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Published on: May 28, 2012
Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation
Eleni Gomes1, Rodrigo Simões Ribeiro Leite, Roberto da Silva
1Laboratory of Biochemistry and Applied Microbiology, Ibilce, Universidade Estadual Paulista (Unesp), Rua Cristovao Colombo, 2265, Jd. Nazareth, São José do Rio Preto, SP, CEP 15054-000, Brazil.
Abstract:
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 degrees 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 mumol min(-1)mg(-1).
