Activity and Stability Studies Of Mucor miehei Lipase Immobilized in Novel Microemulsion-based Organogels
Lipase from Mucor miehei was immobilized in bis-(2-ethylhexyl)sulfosuccinate sodium salt (AOT) as well as lecithin water-in-oil (w/o) microemulsion-based organogels (MBGs) formulated with biopolymers such as agar and hydroxypropylmethyl cellulose (HPMC), respectively. These lipase-containing MBGs pr...
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Veröffentlicht in: | Biocatalysis and biotransformation 2002-01, Vol.20 (5), p.319-327 |
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creator | Delimitsou, Charikleia Zoumpanioti, Maria Xenakis, Aristotelis Stamatis, Haralambos |
description | Lipase from Mucor miehei was immobilized in bis-(2-ethylhexyl)sulfosuccinate sodium salt (AOT) as well as lecithin water-in-oil (w/o) microemulsion-based organogels (MBGs) formulated with biopolymers such as agar and hydroxypropylmethyl cellulose (HPMC), respectively. These lipase-containing MBGs prove to be novel solid-phase catalysts for use in organic media. Using these organogels at 25°C, various esterification reactions in non-polar solvents as well as in solvent free systems were possible. Apparent lipase activity was influenced to some extent by the nature and the concentration of biopolymers used. Lipase stability in such MBGs is much higher than that observed in w/o microemulsions. MBGs containing lipase functioned effectively in repeated batch syntheses of fatty esters. Kinetic studies have shown that ester synthesis catalyzed by immobilized lipase occurs via the Ping-Pong bi-bi mechanism in which only inhibition by excess of alcohol has been identified. Values of all kinetic parameters were determined. |
doi_str_mv | 10.1080/10242420290025539 |
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These lipase-containing MBGs prove to be novel solid-phase catalysts for use in organic media. Using these organogels at 25°C, various esterification reactions in non-polar solvents as well as in solvent free systems were possible. Apparent lipase activity was influenced to some extent by the nature and the concentration of biopolymers used. Lipase stability in such MBGs is much higher than that observed in w/o microemulsions. MBGs containing lipase functioned effectively in repeated batch syntheses of fatty esters. Kinetic studies have shown that ester synthesis catalyzed by immobilized lipase occurs via the Ping-Pong bi-bi mechanism in which only inhibition by excess of alcohol has been identified. 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These lipase-containing MBGs prove to be novel solid-phase catalysts for use in organic media. Using these organogels at 25°C, various esterification reactions in non-polar solvents as well as in solvent free systems were possible. Apparent lipase activity was influenced to some extent by the nature and the concentration of biopolymers used. Lipase stability in such MBGs is much higher than that observed in w/o microemulsions. MBGs containing lipase functioned effectively in repeated batch syntheses of fatty esters. Kinetic studies have shown that ester synthesis catalyzed by immobilized lipase occurs via the Ping-Pong bi-bi mechanism in which only inhibition by excess of alcohol has been identified. Values of all kinetic parameters were determined.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Enzyme engineering</subject><subject>Esterification</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immobilization</subject><subject>Immobilization of enzymes and other molecules</subject><subject>Immobilization techniques</subject><subject>Kinetics</subject><subject>Lipase</subject><subject>Methods. Procedures. 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Psychology</topic><topic>Immobilization</topic><topic>Immobilization of enzymes and other molecules</topic><topic>Immobilization techniques</topic><topic>Kinetics</topic><topic>Lipase</topic><topic>Methods. Procedures. Technologies</topic><topic>Microemulsions</topic><topic>Miscellaneous</topic><topic>Mucor miehei</topic><topic>Organogel</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Delimitsou, Charikleia</creatorcontrib><creatorcontrib>Zoumpanioti, Maria</creatorcontrib><creatorcontrib>Xenakis, Aristotelis</creatorcontrib><creatorcontrib>Stamatis, Haralambos</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biocatalysis and biotransformation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Delimitsou, Charikleia</au><au>Zoumpanioti, Maria</au><au>Xenakis, Aristotelis</au><au>Stamatis, Haralambos</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activity and Stability Studies Of Mucor miehei Lipase Immobilized in Novel Microemulsion-based Organogels</atitle><jtitle>Biocatalysis and biotransformation</jtitle><date>2002-01-01</date><risdate>2002</risdate><volume>20</volume><issue>5</issue><spage>319</spage><epage>327</epage><pages>319-327</pages><issn>1024-2422</issn><eissn>1029-2446</eissn><abstract>Lipase from Mucor miehei was immobilized in bis-(2-ethylhexyl)sulfosuccinate sodium salt (AOT) as well as lecithin water-in-oil (w/o) microemulsion-based organogels (MBGs) formulated with biopolymers such as agar and hydroxypropylmethyl cellulose (HPMC), respectively. These lipase-containing MBGs prove to be novel solid-phase catalysts for use in organic media. Using these organogels at 25°C, various esterification reactions in non-polar solvents as well as in solvent free systems were possible. Apparent lipase activity was influenced to some extent by the nature and the concentration of biopolymers used. Lipase stability in such MBGs is much higher than that observed in w/o microemulsions. MBGs containing lipase functioned effectively in repeated batch syntheses of fatty esters. Kinetic studies have shown that ester synthesis catalyzed by immobilized lipase occurs via the Ping-Pong bi-bi mechanism in which only inhibition by excess of alcohol has been identified. Values of all kinetic parameters were determined.</abstract><cop>Abingdon</cop><pub>Informa UK Ltd</pub><doi>10.1080/10242420290025539</doi><tpages>9</tpages></addata></record> |
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subjects | Biological and medical sciences Biotechnology Enzyme engineering Esterification Fundamental and applied biological sciences. Psychology Immobilization Immobilization of enzymes and other molecules Immobilization techniques Kinetics Lipase Methods. Procedures. Technologies Microemulsions Miscellaneous Mucor miehei Organogel |
title | Activity and Stability Studies Of Mucor miehei Lipase Immobilized in Novel Microemulsion-based Organogels |
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