Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation

An exo-PG obtained from Penicillium viridicatum in submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme was 92 kDa, optimum pH and temperature for activity were pH 5 and 50–55°C. The exo-PG showed a profile of an exo-polygalacturonase, releasing galacturoni...

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Detalles Bibliográficos
Autores principales: Gomes, Eleni, Leite, Rodrigo Simões Ribeiro, da Silva, Roberto, Silva, Dênis
Formato: Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2009
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2817892/
https://www.ncbi.nlm.nih.gov/pubmed/20148174
http://dx.doi.org/10.1155/2009/631942
Descripción
Sumario:An exo-PG obtained from Penicillium viridicatum in submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme was 92 kDa, optimum pH and temperature for activity were pH 5 and 50–55°C. The exo-PG showed a profile of an exo-polygalacturonase, releasing galacturonic acid by hydrolysis of pectin with a high degree of esterification (D.E.). Ions Ca(2+) enhanced the stability of enzyme and its activity by 30%. The K (m) was 1.30 in absence of Ca(2+) and 1.16 mg mL(−1) in presence of this ion. In relation to the V (max) the presence of this ion increased from 1.76 to 2.07 μmol min(−1)mg(−1).

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