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...
| Autores: | , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2017 |
| País: | Argentina |
| Institución: | Universidad Nacional de La Plata |
| Repositorio: | SEDICI (UNLP) |
| Idioma: | inglés |
| OAI Identifier: | oai:sedici.unlp.edu.ar:10915/77307 |
| Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/77307 |
| Access Level: | acceso abierto |
| Palabra clave: | Química Pectinas protopectin protopectinase-SE Langmuir isotherm Michaelis-Menten |
| Sumario: | 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. |
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