The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II

Autores
Sequeiros, Cynthia; Torres, María José; Nievas, Marina Lucrecia; Caffini, Néstor Oscar; Natalucci, Claudia Luisa; López, Laura María Isabel; Trejo, Sebastián Alejandro
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The latex from the patagonic plant Philibertia gilliesii Hook. et Arn. (Apocynaceae) is a milky-white suspension containing a proteolytic system constituted by several cysteine endopeptidases. A proteolytic preparation (philibertain g) from the latex of P. gilliesii fruits was obtained and characterized to evaluate its potential use in bioprocesses. Philibertain g contained 1.2 g/L protein and a specific (caseinolytic) activity of 7.0 Ucas/mg protein. It reached 80 % of its maximum caseinolytic activity in the pH 7–10 range, retained 80 % of the original activity after 2 h of incubation at temperatures ranging from 25 to 45 °C and could be fully inactivated after 5 min at 75 °C. Philibertain g retained 60 % of the initial activity even at 1 M NaCl and was able to hydrolyze proteins from stickwater one, of the main waste effluents generated during fishmeal production. Furthermore, as a contribution to the knowledge of the proteolytic system of P. gilliesii, we are reporting the purification of a new peptidase, named philibertain g II (pI 9.4, molecular mass 23,977 Da, N-terminus LPESVDWREKGVVFPXRNQ) isolated from philibertain g through a purification scheme including acetone fractionation, cation exchange, molecular exclusion chromatography, and ultrafiltration.
Centro de Investigación de Proteínas Vegetales
Materia
Ciencias Exactas
Biología
Apocynaceae
Chromatography
Cysteine peptidase
Fish protein hydrolysates
Stickwater
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/146292
Acceder
id SEDICI_200baa50db4f4d1e83ad1b73b18485ce
oai_identifier_str oai:sedici.unlp.edu.ar:10915/146292
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g IISequeiros, CynthiaTorres, María JoséNievas, Marina LucreciaCaffini, Néstor OscarNatalucci, Claudia LuisaLópez, Laura María IsabelTrejo, Sebastián AlejandroCiencias ExactasBiologíaApocynaceaeChromatographyCysteine peptidaseFish protein hydrolysatesStickwaterThe latex from the patagonic plant <i>Philibertia gilliesii</i> Hook. et Arn. (Apocynaceae) is a milky-white suspension containing a proteolytic system constituted by several cysteine endopeptidases. A proteolytic preparation (philibertain g) from the latex of <i>P. gilliesii</i> fruits was obtained and characterized to evaluate its potential use in bioprocesses. Philibertain g contained 1.2 g/L protein and a specific (caseinolytic) activity of 7.0 Ucas/mg protein. It reached 80 % of its maximum caseinolytic activity in the pH 7–10 range, retained 80 % of the original activity after 2 h of incubation at temperatures ranging from 25 to 45 °C and could be fully inactivated after 5 min at 75 °C. Philibertain g retained 60 % of the initial activity even at 1 M NaCl and was able to hydrolyze proteins from stickwater one, of the main waste effluents generated during fishmeal production. Furthermore, as a contribution to the knowledge of the proteolytic system of <i>P. gilliesii</i>, we are reporting the purification of a new peptidase, named philibertain g II (pI 9.4, molecular mass 23,977 Da, N-terminus LPESVDWREKGVVFPXRNQ) isolated from philibertain g through a purification scheme including acetone fractionation, cation exchange, molecular exclusion chromatography, and ultrafiltration.Centro de Investigación de Proteínas Vegetales2016-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf332-346http://sedici.unlp.edu.ar/handle/10915/146292enginfo:eu-repo/semantics/altIdentifier/issn/1559-0291info:eu-repo/semantics/altIdentifier/issn/0273-2289info:eu-repo/semantics/altIdentifier/doi/10.1007/s12010-016-1997-8info:eu-repo/semantics/altIdentifier/pmid/26852027info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T11:04:39Zoai:sedici.unlp.edu.ar:10915/146292Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:04:39.42SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II
title The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II
spellingShingle The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II
Sequeiros, Cynthia
Ciencias Exactas
Biología
Apocynaceae
Chromatography
Cysteine peptidase
Fish protein hydrolysates
Stickwater
