Purification of an Exopolygalacturonase from Penicillium viridicatum RFC3 Produced in Submerged Fermentation
2009
Gomes, Eleni(Laboratory of Biochemistry and Applied Microbiology, Ibilce) | Leite, Rodrigo Simões Ribeiro(Laboratory of Biochemistry and Applied Microbiology, Ibilce) | da Silva, Roberto(Laboratory of Biochemistry and Applied Microbiology, Ibilce) | Silva, Dênis(Laboratory of Biochemistry and Applied Microbiology, Ibilce)
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.
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