Comparison of Optimal Fungal Pectinase Activities Using the Box-Behnken Design doi.org/10.26538/tjnpr/v5i9.21

Abstract

Pectinases catalyze pectin via hydrolysis and de-esterification to simpler forms. Pectinase produced by the fermentation process can be enhanced through optimization. The Design-Expert Software (package) file version 13.0.3 was used to predict the optimal activity of the enzyme with Citrus sinensis (orange) peels, Triticum aestivum (wheat) bran, and Thaumatococcus danielli (Miraculous berry) fruit peels as substrates, while Aspergillus niger, Penicillium sp. and Pichia kudriavzevii strain F2-T429-5 as microbes for the solid-state fermentation process. The microorganisms were selected based on their zones of hydrolysis of pectin. The Box-Behnken design was used to generate the experiment runs and analyses of the data obtained from the solid-state fermentation process. The following conditions for optimal pectinase activity were considered; fermentation duration, pH, temperature, particle size, inoculum volume, and agitation during enzyme extraction. Aspergillus niger in Citrus sinensis peel fermentation resulted in the best enzyme activity of 5.02 U/mL in approximately 6 days of fermentation, pH 4, at 21oC, 0.06-inch substrate size, 1 mL inoculum, and agitation duration during pectinase extraction in approximately 11 min. Pectinase activity with T. danielli fruit wastes showed 59.36% decrease relative to C. sinensis peel. A. niger and Penicillium sp. produced a more active enzyme (74.02% and 71.81% respectively) than the newly investigated yeast P. kudriavzevii (F2-T429-5) in T. danielli fruit wastes fermentation, a vital contribution to mycology. Nevertheless, Thaumatococcus danielli and P. kudriavzevii (F2-T429-5) employed in the study have good prospects for pectinase production.