Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products

Autores
Lamas, Daniela Lorena; Yeannes, Maria Isabel; Massa, Agueda Elena
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Proteolytic enzymes have been detected and partially purified from Merluccius hubbsiviscera. Crude proteinase extract exhibited its maximal activity at pH 7.94, 59.52ºC and33.93 minutes using azocaseín as a substrate. The molecular weight was estimated to be 25kDa by SDS-PAGE. The best ratio of crude extract to cold acetone for the partial purificationof protease was found in 1:1.25 with a 94.02% of recovery.Results relative to the substrate specific BAPNA, indicated that the recovered protease was atrypsin. The kinetic trypsin constant Km and kcat were 0.38 mM and 0.97/s respectively,while the catalytic efficiency was 2.54/mMs. The stability results obtained with surfactantssuggest that this enzyme can be incorporated as an ingredient in detergent formulations.
Fil: Lamas, Daniela Lorena. Instituto Nacional de Investigaciones y Desarrollo Pesquero; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Yeannes, Maria Isabel. Universidad Nacional de Mar del Plata. Facultad de Ingeniería; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina
Fil: Massa, Agueda Elena. Instituto Nacional de Investigaciones y Desarrollo Pesquero; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina
Materia
PURIFICATION
ALKALINE PROTEASE
MERLUCCIUS HUBBSI
TRYPSIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/128085

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network_name_str CONICET Digital (CONICET)
spelling Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-productsLamas, Daniela LorenaYeannes, Maria IsabelMassa, Agueda ElenaPURIFICATIONALKALINE PROTEASEMERLUCCIUS HUBBSITRYPSINhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Proteolytic enzymes have been detected and partially purified from Merluccius hubbsiviscera. Crude proteinase extract exhibited its maximal activity at pH 7.94, 59.52ºC and33.93 minutes using azocaseín as a substrate. The molecular weight was estimated to be 25kDa by SDS-PAGE. The best ratio of crude extract to cold acetone for the partial purificationof protease was found in 1:1.25 with a 94.02% of recovery.Results relative to the substrate specific BAPNA, indicated that the recovered protease was atrypsin. The kinetic trypsin constant Km and kcat were 0.38 mM and 0.97/s respectively,while the catalytic efficiency was 2.54/mMs. The stability results obtained with surfactantssuggest that this enzyme can be incorporated as an ingredient in detergent formulations.Fil: Lamas, Daniela Lorena. Instituto Nacional de Investigaciones y Desarrollo Pesquero; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Yeannes, Maria Isabel. Universidad Nacional de Mar del Plata. Facultad de Ingeniería; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; ArgentinaFil: Massa, Agueda Elena. Instituto Nacional de Investigaciones y Desarrollo Pesquero; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; ArgentinaWolters Kluwer2015-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/128085Lamas, Daniela Lorena; Yeannes, Maria Isabel; Massa, Agueda Elena; Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products; Wolters Kluwer; International Journal of Food and Nutritional Sciences; 4; 5; 12-2015; 121-1302320-7876CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.ijfans.org/article.asp?issn=2319-1775;year=2015;volume=4;issue=5;spage=121;epage=130;aulast=Lamas;type=0info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:01:03Zoai:ri.conicet.gov.ar:11336/128085instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:01:04.061CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products
title Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products
spellingShingle Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products
Lamas, Daniela Lorena
PURIFICATION
ALKALINE PROTEASE
MERLUCCIUS HUBBSI
TRYPSIN
title_short Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products
title_full Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products
title_fullStr Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products
title_full_unstemmed Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products
title_sort Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products
dc.creator.none.fl_str_mv Lamas, Daniela Lorena
Yeannes, Maria Isabel
Massa, Agueda Elena
author Lamas, Daniela Lorena
author_facet Lamas, Daniela Lorena
Yeannes, Maria Isabel
Massa, Agueda Elena
author_role author
author2 Yeannes, Maria Isabel
Massa, Agueda Elena
author2_role author
author
dc.subject.none.fl_str_mv PURIFICATION
ALKALINE PROTEASE
MERLUCCIUS HUBBSI
TRYPSIN
topic PURIFICATION
ALKALINE PROTEASE
MERLUCCIUS HUBBSI
TRYPSIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Proteolytic enzymes have been detected and partially purified from Merluccius hubbsiviscera. Crude proteinase extract exhibited its maximal activity at pH 7.94, 59.52ºC and33.93 minutes using azocaseín as a substrate. The molecular weight was estimated to be 25kDa by SDS-PAGE. The best ratio of crude extract to cold acetone for the partial purificationof protease was found in 1:1.25 with a 94.02% of recovery.Results relative to the substrate specific BAPNA, indicated that the recovered protease was atrypsin. The kinetic trypsin constant Km and kcat were 0.38 mM and 0.97/s respectively,while the catalytic efficiency was 2.54/mMs. The stability results obtained with surfactantssuggest that this enzyme can be incorporated as an ingredient in detergent formulations.
Fil: Lamas, Daniela Lorena. Instituto Nacional de Investigaciones y Desarrollo Pesquero; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Yeannes, Maria Isabel. Universidad Nacional de Mar del Plata. Facultad de Ingeniería; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina
Fil: Massa, Agueda Elena. Instituto Nacional de Investigaciones y Desarrollo Pesquero; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina
description Proteolytic enzymes have been detected and partially purified from Merluccius hubbsiviscera. Crude proteinase extract exhibited its maximal activity at pH 7.94, 59.52ºC and33.93 minutes using azocaseín as a substrate. The molecular weight was estimated to be 25kDa by SDS-PAGE. The best ratio of crude extract to cold acetone for the partial purificationof protease was found in 1:1.25 with a 94.02% of recovery.Results relative to the substrate specific BAPNA, indicated that the recovered protease was atrypsin. The kinetic trypsin constant Km and kcat were 0.38 mM and 0.97/s respectively,while the catalytic efficiency was 2.54/mMs. The stability results obtained with surfactantssuggest that this enzyme can be incorporated as an ingredient in detergent formulations.
publishDate 2015
dc.date.none.fl_str_mv 2015-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/128085
Lamas, Daniela Lorena; Yeannes, Maria Isabel; Massa, Agueda Elena; Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products; Wolters Kluwer; International Journal of Food and Nutritional Sciences; 4; 5; 12-2015; 121-130
2320-7876
CONICET Digital
CONICET
url http://hdl.handle.net/11336/128085
identifier_str_mv Lamas, Daniela Lorena; Yeannes, Maria Isabel; Massa, Agueda Elena; Partial purification of proteolytic enzymes and characterization of trypsin from merluccius hubbsi by-products; Wolters Kluwer; International Journal of Food and Nutritional Sciences; 4; 5; 12-2015; 121-130
2320-7876
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.ijfans.org/article.asp?issn=2319-1775;year=2015;volume=4;issue=5;spage=121;epage=130;aulast=Lamas;type=0
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wolters Kluwer
publisher.none.fl_str_mv Wolters Kluwer
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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