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Triglyceride hydrolysis and stability of a recombinant cutinase from Fusarium solani in AOT-iso-octane reversed micelles
A recombinant cutinase from Fusarium solani was encapsulated in AOT reversed micelles, Physicochemical parameters of the system were optimized relative to triolein hydrolysis. Kinetic studies of triglyceride hydrolysis showed a decrease in specificity with increase of the acyl chain length. Stabilit...
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| Published in: | Applied biochemistry and biotechnology 1995-01, Vol.50 (1), p.45-56 |
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| Language: | English |
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| container_end_page | 56 |
| container_issue | 1 |
| container_start_page | 45 |
| container_title | Applied biochemistry and biotechnology |
| container_volume | 50 |
| creator | Melo, E.P. (Instituto Superior Tecnico, Lisbon, Portugal.) Aires-Barros, M.R Cabral, J.M.S |
| description | A recombinant cutinase from Fusarium solani was encapsulated in AOT reversed micelles, Physicochemical parameters of the system were optimized relative to triolein hydrolysis. Kinetic studies of triglyceride hydrolysis showed a decrease in specificity with increase of the acyl chain length. Stability of cutinase in the system under study is lower than in aqueous solution and decreases with increase in the water content in the system (W0 = [H2O]/[AOT]). The products of triolein hydrolysis had little effect on the cutinase stability. Although glycerol did not alter the stability, oleic acid decreases the enzyme stability. The increase in log P of solvent (from iso-octane to n-dodecane) decreased the stability. Deactivation profiles were fitted with the Henley and Sadana model (1) |
| doi_str_mv | 10.1007/BF02788039 |
| format | article |
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Deactivation profiles were fitted with the Henley and Sadana model (1)</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/BF02788039</identifier><identifier>PMID: 7535515</identifier><language>eng</language><publisher>United States</publisher><subject>ACIDE OLEIQUE ; ACIDO OLEICO ; ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; BEURRE VEGETAL ; Carboxylic Ester Hydrolases - chemistry ; Dioctyl Sulfosuccinic Acid ; ENCAPSULACION ; ENCAPSULATION ; Enzyme Stability ; Fusarium - enzymology ; FUSARIUM SOLANI ; GRASAS VEGETALES ; HIDROLASAS ; HYDROLASE ; Hydrolysis ; ION ; IONES ; Kinetics ; LIPIDE ; LIPIDOS ; METHODE D'OPTIMISATION ; METODOS DE OPTIMIZACION ; Micelles ; Octanes ; PROTEINAS ; PROTEINE ; Recombinant Proteins - chemistry ; RELACIONES PLANTA AGUA ; RELATION PLANTE EAU ; SOLVANT ; SOLVENTES ; TEMPERATURA ; TEMPERATURE ; TRIGLICERIDOS ; TRIGLYCERIDE ; Triglycerides - chemistry</subject><ispartof>Applied biochemistry and biotechnology, 1995-01, Vol.50 (1), p.45-56</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></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/7535515$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Melo, E.P. 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Although glycerol did not alter the stability, oleic acid decreases the enzyme stability. The increase in log P of solvent (from iso-octane to n-dodecane) decreased the stability. Deactivation profiles were fitted with the Henley and Sadana model (1)</description><subject>ACIDE OLEIQUE</subject><subject>ACIDO OLEICO</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>BEURRE VEGETAL</subject><subject>Carboxylic Ester Hydrolases - chemistry</subject><subject>Dioctyl Sulfosuccinic Acid</subject><subject>ENCAPSULACION</subject><subject>ENCAPSULATION</subject><subject>Enzyme Stability</subject><subject>Fusarium - enzymology</subject><subject>FUSARIUM SOLANI</subject><subject>GRASAS VEGETALES</subject><subject>HIDROLASAS</subject><subject>HYDROLASE</subject><subject>Hydrolysis</subject><subject>ION</subject><subject>IONES</subject><subject>Kinetics</subject><subject>LIPIDE</subject><subject>LIPIDOS</subject><subject>METHODE D'OPTIMISATION</subject><subject>METODOS DE OPTIMIZACION</subject><subject>Micelles</subject><subject>Octanes</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>Recombinant Proteins - chemistry</subject><subject>RELACIONES PLANTA AGUA</subject><subject>RELATION PLANTE EAU</subject><subject>SOLVANT</subject><subject>SOLVENTES</subject><subject>TEMPERATURA</subject><subject>TEMPERATURE</subject><subject>TRIGLICERIDOS</subject><subject>TRIGLYCERIDE</subject><subject>Triglycerides - chemistry</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNqFkL1PwzAQxS0EgvKxMCIheWIL2Oc6tkeoKCBVYqDMkRNfilESFztB5L8nqN2Z7vTe705Pj5BLzm45Y-ruYclAac2EOSAzLqXJGBh-SGaTLDIAbU7IaUqfjHHQUh2TYyWFlFzOyM86-k0zVhi9Q_oxuhiaMflEbedo6m3pG9-PNNTU0ohVaEvf2a6n1dBPS0Jax9DS5ZBs9ENLU2hs56nv6P3rOvMpZKHqbYfT7TfGhI62vsKmwXROjmrbJLzYzzPyvnxcL56z1evTy-J-ldUg8z4T2sytYJKDy_PKcg5CIygUtVBzodkkO4c6B6ltWZVQA-ZY546BhFJJJc7Ize7vNoavAVNftD79RZhShSEVSgEDIfS_IM-15MaICbzeg0PZoiu20bc2jsW-08m_2vm1DYXdRJ-K9zeTi7kyIH4BF2eA_w</recordid><startdate>199501</startdate><enddate>199501</enddate><creator>Melo, E.P. 