Bacillus sp. CSK2 produced thermostable alkaline keratinase using agro-wastes: keratinolytic enzyme characterization.

ABSTRACT:

Background

Chicken feathers are the most abundant agro-wastes emanating from the poultry processing farms and present major concerns to environmentalists. Bioutilization of intractable feather wastes for the production of critical proteolytic enzymes is highly attractive from both ecological and biotechnological perspectives. Consequently, physicochemical conditions influencing keratinase production by Bacillus sp. CSK2 on chicken feathers formulation was optimized, and the keratinase was characterized.

Results

The highest enzyme activity of 1539.09?±?68.14?U/mL was obtained after 48?h of incubation with optimized conditions consisting of chicken feathers (7.5?g/L), maltose (2.0?g/L), initial fermentation pH (5.0), incubation temperature (30?°C), and agitation speed (200?rpm). The keratinase showed optimal catalytic efficiency at pH?8.0 and a temperature range of 60?°C - 80?°C. The keratinase thermostability was remarkable with a half-life of above 120?min at 70?°C. Keratinase catalytic efficiency was halted by ethylenediaminetetraacetic acid and 1,10-phenanthroline. However, keratinase activity was enhanced by 2-mercaptoethanol, dimethyl sulfoxide, tween-80, but was strongly inhibited by Al³⁺ and Fe³⁺. Upon treatment with laundry detergents, the following keratinase residual activities were achieved: 85.19?±?1.33% (Sunlight), 90.33?±?5.95% (Surf), 80.16?±?2.99% (Omo), 99.49?±?3.11% (Ariel), and 87.19?±?0.26% (Maq).

Conclusion

The remarkable stability of the keratinase with an admixture of organic solvents or laundry detergents portends the industrial and biotechnological significance of the biocatalyst.

SUBMITTER: Nnolim NE 

PROVIDER: S-EPMC7734832 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature