The effects of the various carbon and nitrogen substrates on the growth and polygalacturonase activity of Trichoderma viride (BITRS-1001) isolated from the tar sand deposit in Gbelejuloda-Irele Ondo State, Nigeria were investigated in submerged cultivation at 30 °C ± 2 °C. The commercial carbon and nitrogen substrates included sucrose, fructose, starch, maltose, lactose and peptone, sodium nitrate, urea and casein respectively. All the carbon substrates used supported the growth of T. viride (0.566 to 0.156 g/50 mL of culture medium) with starch supporting the highest biomass yield and sucrose the least biomass yield. Maximum polygalacturonase activity of 3033 U/mL was recorded in maltose medium. Maximum biomass yield on the nitrogen sources was observed in the organic nitrogen namely peptone and casein with values not significantly different from each other at p ≤ 0.05. In the determination of the crude enzyme activity on the nitrogen sources, maximum polygalacturonase activity of 12,400 U/mL was recorded in peptone medium. Hence, a careful manipulation of these nutrient substrates could help to optimise the production of this enzyme on a large scale.

Aims: The research was carried out to study the purification, characterization and application of polygalacturonase from Aspergillus niger CSTRF. Methodology and Results: The polygalacturonase (PG) from the fungus was purified by ammonium sulphate precipitation and dialysed. The resulting fraction of the enzyme was further separated by molecular exclusion and ion exchange chromatography. The enzyme was purified 28.19 fold with a yield of approximately 69 % following purification with SP C-50. It has a relative molecular weight of 79,430 daltons and markedly influenced by temperature, pH and substrate concentrations of reactions with optimum activity at 35 °C, pH 4.0 and 8 mg/mL respectively. The PG was heat stable over a broad range of temperatures. Line weaver-Burk plot for the apparent hydrolysis of pectin showed approximately Km value of 2.7 mg/mL. The activity of the enzyme was enhanced by Na+, Ca2+, Mg2+ and Zn2+, while EDTA, PbCl2, HgCl2 and IAA were inhibitory. The ability of the purified enzyme to clarify fruit juice was also investigated. Conclusion, significance and impact of the study: This study revealed that polygalacturonase possesses properties for clarification of fruit juice and by extension bioprocessing applications.