Purification and partial characterization of exopolygalacturonase I from Penicillium frequentans |
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Authors: | Maria Anglica dos Santos Cunha Chellegatti Maria Jos Vieira Fonseca Suraia Said |
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Institution: | aDepartamento de Ciências Farmacêuticas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo. Avenida do Café s/n, Monte Alegre, CEP 14040.903, Ribeirão Preto, São Paulo, Brazil |
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Abstract: | A polygalacturonase with a molecular mass of 74 kDa, an isoelectric point around pH 4.2 and pH – and temperature optima of 3.9 and 50°C, respectively, was purified from a culture fluid of Penicillium frequentans. The enzyme was characterized as an exo-α-1,4-polygalacturonase (exo-PG I). Km and Vmax for sodium polypectate hydrolysis were 0.68 g/l and 596.8 U × mg−1, respectively. The enzyme, a glycoprotein with a carbohydrate content of 81%, is probably the main pectinase of Penicillium frequentans responsible for cleaving monomer units from the non-reducing end of pectin. |
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Keywords: | Brazilian soil exopolygalacturonase pectic enzyme Penicillium frequentans polygalacturonase |
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