Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation.
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).
Gomes
Eleni
E
Laboratory 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.
Leite
Rodrigo Simões Ribeiro
RS
da Silva
Roberto
R
Silva
Dênis
D