Selective adsorption of plant cysteine peptidases onto TiO<SUB>2</SUB>

A crude extract rich in plant cysteine peptidases was obtained from the latex of the fruits of Araujia hortorum, a South American climbing plant. The highly concentrated extractwas immobilized onto titanium dioxide to produce biocatalysts through a simple adsorption procedure. Absorbance measurement...

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Detalles Bibliográficos
Autores principales: Llerena Suster, Carlos Rafael, Foresti, M. Laura, Briand, Laura Estefanía, Morcelle del Valle, Susana Raquel
Formato: Articulo
Lenguaje:Inglés
Publicado: 2009
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/109600
Aporte de:
id I19-R120-10915-109600
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Plant cysteine peptidases
Selective adsorption
Titanium dioxide
Amidasic activity
spellingShingle Biología
Plant cysteine peptidases
Selective adsorption
Titanium dioxide
Amidasic activity
Llerena Suster, Carlos Rafael
Foresti, M. Laura
Briand, Laura Estefanía
Morcelle del Valle, Susana Raquel
Selective adsorption of plant cysteine peptidases onto TiO<SUB>2</SUB>
topic_facet Biología
Plant cysteine peptidases
Selective adsorption
Titanium dioxide
Amidasic activity
description A crude extract rich in plant cysteine peptidases was obtained from the latex of the fruits of Araujia hortorum, a South American climbing plant. The highly concentrated extractwas immobilized onto titanium dioxide to produce biocatalysts through a simple adsorption procedure. Absorbance measurement at 280nm and Bradford’s method for protein quantification revealed that the protein content of the crude extract was selectively adsorbed onto the titanium dioxide surface at a very high rate. In 5 min of contact with the support all protein present in the crude extract was selectively withdrawn from the solution, leading to an immobilized biocatalyst with a high protein concentration. Caseinolytic assays indicated that, except for the catalyst obtained with the highest crude amount contacted with the support, all the proteolytic activity present in the crude extract was adsorbed onto TiO2. The amidasic activity of the immobilized catalysts (Ah/TiO2) was tested in the hydrolysis of a synthetic chromogenic substrate (PFLNA) showing partial deactivation with respect to the native enzyme. In amidasic activity assays the ionic strength of the buffermedium showed to be a key feature to consider in order to avoid protease desorption from the support, indicating the importance of electrostatic interactions between the enzymes and TiO2. Reuse of the produced biocatalysts with PFLNA as substrate revealed that after five successive uses Ah/TiO2 retained more than 20% of its initial activity.
format Articulo
Articulo
author Llerena Suster, Carlos Rafael
Foresti, M. Laura
Briand, Laura Estefanía
Morcelle del Valle, Susana Raquel
author_facet Llerena Suster, Carlos Rafael
Foresti, M. Laura
Briand, Laura Estefanía
Morcelle del Valle, Susana Raquel
author_sort Llerena Suster, Carlos Rafael
title Selective adsorption of plant cysteine peptidases onto TiO<SUB>2</SUB>
title_short Selective adsorption of plant cysteine peptidases onto TiO<SUB>2</SUB>
title_full Selective adsorption of plant cysteine peptidases onto TiO<SUB>2</SUB>
title_fullStr Selective adsorption of plant cysteine peptidases onto TiO<SUB>2</SUB>
title_full_unstemmed Selective adsorption of plant cysteine peptidases onto TiO<SUB>2</SUB>
title_sort selective adsorption of plant cysteine peptidases onto tio<sub>2</sub>
publishDate 2009
url http://sedici.unlp.edu.ar/handle/10915/109600
work_keys_str_mv AT llerenasustercarlosrafael selectiveadsorptionofplantcysteinepeptidasesontotiosub2sub
AT forestimlaura selectiveadsorptionofplantcysteinepeptidasesontotiosub2sub
AT briandlauraestefania selectiveadsorptionofplantcysteinepeptidasesontotiosub2sub
AT morcelledelvallesusanaraquel selectiveadsorptionofplantcysteinepeptidasesontotiosub2sub
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