addata></record> |
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| subjects | Bacteria Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology Composition Enzyme kinetics Enzyme stability Fundamental and applied biological sciences. Psychology logP Methods. Procedures. Technologies Monophasic systems Organic solvents Penicillin V acylase Streptomyces lavendulae Thermodynamic stability Water |
| title | Prediction of penicillin V acylase stability in water-organic co-solvent monophasic systems as a function of solvent composition |
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