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Pectinases accelerate the breakdown of the glycosidic bonds in pectin into simpler forms. Pectinases in the study were produced using three extraction solvents, three fungi, and six substrates. Citrate buffer, distilled water and 0.1 M NaCl were utilized as extraction solvents. Penicillium sp, Pichia kudriavzevii F2-T429-5 and Aspergillus niger were selectively isolated from the environment and identified. The substrates include; wheat bran, banana peels, orange peels, corn cobs, Thaumatococcus daniellii (sweet prayer plant) fruit peels, and leaves in solid-state fermentation. The dinitro salicylic acid (DNS) technique was used to determine pectinase activity. In comparison to distilled water, the study found that extracting the enzyme from the fermentation medium with 0.1 M NaCl solvent resulted in considerable (p<0.05) activity. The best substrate and fungus were orange peels and Aspergillus niger, respectively. In general, when compared to the yeast Pichia kudriavzevii F2-T429-5, the molds (Penicillium sp. and Aspergillus niger) produced pectinases with higher activity. Orange peel resulted in pectinase production with significant (p<0.05) activity compared to wheat bran, banana peels, corn cobs, Thaumatococcus daniellii (sweet prayer plant) fruit peels, and leaves. Additionally, Pichia kudriavzevii F2-T429-5 in Thaumatococcus daniellii fruit peel fermentation produced pectinase with the lowest activity. The inference drawn from the study shows the potential of T. daniellii fruit peels, its leaves, and Pichia kudriavzevii F2-T429-5 for pectinase production.

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