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

الملخص EN

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 Ca2+ enhanced the stability of enzyme and its activity by 30%.

The Km was 1.30 in absence of Ca2+ and 1.16 mg 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.