Lipase and esterase: to what extent can this classification be applied accurately?
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , |
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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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 |
status_str |
publishedVersion |
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 |
_version_ |
1752126316485804032 |