Characterization of polygalacturonase produced by solid-state fermentation using the residue of passion fruit as substrate

Rosane L. A. de Souza Líbia de S. C. Oliveira Flávio L. H. da Silva Beatriz C. Amorim About the authors

Pectinolytic enzymes, or pectinases, are a heterogeneous group of enzymes that hydrolyze the pectic substances present in plant cells. These enzymes are applied in several areas, making it important to know their characteristics for an efficient application. This work aimed to characterize the dry residue of passion fruit (Passiflora edulis) and subsequent characterization of the enzyme polygalacturonase produced by solid state fermentation and leavening agent and the filamentous fungus Aspergillus niger. The residue of passion fruit presented a pectin content of 13.10%, having a potential as a substrate for the production of pectinases. The activity of polygalacturonase reached a maximum value after 66 h of process with 40% initial moisture content and 1% of nitrogen supplementation. In this condition an activity of 20.9 U g-1 was obtained. The polygalacturonase produced the crude enzymatic extract presenting good thermal stability up to temperatures of 50 °C. This enzyme remained stable in the pH range between 3.5 and 5.5 and was not detected for pH values above 6.5.

Passiflora edulis; pectinases; Aspergillus niger; pectin


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