Chicken feathers are one of the greatest sources of keratin. These wastes, on the other hand, can be converted into valuable resources. This current study was conducted to valorize these keratinized wastes to produce microbial keratinase, using the microbes present on feathers. 15 keratinolytic bacterial strains and 15 keratinolytic fungal strains were isolated. Among the isolates from the feathers, Aeromonas caviae was identified as an efficient keratinase producer. This bacterium showed high efficiency in feather degradation (23 %) with a high enzyme activity of 42.59 U/mL at 72 h of cultivation. At 168 h of cultivation, A. caviae produced 182.5 µg/mL of soluble protein. This soluble protein contained 18 amino acids with their derivatives including; histidine, glycine, tryptophan, tyrosine, valine, and β-alanine, alanine, arginine, asparagine, creatine, glutamine, glutathione, isoleucine, leucine, lysine, methionine, cystine, taurine, ornithine, proline, and threonine. The keratinase production conditions were optimized using the Response Surface Method. The obtained enzyme was partially purified using ammonium sulfate precipitation and dialysis. Under optimum conditions of PH 9 and 80 °C a keratinase activity of 48.54 U/mL was obtained. The partially purified keratinase was characterized as a serine protease. It was activated by K+ , Mg2+, Zn2+, and Na+ , salts, and solvents including, SDS, Triton X-100, DMSO, Isopropanol, and TWEEN 80 with a notable increase in activity of 6-10%. H2O2, 2-Mercaptoethanol, and acetonitrile slightly inhibited the activity of keratinase. Moreover, the results revealed the ability of obtainable keratinase to degrade other substrates including casein, gelatin and skim milk with higher relative activity than the control. This study showed that keratinase produced by A. caviea isolated from chicken feathers is a promising tool for different industrial applications.