Cutinase binding and activity at the triolein–water interface monitored by oil drop tensiometry
Changes of the oil–water interfacial tension resulting from binding of Fusarium solani pisi cutinase and subsequent lipid hydrolysis were investigated using the oil drop technique. An ELISA was developed to determine the amount of cutinase bound to the triolein–water interface after biotinylation of...
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| Veröffentlicht in: | Chemistry and physics of lipids 1998-10, Vol.95 (2), p.169-180 |
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| container_title | Chemistry and physics of lipids |
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| creator | Flipsen, J.A.C Kramer, R.A van Duijnhoven, J.P.M van der Hijden, H.T.W.M Egmond, M.R Verheij, H.M |
| description | Changes of the oil–water interfacial tension resulting from binding of
Fusarium solani pisi cutinase and subsequent lipid hydrolysis were investigated using the oil drop technique. An ELISA was developed to determine the amount of cutinase bound to the triolein–water interface after biotinylation of the enzyme. Cutinase irreversibly adsorbs to a maximum value of about 2 mg/m
2. A minimal specific activity of 110
μmol/min/mg was calculated for cutinase acting on a single oil droplet, which is close to the activity found for triglyceride emulsions. At a maximum surface load cutinase could generate one monolayer of fatty acid products per second at the interface. It was found that oleic acid rapidly dissolves into the oil phase under the conditions used. The interfacial tension measured reflects the adsorption of cutinase to the oil droplet and also responds to the fate of the hydrolysis products. A model is presented that describes the catalytic events at the oil–water interface during lipid hydrolysis. |
| doi_str_mv | 10.1016/S0009-3084(98)00072-3 |
| format | Article |
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Fusarium solani pisi cutinase and subsequent lipid hydrolysis were investigated using the oil drop technique. An ELISA was developed to determine the amount of cutinase bound to the triolein–water interface after biotinylation of the enzyme. Cutinase irreversibly adsorbs to a maximum value of about 2 mg/m
2. A minimal specific activity of 110
μmol/min/mg was calculated for cutinase acting on a single oil droplet, which is close to the activity found for triglyceride emulsions. At a maximum surface load cutinase could generate one monolayer of fatty acid products per second at the interface. It was found that oleic acid rapidly dissolves into the oil phase under the conditions used. The interfacial tension measured reflects the adsorption of cutinase to the oil droplet and also responds to the fate of the hydrolysis products. A model is presented that describes the catalytic events at the oil–water interface during lipid hydrolysis.</description><identifier>ISSN: 0009-3084</identifier><identifier>EISSN: 1873-2941</identifier><identifier>DOI: 10.1016/S0009-3084(98)00072-3</identifier><identifier>PMID: 9853365</identifier><language>eng</language><publisher>Ireland: Elsevier Ireland Ltd</publisher><subject>Adsorption ; Biotin ; Carboxylic Ester Hydrolases - chemistry ; Carboxylic Ester Hydrolases - metabolism ; Chemical Phenomena ; Chemistry, Physical ; Cutinase ; Fusarium - enzymology ; Hydrolysis ; Interfacial binding ; Kinetics ; Lipid Metabolism ; Lipids - chemistry ; Lipolysis ; Models, Chemical ; Oil drop tensiometer ; Oleic acid diffusion ; Qualitative model ; Surface Tension ; Triolein ; Triolein hydrolysis ; Water</subject><ispartof>Chemistry and physics of lipids, 1998-10, Vol.95 (2), p.169-180</ispartof><rights>1998 Elsevier Science