Pectinase production from a local isolate of Aspergillus niger using orange bagasse as a carbon source

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TIMOTHY MGBEDE
MIDA HABILA MAYEL
EMOCHONE ROY YOHANNA
MOSES ABAH ADONDUA
UGWUOKE KENNETH CHINEKWU
BIYARGA BUMA BINUNGA
TYRON JANET

Abstract

Abstract. Timothy M, Mayel MH, Yohanna ER, Adondua MA, Chinekwu UK, Binunga BB, Janet T. 2022. Pectinase production from a local isolate of Aspergillus niger using orange bagasse as a carbon source. Asian J Nat Prod Biochem 19: 81-86. Pectinases are a group of enzymes that catalyze the breakdown of pectin substances. The largest industrial applications of pectinases are in fruit juice extraction and clarification. However, it is in short supply, but due to the gradual increase in global population, fruit juice industries will need to increase the production of fruit juices, hence the need for mass production of pectinase. Little or no work has been done on producing pectinase from the locally sourced fungus Aspergillus niger in Wukari using orange bagasse as a carbon source. The present investigation was carried out to produce pectinase from a locally sourced fungus, A. niger, in Wukari, Taraba State, Nigeria. A. niger was identified morphologically and screened for pectinase production. Submerged fermentation was carried out, and the crude pectinase was harvested, with maximum enzyme production at 72 hrs. The effect of pH on pectinase activity was assessed, and different temperatures were used to test for pectinase activity. The crude enzyme's kinetic constants (Km and Vmax) were also determined. The optimal pH of pectinase was alkaline, at pH 8.0. The temperature at the crude enzyme expressed the highest activity was 50ºC. The crude enzyme activity was tested with the effect of substrate concentration; the optimum substrate concentration was discovered to be 2.0%. At the end of this research, the results showed that pectinase could be mass-produced to serve the needs of industries in demand to make good products from fruits available, considering the population increase.

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