Production and characterization of a novel thermo- and detergent stable keratinase from Bacillus sp. NKSP-7 with perceptible applications in leather processing and laundry industries.

International Journal of Biological Macromolecules
Fatima AkramZuriat Jabbar

Abstract

Keratinase has the ability to degrade the recalcitrant keratinous wastes that cannot be degraded by conventional proteases. The present study describes a novel hyperstable keratinolytic enzyme from Bacillus sp. NKSP-7, which has excellent efficiency of keratin-feather biodegradation, washing and dehairing. The production of extracellular keratinase was improved by 3.02-fold through optimization of various parameters. Purified keratinase (25 kDa) showed optimal activity at 65 °C and pH 7.5, and displayed stability over a range of pH (5.5-9.5) and temperature (20-60 °C) for 8 h. No conspicuous effect was perceived with various chemicals and organic solvents, however, the catalytic efficiency was enhanced in the presence of Ca2+, Cd2+, Na+, Mn2+, sodium sulfite, and β-mercaptoethanol. The enzyme was completely inhibited by phenylmethanesulfonyl fluoride (PMSF), suggesting that this keratinase belongs to serine protease family. It displayed prodigious stability and compatibility to salinity and commercial detergents. Enzyme exhibited great substrate specificity but high affinity was observed with keratin-rich substrates. Crude and purified keratinase revealed perceptible potential for destaining of blood-stained fabric (10 min), an...Continue Reading

Citations

Apr 18, 2021·World Journal of Microbiology & Biotechnology·Cíntia Lionela Ambrosio de MenezesRonivaldo Rodrigues da Silva

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