Effect of physicochemical parameters on the polygalacturonase of an Aspergillus sojae mutant using wheat bran, an...

Polygalacturonases (PGs) are valuable enzymes of the food industry; therefore it is of great importance to discover new and GRAS PG-producing microbial strains. In this study, PG enzyme produced from a high PG activity producer mutant Aspergillus sojae using wheat bran at the flask scale under pre-optimized conditions of solid-state fermentation (SSF) was biochemically characterized.

The crude PG enzyme showed optimum activity in the pH range 4.0-5.0 and was stable in the pH range 3.0-7.0. The optimum temperature for the PG was 40 °C and it retained 99% of its activity at 50 °C. The mutant A. sojae PG could preserve more than 50% of its stability between 25 and 50 °C, both for 30 and 60 min, and was found to be stable in the presence of most of the tested compounds and metal ions. The inactivation energy (Ed ) was determined as 125.3 kJ mol(-1) . The enthalpy (ΔH*), free energy (ΔG*) and entropy (ΔS*) of inactivation were found to be stable with increasing temperature.

The mutant A. sojae PG could be suitable for the clarification (depectinization) of orange and grape juices and wine. © 2015 Society of Chemical Industry.