Optimized amylase production from Alternaria citri using low-cost waste materials was achieved, and the resulting enzyme was subsequently purified and biochemically characterized. Fermentation parameters were optimized for maximum amylase production at pH 6.0, 30°C, and 72 h incubation period, using potato peel powder as the substrate at 1%. Crude enzyme was purified by ammonium sulfate precipitation, dialysis, and gel filtration chromatography. Biochemical characterization revealed that the enzyme showed maximum catalytic activity at 50°C and pH 6.0. Kinetic analysis indicated a low Km of 0.34 ± 0.008 mg/mL and a high Vmax value of 0.52 ± 0.037 mg/mL/min, indicating strong substrate affinity and an efficient reaction rate. The enzyme showed good residual activity toward several additives. Amylase showed 85%-100% and 100%-140% activity in the presence of detergents at 40°C and 50°C, respectively, indicating excellent stability and compatibility with commercial detergents. Wash performance analysis further confirmed amylase's suitability as an additive for commercial detergents. The findings establish A. citri-derived amylase as a robust, thermostable, and industrially relevant biocatalyst utilizing waste materials, with significant potential for application in detergent formulations and other biotechnological processes.
Building similarity graph...
Analyzing shared references across papers
Loading...
Shakeel Ahmed
Ahmad Wakeel
Hina Andaleeb
Biotechnology and Applied Biochemistry
Bahauddin Zakariya University
Building similarity graph...
Analyzing shared references across papers
Loading...
Ahmed et al. (Tue,) studied this question.
www.synapsesocial.com/papers/69d8968f6c1944d70ce081ee — DOI: https://doi.org/10.1002/bab.70168