keratolyysin

Keratolyzin is not a widely recognized enzyme name in standard biochemistry references. In practice, the term is sometimes encountered as a misspelling or variant of keratolysin or keratinase. Keratolytic enzymes, more generally, degrade keratin, the tough, fibrous protein that makes up much of the outer skin, hair, and nails.

Keratolytic enzymes cleave peptide bonds in keratin and, in many cases, aid in overcoming keratin’s highly cross-linked structure by reducing disulfide bonds or by acting on keratin’s microfibrillar arrangement. Most keratin-degrading proteases are extracellular and show activity in a neutral to alkaline pH range and at moderate temperatures. Many keratinases belong to serine protease families (such as subtilisin-like enzymes) or to metalloproteases.

Natural sources of keratinolytic enzymes include dermatophyte fungi such as Trichophyton and Microsporum, as well as keratinolytic bacteria such as Bacillus species; these organisms secrete keratinases to utilize keratin as a nutrient source. The enzymes are often produced as inactive zymogens or proenzymes and are activated outside the cell or in the surrounding medium.

Applications and relevance extend to industrial and medical contexts. Enzymatic keratinases are investigated for waste processing (feather and keratin-rich byproducts), detergent formulations, and potential enzymatic debridement or targeted keratolysis. In clinical practice, conventional keratolysis more commonly relies on chemical agents (for example, salicylic acid or urea), while enzymatic approaches remain an area of ongoing research with attention to safety and efficacy.