Produção Nacional
Revisado por pares
Purification and Biochemical Characterization of an Extracellular Endopolygalacturonase from Penicillium frequentans
1996; American Chemical Society; Volume: 44; Issue: 6 Linguagem: Inglês
10.1021/jf9506491
ISSN1520-5118
AutoresMaria de Fátima Borin, Suraia Said, Maria José Vieira Fonseca,
Tópico(s)Biofuel production and bioconversion
ResumoAn extracellular endopolygalacturonase from extracts of liquid cultures of Penicillium frequentans was purified by ion exchange chromatography to homogeneity as judged by electrophoresis and isoelectric focusing. The enzyme is a single subunit glycoprotein with an Mr value of 20 kDa by gel filtration and a pI value of 5.6 by electrofocusing. It is active against pectin and sodium polygalacturonate. Comparison of the rate of enzyme-catalyzed increase in fluidity of solutions of substrate vs the rate of release of reducing sugars indicated that the polygalacturonase is endo-acting. The Km for polygalacturonase is 2.7 g/L, and the Vmax is 488.28 U of reducing sugar·mg-1. The optimum temperature and pH values under the assay conditions used were 50 °C and pH 4.0−4.7, respectively. Keywords: Endopolygalacturonase; Penicillium frequentans
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