Artigo
Purification of an exopolygalacturonase from Penicillium viridicatum RFC3 produced in submerged fermentation
Fecha
2009-12-01Registro en:
International Journal of Microbiology.
1687-918X
1687-9198
10.1155/2009/631942
2-s2.0-80052506411
2-s2.0-80052506411.pdf
7091241742851920
9424175688206545
Autor
Universidade Estadual Paulista (Unesp)
Resumen
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 1.16mg mL -1 in presence of this ion. In relation to the Vmax the presence of this ion increased from 1.76 to 2.07 μmol min -1mg -1. Copyright © 2009 Eleni Gomes et al.