Kinetics, mechanism, and time course analysis of lipase-catalyzed hydrolysis of high concentration olive oil in AOT-isooctane reversed micelles

Candida rugosa lipase has been used to investigate the hydrolysis of high concentration olive oil in the AOT-isooctane reversed micellar system at w(o) = 10, pH 7.1, and 37 degrees C. Results from this work show the hydrolytic reaction obeys Michaelis-Menten kinetics up to the initial substrate conc...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biotechnology and bioengineering 1991-06, Vol.38 (2), p.206-211
Hauptverfasser: Tsai, Shau-Wei, Chiang, Chen-Li
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 211
container_issue 2
container_start_page 206
container_title Biotechnology and bioengineering
container_volume 38
creator Tsai, Shau-Wei
Chiang, Chen-Li
description Candida rugosa lipase has been used to investigate the hydrolysis of high concentration olive oil in the AOT-isooctane reversed micellar system at w(o) = 10, pH 7.1, and 37 degrees C. Results from this work show the hydrolytic reaction obeys Michaelis-Menten kinetics up to the initial substrate concentration of 1.37 M, with turnover number k(cat) and Michaelis constant Km of 67.1 micromoles/min mg enzyme and 0.717 M, respectively. A competitive inhibition by the main product, oleic acid, has been found with a dissociation constant Ki for the complex EP( ) of 0.089 M. The rate equation was further analyzed in the time course reaction and was found in agreement with the experimental results for lower substrate concentrations, up to 0.341 M. Large deviations occurred at high substrate concentrations, which may be due to the effects of large consumption of water on kinetics, on the formation of glycerol, and on the deactivation of lipase in the hydrolysis reaction as well.
doi_str_mv 10.1002/bit.260380213
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_16028773</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>16028773</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5293-107e573377aabad28df5614663dc9f9341c30a8052609f76957bdb7e4a04c8003</originalsourceid><addsrcrecordid>eNp9kUFv1DAQhS0EotuFI1fkA-LUlHG8seNjW0FbUehWbIXExXKcSdeQxIudbVn-BH8ZrzbacuJkj_3Ne08zhLxicMwA8neVG45zAbyEnPEnZMJAyQxyBU_JBABExguVH5DDGL-nUpZCPCcHrBTpXrAJ-fPR9Tg4G49oh3Zpehe7I2r6mg6uQ2r9OkRMtWk30UXqG9q6lYmYWTOkt99Y0-WmDn7_vXR3y9TWW-yHYAbne-pbd4_Uu5a6np5cLzIXvbeD6ZEGvMdkUNPOWWxbjC_Is8a0EV-O55Tcfni_OLvIrq7PL89OrjJb5IpnDCQWknMpjalMnZd1Uwg2E4LXVjWKz5jlYEoo0mhUI4UqZFVXEmcGZrYE4FPydqe7Cv7nGuOgOxe3EVIqv46aCchLmRymJNuBNvgYAzZ6FVxnwkYz0NsN6LQBvd9A4l-Pwuuqw_qRHkeegDcjYKI1bRNMb13ccwUUMpcqYXKHPbgWN_831aeXi38TjIldHPDXvtOEH1pILgv99fO5hk83Fzff5nM9f0zcGK_NXUhhbr8wpTiwHLaKfwFUk7hD</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16028773</pqid></control><display><type>article</type><title>Kinetics, mechanism, and time course analysis of lipase-catalyzed hydrolysis of high concentration olive oil in AOT-isooctane reversed micelles</title><source>Wiley-Blackwell Journals</source><creator>Tsai, Shau-Wei ; Chiang, Chen-Li</creator><creatorcontrib>Tsai, Shau-Wei ; Chiang, Chen-Li ; Private Agencies Collaborating Together (Organization) (USA). United States. Agency for International Development. Bureau for Food for Peace and Voluntary Assistance. Office of Private and Voluntary Cooperation ; National Cheng Kung University, Tainan, Taiwan, Republic of China</creatorcontrib><description>Candida rugosa lipase has been used to investigate the hydrolysis of high concentration olive oil in the AOT-isooctane reversed micellar system at w(o) = 10, pH 7.1, and 37 degrees C. Results from this work show the hydrolytic reaction obeys Michaelis-Menten kinetics up to the initial substrate concentration of 1.37 M, with turnover number k(cat) and Michaelis constant Km of 67.1 micromoles/min mg enzyme and 0.717 M, respectively. A competitive inhibition by the main product, oleic acid, has been found with a dissociation constant Ki for the complex EP( ) of 0.089 M. The rate equation was further analyzed in the time course reaction and was found in agreement with the experimental results for lower substrate concentrations, up to 0.341 M. Large deviations occurred at high substrate concentrations, which may be due to the effects of large consumption of water on kinetics, on the formation of glycerol, and on the deactivation of lipase in the hydrolysis reaction as well.