Enhanced production of polygalacturonase in solid-state fermentation: selection of the process conditions, isolation and partial characterization of the enzyme

• Authors: Halina Zaslona , Anna Trusek-Holownia
• Languages of publication: EN

Abstracts

EN

Polygalacturonase (PG) production by Penicillium chrysogenum during solid-state fermentation was accompanied by decomposition of orange peels. A leaching procedure was developed through the selection of solvent, time and intensity of stirring. A maximum PG activity was observed after 48 h peel inoculation. Further cultivation decreased the enzyme activity significantly, up to 60% of the maximum PG activity. During fermentation, a rapid acidification of the solid medium which inhibited the pectinolytic enzyme, was observed. Buffering agents with different pH values and different ionic strengths were examined to identify the most suitable medium to avoid this problem. Buffer addition counteracted acidification and enhanced active protein production, which was observed for all of the applied pH values (6.5-8.0) of the buffering agent. The most satisfactory results were obtained when using the highest pH at 8.0. The protein content and PG activity increased from 3.5 mg/g and 1.09 U/g to 7.7 mg/g and 7.11 U/g during cultivation, with uncontrolled and pH-controlled medium, respectively. Measurements at wide pH and temperature ranges indicated an optimum for PG activity at pH 5.0 and 43°C; however, high thermal stability corresponded to lower temperatures, and a temperature of 37°C is thus recommended. Under these conditions, the operational stability was determined to be t1/2=570 h.

Keywords

EN

polygalacturonase; solid-state fermentation; constant pH maintaining; moisture content; phosphorus source; Penicillium chrysogenum

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2015
• Volume: 62
• Issue: 4
• Pages: 651-657

Dates

published

2015

received

2015-06-11

revised

2015-08-27

accepted

2015-10-14

(unknown)

2015-10-26

Contributors

author

Halina Zaslona

• Group of Bioprocess and Biomedical Engineering, Department of Chemistry, Wroclaw University of Technology, Wrocław, Poland

author

Anna Trusek-Holownia

• Group of Bioprocess and Biomedical Engineering, Department of Chemistry, Wroclaw University of Technology, Wrocław, Poland

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Identifiers

DOI

10.18388/abp.2015_1081