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Purification and partial characterization of exopolygalacturonase I fromPenicillium frequentans

Authors
Journal
Microbiological Research
0944-5013
Publisher
Elsevier
Publication Date
Volume
157
Issue
1
Identifiers
DOI: 10.1078/0944-5013-00127
Keywords
  • Brazilian Soil
  • Exopolygalacturonase
  • Pectic Enzyme
  • Penicillium Frequentans
  • Polygalacturonase
Disciplines
  • Biology

Abstract

Summary 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). K m and V max 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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