Purification and Properties of Wickerhanomyces Anomalus Keratinase and Its Prospective Application in Poultry Feed Industries.
The pollution resulting from growing livestock wastes are posing significant threat to human health and the environment. Animal wastes emanating from cow horns, hooves and feathers contain keratin which can only be degraded by keratinolytic microorganisms. This study was carried out using cow hooves as substrate for the production of keratinase from fungus identified as Wickerhomyces anomalus 9 (18S rDNA gene sequencing) isolated from soil rich hooves using basal salt agar medium and potato dextrose agar. Keratinase activity of the isolate was assessed using skim milk agar and the enzyme was produced by solid state fermentation. The crude enzyme was purified using ammonium sulphate precipitation, ion-exchange and gel-filtration chromatography. The specific activity of the enzyme was 0.29 U/mg with a yield of 45% and a 7.25 purification fold. The optimal pH and temperature of the enzyme were 8.0 and 600C respectively. The enzyme was observed to be thermo-stable at 500C for 30 minutes. The kinetics revealed that the Vmax was 0.384U/min with Km 86.95mg/ml. The native molecular weight of the enzyme was found to be 34KDa. There was significance differences at 95% confidence with poultry feed treated with Wickerhanomyces anomalus keratinase in moisture, ash content, crude fibre, crude fat, nitrogen content, crude protein and carbohydrate compare to the untreated feed. This results suggest an environment-friendly approach for biodegradation of cow hooves wastes for production of keratinases, animal waste management as well as a promising tool for chicken feed additives.
Keywords: Keratinase, Wickerhomyces anomalus, Chromatography, Purification, Cow hooves.
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Copyright (c) 2021 Ayandiran Aina, C. O Ezeamagu, S. T. Akindele, A. O. Aleshinloye
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