Biochemical and Molecular Characterization of Microbial Keratinase and Its Remarkable Applications

TLDR: The bioconversion of insoluble feather keratin to soluble feather residue has high nutritional values and can be employed as a supplement for livestock feeds and other promising applications have been associated with keratinolytic enzymes.

Abstract: Microbial keratinase have become biotechnologically important enzyme since they target the hydrolysis of highly rigid, strongly cross-linked structural polypeptides “Keratin” recalcitrant. Keratins are insoluble fibrous proteins found in hair, wool, feather, nail, horns and other epithelial coursing contains beta helical coil which is linked through cysteins bridges. Keratinases, which are produced by several bacteria, fungi and actinomycetes that have been often isolated from terrestrial and marine sources. The bioconversion of insoluble feather keratin to soluble feather residue has high nutritional values and can be employed as a supplement for livestock feeds. Other promising applications have been associated with keratinolytic enzymes, including elimination of keratin in acne, depilation process, preparation of vaccinine for dermatophytosis therapy, pharmaceutical enhancement of the nail treatment and degradation of prion and prion like proteins.