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In silico characterization of broad range proteases produced by Serratia marcescens EGD‐HP20

In the present study, Serratia marcescens EGD‐HP20 strain was demonstrated to utilize poultry waste comprising of both white non‐melanized and dark/brown melanized poultry feathers. The potential of the isolate to hydrolyze diverse keratinous wastes was further corroborated by comparative genomics which indicated the presence of genes for broad substrate specific proteases including metallo‐proteases, serine endoprotease, dipeptidase, oligopeptidase, etc. Multiple gene sequence alignments of above genes showed 99–100% sequence identities with that of closely related strains of S. marcescens. The secondary structure, 3D structures and energy models suggested the stable nature of all the observed enzymes. Comparative genomics and hydrolysis of mixed feather waste indicated that the above potential of the isolate was associated with synergistic action of various types of proteases.