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

Detalhes bibliográficos
Autor(a) principal: Lopes,Danielle Branta
Data de Publicação: 2011
Outros Autores: Fraga,Laira Priscila, Fleuri,Luciana Francisco, Macedo,Gabriela Alves
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Food Science and Technology (Campinas)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612011000300009
Resumo: Enzyme 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.
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spelling Lipase and esterase: to what extent can this classification be applied accurately?lipaseesterasecutinaselipase specific activityesterase specific activityEnzyme 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.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2011-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612011000300009Food Science and Technology v.31 n.3 2011reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/S0101-20612011000300009info:eu-repo/semantics/openAccessLopes,Danielle BrantaFraga,Laira PriscilaFleuri,Luciana FranciscoMacedo,Gabriela Alveseng2011-10-21T00:00:00Zoai:scielo:S0101-20612011000300009Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2011-10-21T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false
dc.title.none.fl_str_mv Lipase and esterase: to what extent can this classification be applied accurately?
title Lipase and esterase: to what extent can this classification be applied accurately?
spellingShingle Lipase and esterase: to what extent can this classification be applied accurately?
Lopes,Danielle Branta
lipase
esterase
cutinase
lipase specific activity
esterase specific activity
title_short Lipase and esterase: to what extent can this classification be applied accurately?
title_full Lipase and esterase: to what extent can this classification be applied accurately?
title_fullStr Lipase and esterase: to what extent can this classification be applied accurately?
title_full_unstemmed Lipase and esterase: to what extent can this classification be applied accurately?
title_sort Lipase and esterase: to what extent can this classification be applied accurately?
author Lopes,Danielle Branta
author_facet Lopes,Danielle Branta
Fraga,Laira Priscila
Fleuri,Luciana Francisco
Macedo,Gabriela Alves
author_role author
author2 Fraga,Laira Priscila
Fleuri,Luciana Francisco
Macedo,Gabriela Alves
author2_role author
author
author
dc.contributor.author.fl_str_mv Lopes,Danielle Branta
Fraga,Laira Priscila
Fleuri,Luciana Francisco
Macedo,Gabriela Alves
dc.subject.por.fl_str_mv lipase
esterase
cutinase
lipase specific activity
esterase specific activity
topic lipase
esterase
cutinase
lipase specific activity
esterase specific activity
description Enzyme 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.
publishDate 2011
dc.date.none.fl_str_mv 2011-09-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
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dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612011000300009
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612011000300009
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0101-20612011000300009
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Ciência e Tecnologia de Alimentos
publisher.none.fl_str_mv Sociedade Brasileira de Ciência e Tecnologia de Alimentos
dc.source.none.fl_str_mv Food Science and Technology v.31 n.3 2011
reponame:Food Science and Technology (Campinas)
instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
instacron:SBCTA
instname_str Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
instacron_str SBCTA
institution SBCTA
reponame_str Food Science and Technology (Campinas)
collection Food Science and Technology (Campinas)
repository.name.fl_str_mv Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
repository.mail.fl_str_mv ||revista@sbcta.org.br
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