Optimization of Inducer Concentration to Enhance Leather Degrading Enzymes of Bacillus Sp Isolated from Different Environmental Samples

Abstract

Leather being an organic material from animal hides are resistant to be decayed. It contains protein that are challenging to be decayed as it contains complex collagen along with toxic dyes. The degradation of collagen includes the breaking down of sulfuric acid and redox reaction to produce ammonia. For this reaction to occur it takes about a time period of 25 to 50 years. Through bioremediation, the process can be fastened. Bacillus subtilis produce laccases and peroxidases (oxido reductases) in a minimum quantity. This study isolated a Bacillus sp. from soil and optimized its production of laccase and peroxidase enzymes for leather waste bioremediation. The bacteria demonstrated collagen-degrading ability, forming a clear hydrolysis zone. Enzyme production was maximized at 1.5mM Cu₂SO₄ (laccase) and 2mM MnSO₄ (peroxidase). Following partial purification and SDS-PAGE characterization, these induced enzymes showed high activity, presenting an effective, eco-friendly method for accelerating the degradation of tough leather proteins.