The characterization of a pectin-degrading enzyme from Aspergillus oryzae grown on passion fruit peel as the carbon source and the evaluation of its potential for industrial applications

An extracellular pectinase (PEC-I) was isolated from the crude extract of Aspergillus oryzae when grown on passion fruit peel (PFP) as the carbon source and partially purified by ultra filtration, gel filtration and ion-exchange chromatography procedures. Pectinase activity was predominantly found in the retentate. The pectinase from retentate (PEC-Ret) was most active at 50 degrees C and pH 7.0 and stable at 50 degrees C with a half-life of approximately 8h. PEC-I showed higher activity at pH 4.5 and 55 degrees C, 70 degrees C and 75 degrees C and was inhibited by cations (Ag+, Fe2+, Fe3+, Co2+, Ca2+ and Hg2+), EDTA, tannic acid and vanillin. On the other hand, PEC-I was activated by Cu2+, ferulic acid, cinnamic acid and 4-hydroxybenzoic acid. The gel under denaturing conditions of PEC-Ret and PEC-I samples showed a protein band of approximate to 45kDa coincident with that found by staining for pectinase activity. In the bioscouring of cotton fabric the PEC-Ret pectinase preparation led to a better wettability and removed more pectin from the cotton fibers than the commercial enzyme preparation Viscozyme L, but was less effective than a commercial alkaline pectate lyase preparation and alkaline scouring. The incubation of PEC-Ret with guava juice resulted in a 4.15% decrease in juice viscosity.