Ireland Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c360t-ef1841275cdd7ff59a9d4c27a534539069b1406e911c5be15b5bf3f2052bc6753</citedby><cites>FETCH-LOGICAL-c360t-ef1841275cdd7ff59a9d4c27a534539069b1406e911c5be15b5bf3f2052bc6753</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0009308498000723$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9853365$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Flipsen, J.A.C</creatorcontrib><creatorcontrib>Kramer, R.A</creatorcontrib><creatorcontrib>van Duijnhoven, J.P.M</creatorcontrib><creatorcontrib>van der Hijden, H.T.W.M</creatorcontrib><creatorcontrib>Egmond, M.R</creatorcontrib><creatorcontrib>Verheij, H.M</creatorcontrib><title>Cutinase binding and activity at the triolein–water interface monitored by oil drop tensiometry</title><title>Chemistry and physics of lipids</title><addtitle>Chem Phys Lipids</addtitle><description>Changes of the oil–water interfacial tension resulting from binding of
Fusarium solani pisi cutinase and subsequent lipid hydrolysis were investigated using the oil drop technique. An ELISA was developed to determine the amount of cutinase bound to the triolein–water interface after biotinylation of the enzyme. Cutinase irreversibly adsorbs to a maximum value of about 2 mg/m
2. A minimal specific activity of 110
μmol/min/mg was calculated for cutinase acting on a single oil droplet, which is close to the activity found for triglyceride emulsions. At a maximum surface load cutinase could generate one monolayer of fatty acid products per second at the interface. It was found that oleic acid rapidly dissolves into the oil phase under the conditions used. The interfacial tension measured reflects the adsorption of cutinase to the oil droplet and also responds to the fate of the hydrolysis products. A model is presented that describes the catalytic events at the oil–water interface during lipid hydrolysis.</description><subject>Adsorption</subject><subject>Biotin</subject><subject>Carboxylic Ester Hydrolases - chemistry</subject><subject>Carboxylic Ester Hydrolases - metabolism</subject><subject>Chemical Phenomena</subject><subject>Chemistry, Physical</subject><subject>Cutinase</subject><subject>Fusarium - enzymology</subject><subject>Hydrolysis</subject><subject>Interfacial binding</subject><subject>Kinetics</subject><subject>Lipid Metabolism</subject><subject>Lipids - chemistry</subject><subject>Lipolysis</subject><subject>Models, Chemical</subject><subject>Oil drop tensiometer</subject><subject>Oleic acid diffusion</subject><subject>Qualitative model</subject><subject>Surface Tension</subject><subject>Triolein</subject><subject>Triolein hydrolysis</subject><subject>Water</subject><issn>0009-3084</issn><issn>1873-2941</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM9O3DAQxq2qiC7QR0DyCbWHgB3HSXyqqlX5I63EoeVsOfaknSqxF9sB7Y134A15EgK72iuXGX2a75vR_Ag55eycM15f_GaMqUKwtvqm2u-zaMpCfCIL3jaiKFXFP5PF3vKFHKX0f5ZMSn5IDlUrhajlgpjllNGbBLRD79D_pcY7amzGB8wbajLN_4DmiGEA9C9Pz48mQ6To59obC3QMHnOI4Gi3oQEH6mJY0ww-YRghx80JOejNkODrrh-Tu8tff5bXxer26mb5c1VYUbNcQM_bipeNtM41fS-VUa6yZWOkqKRQrFYdr1gNinMrO-Cyk10v-pLJsrN1I8UxOdvuXcdwP0HKesRkYRiMhzAlXSvWlo2qZqPcGm0MKUXo9TriaOJGc6bf0Op3tPqNm1atfkerxZw73R2YuhHcPrVjOc9_bOcwf_mAEHWyCN6Cwwg2axfwgwuvHYeKkw</recordid><startdate>19981001</startdate><enddate>19981001</enddate><creator>Flipsen, J.A.C</creator><creator>Kramer, R.A</creator><creator>van Duijnhoven, J.P.M</creator><creator>van der Hijden, H.T.W.M</creator><creator>Egmond, M.R</creator><creator>Verheij, H.M</creator><general>Elsevier Ireland Ltd</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>19981001</creationdate><title>Cutinase binding and activity at the triolein–water interface monitored by oil drop tensiometry</title><author>Flipsen, J.A.C ; Kramer, R.A ; van Duijnhoven, J.P.M ; van der Hijden, H.T.W.M ; Egmond, M.R ; Verheij, H.M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c360t-ef1841275cdd7ff59a9d4c27a534539069b1406e911c5be15b5bf3f2052bc6753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Adsorption</topic><topic>Biotin</topic><topic>Carboxylic Ester Hydrolases - chemistry</topic><topic>Carboxylic Ester Hydrolases - metabolism</topic><topic>Chemical Phenomena</topic><topic>Chemistry, Physical</topic><topic>Cutinase</topic><topic>Fusarium - enzymology</topic><topic>Hydrolysis</topic><topic>Interfacial binding</topic><topic>Kinetics</topic><topic>Lipid Metabolism</topic><topic>Lipids - chemistry</topic><topic>Lipolysis</topic><topic>Models, Chemical</topic><topic>Oil drop tensiometer</topic><topic>Oleic acid diffusion</topic><topic>Qualitative model</topic><topic>Surface Tension</topic><topic>Triolein</topic><topic>Triolein hydrolysis</topic><topic>Water</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Flipsen, J.A.C</creatorcontrib><creatorcontrib>Kramer, R.A</creatorcontrib><creatorcontrib>van Duijnhoven, J.P.M</creatorcontrib><creatorcontrib>van der Hijden, H.T.W.M</creatorcontrib><creatorcontrib>Egmond, M.R</creatorcontrib><creatorcontrib>Verheij, H.M</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>Chemistry and physics of lipids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Flipsen, J.A.C</au><au>Kramer, R.A</au><au>van Duijnhoven, J.P.M</au><au>van der Hijden, H.T.W.M</au><au>Egmond, M.R</au><au>Verheij, H.M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cutinase binding and activity at the triolein–water interface monitored by oil drop tensiometry</atitle><jtitle>Chemistry and physics of lipids</jtitle><addtitle>Chem Phys Lipids</addtitle><date>1998-10-01</date><risdate>1998</risdate><volume>95</volume><issue>2</issue><spage>169</spage><epage>180</epage><pages>169-180</pages><issn>0009-3084</issn><eissn>1873-2941</eissn><abstract>Changes of the oil–water interfacial tension resulting from binding of
Fusarium solani pisi cutinase and subsequent lipid hydrolysis were investigated using the oil drop technique. An ELISA was developed to determine the amount of cutinase bound to the triolein–water interface after biotinylation of the enzyme. Cutinase irreversibly adsorbs to a maximum value of about 2 mg/m
2. A minimal specific activity of 110
μmol/min/mg was calculated for cutinase acting on a single oil droplet, which is close to the activity found for triglyceride emulsions. At a maximum surface load cutinase could generate one monolayer of fatty acid products per second at the interface. It was found that oleic acid rapidly dissolves into the oil phase under the conditions used. The interfacial tension measured reflects the adsorption of cutinase to the oil droplet and also responds to the fate of the hydrolysis products. A model is presented that describes the catalytic events at the oil–water interface during lipid hydrolysis.</abstract><cop>Ireland</cop><pub>Elsevier Ireland Ltd</pub><pmid>9853365</pmid><doi>10.1016/S0009-3084(98)00072-3</doi><tpages>12</tpages></addata></record> |
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| subjects | Adsorption Biotin Carboxylic Ester Hydrolases - chemistry Carboxylic Ester Hydrolases - metabolism Chemical Phenomena Chemistry, Physical Cutinase Fusarium - enzymology Hydrolysis Interfacial binding Kinetics Lipid Metabolism Lipids - chemistry Lipolysis Models, Chemical Oil drop tensiometer Oleic acid diffusion Qualitative model Surface Tension Triolein Triolein hydrolysis Water |
| title | Cutinase binding and activity at the triolein–water interface monitored by oil drop tensiometry |
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