International Journal For Multidisciplinary Research

E-ISSN: 2582-2160   •   Impact Factor: 9.24

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From Dairy Waste to Green Biocatalysis: Industrial Applications of Aspergillus niger Extracellular Protease in Eco-Friendly Dehairing, Detergent Synergy, and Peptide Synthesis

Author(s) Prof Priyanka Vidyadhar Kande Patil, Pathan Sadiya Rasul
Country India
Abstract Extracellular proteases are industrially significant enzymes widely used in the food, pharmaceutical, textile, bioremediation, and detergent industries. This study investigates the production, optimization, and characterization of extracellular protease by Aspergillus niger utilizing skim milk casein as an efficient, protein-rich, and cost-effective inducer substrate under submerged fermentation (SmF) conditions. The fungal strain was successfully isolated, screened qualitatively on skim milk agar plates, and monitored quantitatively via standard biochemical assays. Qualitative screening demonstrated prominent proteolytic activity with clear zones of casein hydrolysis around the fungal colonies. Quantitative optimization of key process variables revealed that maximum protease yield was achieved at an incubation period of 72 to 120 hours, a moderate incubation temperature of 28–30°C, and an optimal pH range of 5.0–6.0. The crude enzyme, harvested via high-speed centrifugation, displayed stable catalytic breakdown of casein substrate, yielding significant tyrosine equivalents. These findings reinforce the robust secretory capacity and commercial viability of Aspergillus niger as a generally recognized as safe (GRAS) microbial factory, demonstrating that dairy by-products like skim milk casein can serve as high-yield industrial substrates, advancing sustainable waste valorization and green biocatalysis.
Keywords Aspergillus niger, Extracellular Protease, Skim Milk Casein, Submerged Fermentation, Process Optimization, Waste Valorization.
Field Biology
Published In Volume 8, Issue 3, May-June 2026
Published On 2026-06-02
DOI https://doi.org/10.36948/ijfmr.2026.v08i03.80266
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