Cutinase structure, function and biocatalytic applications
This review analyses the role of cutinases in nature and their potential biotechnological applications. The cloning and expression of a fungal cutinase from Fusarium solani f. pisi, in Escherichia coli and Saccharomyces cerevisiae hosts are described. The three dimensional structure of this cutinase...
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| Veröffentlicht in: | Electronic Journal of Biotechnology 2003-04, Vol.1 (3) |
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| container_title | Electronic Journal of Biotechnology |
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| creator | Carvalho, Cristina M. L Aires-Barros, Maria Raquel Cabral, Joaquim M. S |
| description | This review analyses the role of cutinases in nature and their
potential biotechnological applications. The cloning and expression of
a fungal cutinase from Fusarium solani f. pisi, in Escherichia coli
and Saccharomyces cerevisiae hosts are described. The three
dimensional structure of this cutinase is also analysed and its
function as a lipase discussed and compared with other lipases. The
biocatalytic applications of cutinase are described taking into account
the preparation of different cutinase forms and the media where the
different types of enzymatic reactions have been performed, namely
hydrolysis, esterification, transesterification and resolution of
racemic mixtures. The stability of cutinase preparations is discussed,
particularly in anionic reversed micelles considering the role of
hexanol as substrate, co-surfactant and stabilizer. Process development
based on the operation of cutinase reactors is also reviewed. |
| format | Article |
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potential biotechnological applications. The cloning and expression of
a fungal cutinase from Fusarium solani f. pisi, in Escherichia coli
and Saccharomyces cerevisiae hosts are described. The three
dimensional structure of this cutinase is also analysed and its
function as a lipase discussed and compared with other lipases. The
biocatalytic applications of cutinase are described taking into account
the preparation of different cutinase forms and the media where the
different types of enzymatic reactions have been performed, namely
hydrolysis, esterification, transesterification and resolution of
racemic mixtures. The stability of cutinase preparations is discussed,
particularly in anionic reversed micelles considering the role of
hexanol as substrate, co-surfactant and stabilizer. Process development
based on the operation of cutinase reactors is also reviewed.</description><identifier>ISSN: 0717-3458</identifier><identifier>EISSN: 0717-3458</identifier><language>eng</language><publisher>Universidad Católica de Valparaíso</publisher><subject>Biocatalysis, Bioreactors, Cloning, Cutinase, Function, Stability, Structure</subject><ispartof>Electronic Journal of Biotechnology, 2003-04, Vol.1 (3)</ispartof><rights>1998 by Universidad Católica de Valparaíso -- Chile</rights><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>314,780,784,79197</link.rule.ids></links><search><creatorcontrib>Carvalho, Cristina M. L</creatorcontrib><creatorcontrib>Aires-Barros, Maria Raquel</creatorcontrib><creatorcontrib>Cabral, Joaquim M. S</creatorcontrib><title>Cutinase structure, function and biocatalytic applications</title><title>Electronic Journal of Biotechnology</title><description>This review analyses the role of cutinases in nature and their
potential biotechnological applications. The cloning and expression of
a fungal cutinase from Fusarium solani f. pisi, in Escherichia coli
and Saccharomyces cerevisiae hosts are described. The three
dimensional structure of this cutinase is also analysed and its
function as a lipase discussed and compared with other lipases. The
biocatalytic applications of cutinase are described taking into account
the preparation of different cutinase forms and the media where the
different types of enzymatic reactions have been performed, namely
hydrolysis, esterification, transesterification and resolution of
racemic mixtures. The stability of cutinase preparations is discussed,
particularly in anionic reversed micelles considering the role of
hexanol as substrate, co-surfactant and stabilizer. Process development
based on the operation of cutinase reactors is also reviewed.</description><subject>Biocatalysis, Bioreactors, Cloning, Cutinase, Function, Stability, Structure</subject><issn>0717-3458</issn><issn>0717-3458</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>RBI</sourceid><recordid>eNqVTUsKwjAUDKJg_dwhB7ASbSTVbVE8gPvyGlN4JaYheVn09mah4FYYmB_DzFgh1EGVlTzV8x-9ZKsYByGOQipZsEuTCB1EwyOFpCkFs-N9cppwdBzck3c4aiCwE6Hm4L3FbHMZN2zRg41m--E129-uj-Ze5oVFZ1of8AVhanVAaL-hGTLOdf6v_h68AdnSQ1U</recordid><startdate>20030407</startdate><enddate>20030407</enddate><creator>Carvalho, Cristina M. L</creator><creator>Aires-Barros, Maria Raquel</creator><creator>Cabral, Joaquim M. S</creator><general>Universidad Católica de Valparaíso</general><scope>RBI</scope></search><sort><creationdate>20030407</creationdate><title>Cutinase structure, function and biocatalytic applications</title><author>Carvalho, Cristina M. L ; Aires-Barros, Maria Raquel ; Cabral, Joaquim M. S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-bioline_primary_cria_bioline_ej_ej980203</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Biocatalysis, Bioreactors, Cloning, Cutinase, Function, Stability, Structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carvalho, Cristina M. L</creatorcontrib><creatorcontrib>Aires-Barros, Maria Raquel</creatorcontrib><creatorcontrib>Cabral, Joaquim M. S</creatorcontrib><collection>Bioline International</collection><jtitle>Electronic Journal of Biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Carvalho, Cristina M. L</au><au>Aires-Barros, Maria Raquel</au><au>Cabral, Joaquim M. S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cutinase structure, function and biocatalytic applications</atitle><jtitle>Electronic Journal of Biotechnology</jtitle><date>2003-04-07</date><risdate>2003</risdate><volume>1</volume><issue>3</issue><issn>0717-3458</issn><eissn>0717-3458</eissn><abstract>This review analyses the role of cutinases in nature and their
potential biotechnological applications. The cloning and expression of
a fungal cutinase from Fusarium solani f. pisi, in Escherichia coli
and Saccharomyces cerevisiae hosts are described. The three
dimensional structure of this cutinase is also analysed and its
function as a lipase discussed and compared with other lipases. The
biocatalytic applications of cutinase are described taking into account
the preparation of different cutinase forms and the media where the
different types of enzymatic reactions have been performed, namely
hydrolysis, esterification, transesterification and resolution of
racemic mixtures. The stability of cutinase preparations is discussed,
particularly in anionic reversed micelles considering the role of
hexanol as substrate, co-surfactant and stabilizer. Process development
based on the operation of cutinase reactors is also reviewed.</abstract><pub>Universidad Católica de Valparaíso</pub></addata></record> |
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| ispartof | Electronic Journal of Biotechnology, 2003-04, Vol.1 (3) |
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| language | eng |
| recordid | cdi_bioline_primary_cria_bioline_ej_ej98020 |
| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Bioline International; Free Full-Text Journals in Chemistry |
| subjects | Biocatalysis, Bioreactors, Cloning, Cutinase, Function, Stability, Structure |
| title | Cutinase structure, function and biocatalytic applications |
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