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(Instituto Superior Tecnico, Lisbon, Portugal.) ; Aires-Barros, M.R ; Cabral, J.M.S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f256t-3894a30512d66ca11238e27e3f3743802d6dde86258abcb2f2e6ef6d0252b7573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>ACIDE OLEIQUE</topic><topic>ACIDO OLEICO</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>BEURRE VEGETAL</topic><topic>Carboxylic Ester Hydrolases - chemistry</topic><topic>Dioctyl Sulfosuccinic Acid</topic><topic>ENCAPSULACION</topic><topic>ENCAPSULATION</topic><topic>Enzyme Stability</topic><topic>Fusarium - enzymology</topic><topic>FUSARIUM SOLANI</topic><topic>GRASAS VEGETALES</topic><topic>HIDROLASAS</topic><topic>HYDROLASE</topic><topic>Hydrolysis</topic><topic>ION</topic><topic>IONES</topic><topic>Kinetics</topic><topic>LIPIDE</topic><topic>LIPIDOS</topic><topic>METHODE D'OPTIMISATION</topic><topic>METODOS DE OPTIMIZACION</topic><topic>Micelles</topic><topic>Octanes</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>Recombinant Proteins - chemistry</topic><topic>RELACIONES PLANTA AGUA</topic><topic>RELATION PLANTE EAU</topic><topic>SOLVANT</topic><topic>SOLVENTES</topic><topic>TEMPERATURA</topic><topic>TEMPERATURE</topic><topic>TRIGLICERIDOS</topic><topic>TRIGLYCERIDE</topic><topic>Triglycerides - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Melo, E.P. (Instituto Superior Tecnico, Lisbon, Portugal.)</creatorcontrib><creatorcontrib>Aires-Barros, M.R</creatorcontrib><creatorcontrib>Cabral, J.M.S</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering 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>Melo, E.P. (Instituto Superior Tecnico, Lisbon, Portugal.)</au><au>Aires-Barros, M.R</au><au>Cabral, J.M.S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Triglyceride hydrolysis and stability of a recombinant cutinase from Fusarium solani in AOT-iso-octane reversed micelles</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><addtitle>Appl Biochem Biotechnol</addtitle><date>1995-01</date><risdate>1995</risdate><volume>50</volume><issue>1</issue><spage>45</spage><epage>56</epage><pages>45-56</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><abstract>A recombinant cutinase from Fusarium solani was encapsulated in AOT reversed micelles, Physicochemical parameters of the system were optimized relative to triolein hydrolysis. Kinetic studies of triglyceride hydrolysis showed a decrease in specificity with increase of the acyl chain length. Stability of cutinase in the system under study is lower than in aqueous solution and decreases with increase in the water content in the system (W0 = [H2O]/[AOT]). The products of triolein hydrolysis had little effect on the cutinase stability. Although glycerol did not alter the stability, oleic acid decreases the enzyme stability. The increase in log P of solvent (from iso-octane to n-dodecane) decreased the stability. Deactivation profiles were fitted with the Henley and Sadana model (1)</abstract><cop>United States</cop><pmid>7535515</pmid><doi>10.1007/BF02788039</doi><tpages>12</tpages></addata></record> |
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| ispartof | Applied biochemistry and biotechnology, 1995-01, Vol.50 (1), p.45-56 |
| issn | 0273-2289 1559-0291 |
| language | eng |
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| source | SpringerLink Online Journals Archive Complete |
| subjects | ACIDE OLEIQUE ACIDO OLEICO ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE BEURRE VEGETAL Carboxylic Ester Hydrolases - chemistry Dioctyl Sulfosuccinic Acid ENCAPSULACION ENCAPSULATION Enzyme Stability Fusarium - enzymology FUSARIUM SOLANI GRASAS VEGETALES HIDROLASAS HYDROLASE Hydrolysis ION IONES Kinetics LIPIDE LIPIDOS METHODE D'OPTIMISATION METODOS DE OPTIMIZACION Micelles Octanes PROTEINAS PROTEINE Recombinant Proteins - chemistry RELACIONES PLANTA AGUA RELATION PLANTE EAU SOLVANT SOLVENTES TEMPERATURA TEMPERATURE TRIGLICERIDOS TRIGLYCERIDE Triglycerides - chemistry |
| title | Triglyceride hydrolysis and stability of a recombinant cutinase from Fusarium solani in AOT-iso-octane reversed micelles |
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