title_short The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II
title_full The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II
title_fullStr The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II
title_full_unstemmed The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II
title_sort The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II
dc.creator.none.fl_str_mv Sequeiros, Cynthia
Torres, María José
Nievas, Marina Lucrecia
Caffini, Néstor Oscar
Natalucci, Claudia Luisa
López, Laura María Isabel
Trejo, Sebastián Alejandro
author Sequeiros, Cynthia
author_facet Sequeiros, Cynthia
Torres, María José
Nievas, Marina Lucrecia
Caffini, Néstor Oscar
Natalucci, Claudia Luisa
López, Laura María Isabel
Trejo, Sebastián Alejandro
author_role author
author2 Torres, María José
Nievas, Marina Lucrecia
Caffini, Néstor Oscar
Natalucci, Claudia Luisa
López, Laura María Isabel
Trejo, Sebastián Alejandro
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Biología
Apocynaceae
Chromatography
Cysteine peptidase
Fish protein hydrolysates
Stickwater
topic Ciencias Exactas
Biología
Apocynaceae
Chromatography
Cysteine peptidase
Fish protein hydrolysates
Stickwater
dc.description.none.fl_txt_mv The latex from the patagonic plant <i>Philibertia gilliesii</i> Hook. et Arn. (Apocynaceae) is a milky-white suspension containing a proteolytic system constituted by several cysteine endopeptidases. A proteolytic preparation (philibertain g) from the latex of <i>P. gilliesii</i> fruits was obtained and characterized to evaluate its potential use in bioprocesses. Philibertain g contained 1.2 g/L protein and a specific (caseinolytic) activity of 7.0 Ucas/mg protein. It reached 80 % of its maximum caseinolytic activity in the pH 7–10 range, retained 80 % of the original activity after 2 h of incubation at temperatures ranging from 25 to 45 °C and could be fully inactivated after 5 min at 75 °C. Philibertain g retained 60 % of the initial activity even at 1 M NaCl and was able to hydrolyze proteins from stickwater one, of the main waste effluents generated during fishmeal production. Furthermore, as a contribution to the knowledge of the proteolytic system of <i>P. gilliesii</i>, we are reporting the purification of a new peptidase, named philibertain g II (pI 9.4, molecular mass 23,977 Da, N-terminus LPESVDWREKGVVFPXRNQ) isolated from philibertain g through a purification scheme including acetone fractionation, cation exchange, molecular exclusion chromatography, and ultrafiltration.
Centro de Investigación de Proteínas Vegetales
description The latex from the patagonic plant <i>Philibertia gilliesii</i> Hook. et Arn. (Apocynaceae) is a milky-white suspension containing a proteolytic system constituted by several cysteine endopeptidases. A proteolytic preparation (philibertain g) from the latex of <i>P. gilliesii</i> fruits was obtained and characterized to evaluate its potential use in bioprocesses. Philibertain g contained 1.2 g/L protein and a specific (caseinolytic) activity of 7.0 Ucas/mg protein. It reached 80 % of its maximum caseinolytic activity in the pH 7–10 range, retained 80 % of the original activity after 2 h of incubation at temperatures ranging from 25 to 45 °C and could be fully inactivated after 5 min at 75 °C. Philibertain g retained 60 % of the initial activity even at 1 M NaCl and was able to hydrolyze proteins from stickwater one, of the main waste effluents generated during fishmeal production. Furthermore, as a contribution to the knowledge of the proteolytic system of <i>P. gilliesii</i>, we are reporting the purification of a new peptidase, named philibertain g II (pI 9.4, molecular mass 23,977 Da, N-terminus LPESVDWREKGVVFPXRNQ) isolated from philibertain g through a purification scheme including acetone fractionation, cation exchange, molecular exclusion chromatography, and ultrafiltration.
publishDate 2016
dc.date.none.fl_str_mv 2016-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/146292
url http://sedici.unlp.edu.ar/handle/10915/146292
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1559-0291
info:eu-repo/semantics/altIdentifier/issn/0273-2289
info:eu-repo/semantics/altIdentifier/doi/10.1007/s12010-016-1997-8
info:eu-repo/semantics/altIdentifier/pmid/26852027
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
332-346
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.13397

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