PURIFICATION AND CHARACTERIZATION OF KERATINASE FROM BACTERIAL ISOLATE AND ITS APPLICATION IN DEHAIRINGN. SARASWATHY, R.S. JANANI, S. SAHANA, N. SUBARNA, R. SHANA RAM, S. BALAJI, V. VEERABHUVANESHWARI AND P. RAMALINGAMAbstract Feather waste reaches millions of tons per year worldwide as a byproduct of commercial poultry processing plants constitutes over 90% protein, the main component is beta-keratin, a fibrous and insoluble structural protein extensively cross-linked by disulfide bonds, which is not easily degradable by common proteolytic enzymes. Alternatively, keratinases which are produced by the keratinolytic organisms could be used as a sustainable approach to degrade the feather waste. An effective feather degrading bacterium was isolated from soil in slaughter house dumping site. The zone of hydrolysis in casein agar plate confirms the keratinase efficiency of bacterium BSK5. The 16 S rRNA sequencing showed BSK5 strain phylogenetically homologous to Bacillus sp and the partial sequence was submitted in NCBI GenBank Databse. The total keratinase activity was found to be 16 (U/mL) in crude extract and it was partially purified by ultrafiltration. The partially purified keratinase was investigated for its dehairing efficiency in goat rawhide. Comparative study of enzymatic dehairing over conventional dehairing suggested that partially purified keratinase is a sustainable method.
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