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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  μ mol min −1 mg −1 .

Purification of an Exopolygalacturonase fromPenicillium viridicatum RFC3Produced in Submerged Fermentation