article · Biotechnology & Biotechnological Equipment
A wild-type bacterium identified as Bacillus safensis and its ultraviolet-induced mutant produce keratinase enzymes capable of breaking down tough proteins. Testing established that the mutant variant generated higher yields of keratinase than the wild strain across a 120-hour period. Both enzyme variants operated optimally at 40 degrees Celsius and neutral pH, exhibiting notable stability over twelve hours under these conditions. The enzymes displayed strong specificity towards chicken feathers rather than human or bovine hair. Furthermore, both strains degraded whole chicken feathers completely at ambient temperature and dehaired goat skin without causing damage, with the mutant achieving faster processing times. The enzymes also successfully cleared blood stains from fabric within three hours, demonstrating that the strain and its mutant serve as effective biocatalysts across multiple degradation and cleaning tasks.
Managing tough biological waste like feathers and processing animal skins often requires harsh chemicals that harm the environment. Keratinase enzymes from Bacillus safensis offer a biological alternative capable of breaking down resilient keratins, cleaning fabrics, and processing animal hides gently. Improving enzyme yields through strain mutation makes these environmentally friendly biological processes substantially faster and more efficient for practical use.
The findings point to direct applications in poultry waste management, leather tanning for skin dehairing, and laundry detergent formulation for stain removal. Target users include tanneries, agricultural waste processors, and cleaning product manufacturers. The research represents early-stage to applied laboratory testing, having confirmed efficacy on real substrates like feathers, goat skin, and fabric, but industrial scale-up and commercial viability have not yet been evaluated.
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A newly isolated bacterium identified as Bacillus safensis based on biochemical tests and 16S rRNA analysis and its mutant variant created by exposure to ultraviolet radiation at 254 nm were investigated for keratinolytic activity. The wild-type strain produced 35.4–50.4 U/mL keratinase over a period of 120 h, while the mutant one yielded 64.4–108.5 U/mL keratinase for the same period of 120 h. The optimal conditions for the enzyme activities were pH 7.5 and 40 °C. The mutant and wild-type strain keratinases retained 59% and 54% of their activity after 12 h pretreatment at 40 °C, and 64% and 60% of their activity after 12 h at pH 7.5, respectively. The keratinases showed high substrate specificity for feathers, but low specificity for human and bovine hairs. The enzymes were activated by Na+, Ca2+, Fe2+ and Mg2+. However, while Mn2+ activated the enzyme from the mutant strain, it inhibited that of the wild type. The mutant and wild-type strain completely degraded whole chicken feathers after 6 and 9 days at 30 ± 2 °C, and also completely dehaired goat skin within 12 and 16 h, respectively, without damage to the skin. Similarly, remarkable destaining of blood-stained cloth occurred within 2–3 h. The obtained results showed an improvement in the properties of the mutant strain for use of the micro-organism or its enzyme as biocatalysts.
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DOI: 10.1080/13102818.2014.986360
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