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

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...

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Detalles Bibliográficos
Autores principales: Sequeiros, Cynthia, Torres, María José, Nievas, Marina Lucrecia, Caffini, Néstor Oscar, Natalucci, Claudia Luisa, López, Laura María Isabel, Trejo, Sebastián Alejandro
Formato: Articulo
Lenguaje:Inglés
Publicado: 2016
Materias:
Ciencias Exactas
Biología
Apocynaceae
Chromatography
Cysteine peptidase
Fish protein hydrolysates
Stickwater
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/146292
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-146292
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Biología
Apocynaceae
Chromatography
Cysteine peptidase
Fish protein hydrolysates
Stickwater
spellingShingle Ciencias Exactas
Biología
Apocynaceae
Chromatography
Cysteine peptidase
Fish protein hydrolysates
Stickwater
Sequeiros, Cynthia
Torres, María José
Nievas, Marina Lucrecia
Caffini, Néstor Oscar
Natalucci, Claudia Luisa
López, Laura María Isabel
Trejo, Sebastián Alejandro
The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II
topic_facet Ciencias Exactas
Biología
Apocynaceae
Chromatography
Cysteine peptidase
Fish protein hydrolysates
Stickwater
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.
format Articulo
Articulo
author Sequeiros, Cynthia
Torres, María José
Nievas, Marina Lucrecia
Caffini, Néstor Oscar
Natalucci, Claudia Luisa
López, Laura María Isabel
Trejo, Sebastián Alejandro
author_facet Sequeiros, Cynthia
Torres, María José
Nievas, Marina Lucrecia
Caffini, Néstor Oscar
Natalucci, Claudia Luisa
López, Laura María Isabel
Trejo, Sebastián Alejandro
author_sort Sequeiros, Cynthia
title The Proteolytic Activity of <i>Philibertia gilliesii</i> Latex : Purification of Philibertain g II
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 proteolytic activity of <i>philibertia gilliesii</i> latex : purification of philibertain g ii
publishDate 2016
url http://sedici.unlp.edu.ar/handle/10915/146292
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