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.260380213</identifier><identifier>PMID: 18600751</identifier><identifier>CODEN: BIBIAU</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>aceite de oliva ; actividad enzimatica ; activite enzymatique ; Biological and medical sciences ; Biotechnology ; Candida rugosa ; competitive product inhibition ; Enzyme engineering ; enzymic activity ; Fundamental and applied biological sciences. Psychology ; hidrolisis ; huile d' olive ; hydrolyse ; hydrolysis ; lipase ; Methods. Procedures. Technologies ; Miscellaneous ; olive oil ; reversed micelles ; triacilglicerol lipasa ; triacylglycerol lipase</subject><ispartof>Biotechnology and bioengineering, 1991-06, Vol.38 (2), p.206-211</ispartof><rights>Copyright © 1991 John Wiley &amp; Sons, Inc.</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5293-107e573377aabad28df5614663dc9f9341c30a8052609f76957bdb7e4a04c8003</citedby><cites>FETCH-LOGICAL-c5293-107e573377aabad28df5614663dc9f9341c30a8052609f76957bdb7e4a04c8003</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.260380213$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbit.260380213$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=5057279$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18600751$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tsai, Shau-Wei</creatorcontrib><creatorcontrib>Chiang, Chen-Li</creatorcontrib><creatorcontrib>Private Agencies Collaborating Together (Organization) (USA). United States. Agency for International Development. Bureau for Food for Peace and Voluntary Assistance. Office of Private and Voluntary Cooperation</creatorcontrib><creatorcontrib>National Cheng Kung University, Tainan, Taiwan, Republic of China</creatorcontrib><title>Kinetics, mechanism, and time course analysis of lipase-catalyzed hydrolysis of high concentration olive oil in AOT-isooctane reversed micelles</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol. Bioeng</addtitle><description>Candida rugosa lipase has been used to investigate the hydrolysis of high concentration olive oil in the AOT-isooctane reversed micellar system at w(o) = 10, pH 7.1, and 37 degrees C. Results from this work show the hydrolytic reaction obeys Michaelis-Menten kinetics up to the initial substrate concentration of 1.37 M, with turnover number k(cat) and Michaelis constant Km of 67.1 micromoles/min mg enzyme and 0.717 M, respectively. A competitive inhibition by the main product, oleic acid, has been found with a dissociation constant Ki for the complex EP( ) of 0.089 M. The rate equation was further analyzed in the time course reaction and was found in agreement with the experimental results for lower substrate concentrations, up to 0.341 M. Large deviations occurred at high substrate concentrations, which may be due to the effects of large consumption of water on kinetics, on the formation of glycerol, and on the deactivation of lipase in the hydrolysis reaction as well.</description><subject>aceite de oliva</subject><subject>actividad enzimatica</subject><subject>activite enzymatique</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Candida rugosa</subject><subject>competitive product inhibition</subject><subject>Enzyme engineering</subject><subject>enzymic activity</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hidrolisis</subject><subject>huile d' olive</subject><subject>hydrolyse</subject><subject>hydrolysis</subject><subject>lipase</subject><subject>Methods. Procedures. Technologies</subject><subject>Miscellaneous</subject><subject>olive oil</subject><subject>reversed micelles</subject><subject>triacilglicerol lipasa</subject><subject>triacylglycerol lipase</subject><issn>0006-3592</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNp9kUFv1DAQhS0EotuFI1fkA-LUlHG8seNjW0FbUehWbIXExXKcSdeQxIudbVn-BH8ZrzbacuJkj_3Ne08zhLxicMwA8neVG45zAbyEnPEnZMJAyQxyBU_JBABExguVH5DDGL-nUpZCPCcHrBTpXrAJ-fPR9Tg4G49oh3Zpehe7I2r6mg6uQ2r9OkRMtWk30UXqG9q6lYmYWTOkt99Y0-WmDn7_vXR3y9TWW-yHYAbne-pbd4_Uu5a6np5cLzIXvbeD6ZEGvMdkUNPOWWxbjC_Is8a0EV-O55Tcfni_OLvIrq7PL89OrjJb5IpnDCQWknMpjalMnZd1Uwg2E4LXVjWKz5jlYEoo0mhUI4UqZFVXEmcGZrYE4FPydqe7Cv7nGuOgOxe3EVIqv46aCchLmRymJNuBNvgYAzZ6FVxnwkYz0NsN6LQBvd9A4l-Pwuuqw_qRHkeegDcjYKI1bRNMb13ccwUUMpcqYXKHPbgWN_831aeXi38TjIldHPDXvtOEH1pILgv99fO5hk83Fzff5nM9f0zcGK_NXUhhbr8wpTiwHLaKfwFUk7hD</recordid><startdate>19910620</startdate><enddate>19910620</enddate><creator>Tsai, Shau-Wei</creator><creator>Chiang, Chen-Li</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>19910620</creationdate><title>Kinetics, mechanism, and time course analysis of lipase-catalyzed hydrolysis of high concentration olive oil in AOT-isooctane reversed micelles</title><author>Tsai, Shau-Wei ; Chiang, Chen-Li</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5293-107e573377aabad28df5614663dc9f9341c30a8052609f76957bdb7e4a04c8003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>aceite de oliva</topic><topic>actividad enzimatica</topic><topic>activite enzymatique</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Candida rugosa</topic><topic>competitive product