Purification of an Exopolygalacturonase fromPenicillium viridicatum RFC3Produced in Submerged Fermentation

Abstract

An exo-PG obtained fromPenicillium viridicatumin 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.). IonsCa2+enhanced the stability of enzyme and its activity by 30%. TheKmwas 1.30 in absence ofCa2+and 1.16 mgmL−1in presence of this ion. In relation to theVmaxthe presence of this ion increased from 1.76 to 2.07 μmolmin−1mg−1.