PRODUCTION AND CHARACTERIZATION OF TANNASE ENZYME BY ASPERGILLUS NIGER UNDER SOLID STATE FERMENTATION USING FRUIT PEELINGS (ORANGE AND BANANA PEELS)

Authors

  • Anum Shahbaz
  • Aneela Tabassum
  • Sara Mahmood
  • Dr Afsheen Aqeel
  • Qaiser Ali Sultan
  • Yasmin Khanam
  • Rida Sattar
  • Kiran Ghafoor

Keywords:

Tananse enzyme, Solid state fermentation, Aspergillus niger, Fruit Peelings

Abstract

Tannase (tannin acyl hydrolase) is a hydrolytic enzyme widely used in food and medical industries. Pure tannic acid is currently used for industrial scale production of tannase which is expensive and adds on to the cost of the final product. The present study focuses on utilization of fruit peelings (banana and orange peels) as a cheap substrate for producing tannase through solid state fermentation by using Aspergillus niger. Fermentation parameters like temperature, pH and fermentation period etc were optimized for enzyme production. The maximum yield (23.3U/ml/min) of tannase was obtained by using banana peels substrate at 35oC, pH 5 and an incubation period of 96 hrs by using Aspergillus niger. After optimization tannase was partially purified by ammonium sulphate fractionation. Partially purified enzyme was characterized by considering the effects of different parameters on enzyme activity. Highest activity of partially purified tannase was found at temperature (35oC),incubation time (25min),pH (5) and tannic acid concentration (0.7%w/v) with substrate of banana peels .The purified enzyme showed maximum activity at the Vmax of 0.83U/ml and Km of 0.155 g/ml when orange peels was used as a substrate using Aspergillus niger.

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Published

2025-09-20

How to Cite

Anum Shahbaz, Aneela Tabassum, Sara Mahmood, Dr Afsheen Aqeel, Qaiser Ali Sultan, Yasmin Khanam, … Kiran Ghafoor. (2025). PRODUCTION AND CHARACTERIZATION OF TANNASE ENZYME BY ASPERGILLUS NIGER UNDER SOLID STATE FERMENTATION USING FRUIT PEELINGS (ORANGE AND BANANA PEELS). Policy Research Journal, 3(9), 664–672. Retrieved from https://policyrj.com/1/article/view/1052