inhibition</topic><topic>Enzyme engineering</topic><topic>enzymic activity</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hidrolisis</topic><topic>huile d' olive</topic><topic>hydrolyse</topic><topic>hydrolysis</topic><topic>lipase</topic><topic>Methods. Procedures. Technologies</topic><topic>Miscellaneous</topic><topic>olive oil</topic><topic>reversed micelles</topic><topic>triacilglicerol lipasa</topic><topic>triacylglycerol lipase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tsai, Shau-Wei</creatorcontrib><creatorcontrib>Chiang, Chen-Li</creatorcontrib><creatorcontrib>Private Agencies Collaborating Together (Organization) (USA). United States. Agency for International Development. Bureau for Food for Peace and Voluntary Assistance. Office of Private and Voluntary Cooperation</creatorcontrib><creatorcontrib>National Cheng Kung University, Tainan, Taiwan, Republic of China</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biotechnology and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tsai, Shau-Wei</au><au>Chiang, Chen-Li</au><aucorp>Private Agencies Collaborating Together (Organization) (USA). United States. Agency for International Development. Bureau for Food for Peace and Voluntary Assistance. Office of Private and Voluntary Cooperation</aucorp><aucorp>National Cheng Kung University, Tainan, Taiwan, Republic of China</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetics, mechanism, and time course analysis of lipase-catalyzed hydrolysis of high concentration olive oil in AOT-isooctane reversed micelles</atitle><jtitle>Biotechnology and bioengineering</jtitle><addtitle>Biotechnol. Bioeng</addtitle><date>1991-06-20</date><risdate>1991</risdate><volume>38</volume><issue>2</issue><spage>206</spage><epage>211</epage><pages>206-211</pages><issn>0006-3592</issn><eissn>1097-0290</eissn><coden>BIBIAU</coden><abstract>Candida rugosa lipase has been used to investigate the hydrolysis of high concentration olive oil in the AOT-isooctane reversed micellar system at w(o) = 10, pH 7.1, and 37 degrees C. Results from this work show the hydrolytic reaction obeys Michaelis-Menten kinetics up to the initial substrate concentration of 1.37 M, with turnover number k(cat) and Michaelis constant Km of 67.1 micromoles/min mg enzyme and 0.717 M, respectively. A competitive inhibition by the main product, oleic acid, has been found with a dissociation constant Ki for the complex EP( ) of 0.089 M. The rate equation was further analyzed in the time course reaction and was found in agreement with the experimental results for lower substrate concentrations, up to 0.341 M. Large deviations occurred at high substrate concentrations, which may be due to the effects of large consumption of water on kinetics, on the formation of glycerol, and on the deactivation of lipase in the hydrolysis reaction as well.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>18600751</pmid><doi>10.1002/bit.260380213</doi><tpages>6</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-3592
ispartof Biotechnology and bioengineering, 1991-06, Vol.38 (2), p.206-211
issn 0006-3592
1097-0290
language eng
recordid cdi_proquest_miscellaneous_16028773
source Wiley-Blackwell Journals
subjects aceite de oliva
actividad enzimatica
activite enzymatique
Biological and medical sciences
Biotechnology
Candida rugosa
competitive product inhibition
Enzyme engineering
enzymic activity
Fundamental and applied biological sciences. Psychology
hidrolisis
huile d' olive
hydrolyse
hydrolysis
lipase
Methods. Procedures. Technologies
Miscellaneous
olive oil
reversed micelles
triacilglicerol lipasa
triacylglycerol lipase
title Kinetics, mechanism, and time course analysis of lipase-catalyzed hydrolysis of high concentration olive oil in AOT-isooctane reversed micelles
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-18T19%3A43%3A23IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Kinetics,%20mechanism,%20and%20time%20course%20analysis%20of%20lipase-catalyzed%20hydrolysis%20of%20high%20concentration%20olive%20oil%20in%20AOT-isooctane%20reversed%20micelles&rft.jtitle=Biotechnology%20and%20bioengineering&rft.au=Tsai,%20Shau-Wei&rft.aucorp=Private%20Agencies%20Collaborating%20Together%20(Organization)%20(USA).%20United%20States.%20Agency%20for%20International%20Development.%20Bureau%20for%20Food%20for%20Peace%20and%20Voluntary%20Assistance.%20Office%20of%20Private%20and%20Voluntary%20Cooperation&rft.date=1991-06-20&rft.volume=38&rft.issue=2&rft.spage=206&rft.epage=211&rft.pages=206-211&rft.issn=0006-3592&rft.eissn=1097-0290&rft.coden=BIBIAU&rft_id=info:doi/10.1002/bit.260380213&rft_dat=%3Cproquest_cross%3E16028773%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16028773&rft_id=info:pmid/18600751&rfr_iscdi=true