1. Production, characterization, and application of Pseudomonas aeruginosaS-04 keratinase for feather utilization
- Author
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Ramalingum, Nolene, Bhagwat, Prashant, Permaul, Kugenthiren, and Pillai, Santhosh
- Abstract
The application of biotechnology through the utilization of enzymes is considered an easy and inexpensive method of producing valuable products from waste resources. The present study describes the production of a keratinolytic enzyme from Pseudomonas aeruginosaS-04, which showed efficiency for feather biodegradation. The production of extracellular keratinase was improved 1.3-fold by optimizing various parameters through the one factor at a time (OFAT) approach. The keratinase was purified to homogeneity by ammonium sulfate precipitation and DEAE-cellulose anion exchange chromatography. The purified keratinase (35.5 kDa) displayed optimal activity at 60 °C and pH 9.5 and was stable between pH 7 and 9.5 and temperatures ranging from 4 to 40 °C for 2 h. The catalytic activity of keratinase was enhanced in the presence of Fe3+and Mn2+ions, Triton X-100, Tween 20, DMSO, isopropyl alcohol and ethanol, but reduced activity was recorded in the presence of methanol and acetone. Furthermore, the enzyme activity was deactivated by EDTA, suggesting that this keratinase belongs to a metalloprotease family. The Kmand Vmaxof the purified keratinase were 7.62 mg/ml and 200 U/mg protein, respectively. The partially purified keratinase displayed remarkable feather degradation capabilities (93% after 24 h), and the nutritional properties of the resulting feather hydrolysate make it a promising candidate for use as a poultry feed ingredient. Thus, thermostable alkaline keratinase from P. aeruginosaS-04 is a promising candidate that converts low-cost chicken feather waste into a value-added product, indicating a novel approach to feather waste treatment and utilization.
- Published
- 2024
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