Protopectinase-se from <i>Geotrichum klebahnii</i>: Studies of the adsorption and pectin-solubilization capacity

Protopectinase SE (PPase-SE) is a polygalacturonase produced by Geotrichum klebahnii with the capacity to liberate pectin through protopectin hydrolysis. The protopectin cleavage is a typical heterogeneous-catalysis reaction whose interaction between the enzyme and the protopectin substrate from lem...

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Detalles Bibliográficos
Autores principales: Zapata Zapata, Arley David, Hours, Roque Alberto, Cavalitto, Sebastián Fernando
Formato: Articulo
Lenguaje:Inglés
Publicado: 2017
Materias:
Química
Pectinas
protopectin
protopectinase-SE
Langmuir isotherm
Michaelis-Menten
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/77307
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-77307
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
Pectinas
protopectin
protopectinase-SE
Langmuir isotherm
Michaelis-Menten
spellingShingle Química
Pectinas
protopectin
protopectinase-SE
Langmuir isotherm
Michaelis-Menten
Zapata Zapata, Arley David
Hours, Roque Alberto
Cavalitto, Sebastián Fernando
Protopectinase-se from <i>Geotrichum klebahnii</i>: Studies of the adsorption and pectin-solubilization capacity
topic_facet Química
Pectinas
protopectin
protopectinase-SE
Langmuir isotherm
Michaelis-Menten
description Protopectinase SE (PPase-SE) is a polygalacturonase produced by Geotrichum klebahnii with the capacity to liberate pectin through protopectin hydrolysis. The protopectin cleavage is a typical heterogeneous-catalysis reaction whose interaction between the enzyme and the protopectin substrate from lemon albedo along with the release of the pectin-reaction product were the objectives of this investigation. The interaction between PPase-SE and protopectin depended on the particle size and the structure of the substrate as well as on the nature of the buffer. The adsorption kinetics follows, for small particles, a Langmuir isotherm pattern. The reaction exhibited Michaelis-Menten kinetics, giving respective apparent-Km and Vmax values of 30.2 g/l and 57.3 g/l.h. The better results in enzyme adsorption and pectin releasing were obtained with citrate and citrate-phosphate buffers. This report constitutes the first investigation in pectin solubilization involving a model for the substrate-binding mechanism within the pectinase-protopectinase system.
format Articulo
Articulo
author Zapata Zapata, Arley David
Hours, Roque Alberto
Cavalitto, Sebastián Fernando
author_facet Zapata Zapata, Arley David
Hours, Roque Alberto
Cavalitto, Sebastián Fernando
author_sort Zapata Zapata, Arley David
title Protopectinase-se from <i>Geotrichum klebahnii</i>: Studies of the adsorption and pectin-solubilization capacity
title_short Protopectinase-se from <i>Geotrichum klebahnii</i>: Studies of the adsorption and pectin-solubilization capacity
title_full Protopectinase-se from <i>Geotrichum klebahnii</i>: Studies of the adsorption and pectin-solubilization capacity
title_fullStr Protopectinase-se from <i>Geotrichum klebahnii</i>: Studies of the adsorption and pectin-solubilization capacity
title_full_unstemmed Protopectinase-se from <i>Geotrichum klebahnii</i>: Studies of the adsorption and pectin-solubilization capacity
title_sort protopectinase-se from <i>geotrichum klebahnii</i>: studies of the adsorption and pectin-solubilization capacity
publishDate 2017
url http://sedici.unlp.edu.ar/handle/10915/77307
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