PMID: 11911610Mar 26, 2002Paper

Purification and partial characterization of exopolygalacturonase I from Penicillium frequentans

Microbiological Research
Maria Angélica dos Santos Cunha ChellegattiS Said

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 degrees C, respectively, was purified from a culture fluid of Penicillium frequentans. The enzyme was characterized as an exo-alpha-1,4-polygalacturonase (exo-PG I). Km and Vmax for sodium polypectate hydrolysis were 0.68 g/l and 596.8 U x 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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Citations

Jan 29, 2013·Applied Biochemistry and Biotechnology·Janaina Aparecida TeixeiraElza Fernandes de Araújo
Apr 1, 2014·Preparative Biochemistry & Biotechnology·Manasi JoshiRavindra Adivarekar
Mar 10, 2004·Biotechnology and Bioengineering·I VerlentM E Hendrickx

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