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...
Gespeichert in:
Veröffentlicht in: | Biotechnology and bioengineering 1991-06, Vol.38 (2), p.206-211 |
---|---|
Hauptverfasser: | , |
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 & 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&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 |