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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/128085
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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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1842269673761013760 |
score |
13.13397 |