Lipase and esterase - to what extent can this classification be applied accurately?

dc.creatorLopes, DB
dc.creatorFraga, LP
dc.creatorFleuri, LF
dc.creatorMacedo, GA
dc.date2011
dc.dateJUL-SEP
dc.date2014-08-01T18:35:23Z
dc.date2015-11-26T18:04:19Z
dc.date2014-08-01T18:35:23Z
dc.date2015-11-26T18:04:19Z
dc.date.accessioned2018-03-29T00:46:25Z
dc.date.available2018-03-29T00:46:25Z
dc.identifierCiencia E Tecnologia De Alimentos. Soc Brasileira Ciencia Tecnologia Alimentos, v. 31, n. 3, n. 608, n. 613, 2011.
dc.identifier0101-2061
dc.identifier1678-457X
dc.identifierWOS:000297040700009
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/81155
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/81155
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1292815
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionEnzyme technology is an ever-growing field of knowledge and, in recent years, this technology has raised renewed interest, due to the search for new paradigms in several productive processes. Lipases, esterases and cutinases are enzymes used in a wide range of processes involving synthesis and hydrolysis reactions. The objective of this work was to investigate and compare the specific lipase and esterase activities of five enzymes - four already classified as lipases and one classified as cutinase - in the presence of natural and synthetic substrates. All tested enzymes presented both esterase and lipase specific activities. The highest specific esterase activity was observed for Aspergillus 1068 lipase in natural substrate and for F. oxysporum cutinase in synthetic substrate, while the highest specific lipase activity was observed for Geotrichum sp. lipase in natural substrate and for F. oxysporum cutinase in synthetic substrate. These results display some interface-independent lipolytic activity for all lipases tested. This is in accordance with the rationale that a new and broader definition of lipases may be necessary.
dc.description31
dc.description3
dc.description608
dc.description613
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageen
dc.publisherSoc Brasileira Ciencia Tecnologia Alimentos
dc.publisherCampinas
dc.publisherBrasil
dc.relationCiencia E Tecnologia De Alimentos
dc.relationCiencia Tecnol. Aliment.
dc.rightsaberto
dc.sourceWeb of Science
dc.subjectlipase
dc.subjectesterase
dc.subjectcutinase
dc.subjectlipase specific activity
dc.subjectesterase specific activity
dc.subject(s)-ketoprofen Ethyl-ester
dc.subjectAlpha/beta-hydrolase Fold
dc.subjectNitrophenyl Palmitate
dc.subjectSensitive Method
dc.subjectCutinase
dc.subjectEnzyme
dc.subjectSelectivity
dc.subjectProteins
dc.subjectSequence
dc.subjectSolvent
dc.titleLipase and esterase - to what extent can this classification be applied accurately?
dc.typeArtículos de revistas


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