Patented Keratinolytic Enzymes for Industrial Application: An Overview.

Proteases that perform keratin hydrolysis (keratinases) have great potential in biotechnology. After investigation, the next step to an industrial application is protecting intellectual property by patenting. There are many fields of discovered keratinase implementation dictated by features of the molecule and its producer.

Keratinolytic Properties of Promising for Biodegradation.

The high demand for keratinolytic enzymes and the modest presentation of fungal keratinase diversity studies in scientific sources cause a significant interest in identifying new fungal strains of keratinase producers, isolating new enzymes and studying their properties. Four out of the 32 cultures showed a promising target activity on protein-containing agar plates- A6, VKPM F-1593, 247, and 1779. The highest values of keratinolytic activity were demonstrated by extracellular proteins synthesized by VKPM F-1593 cultivated under submerged conditions on a medium containing milled chicken feathers.

Chicken Feather Waste Valorization Into Nutritive Protein Hydrolysate: Role of Novel Thermostable Keratinase From RSA27.

Microbial keratinases exhibit a momentous role in converting keratin biowastes into exceedingly valuable protein supplements. This study reports a novel, highly stable keratinase from RSA27 for the production of pure peptides rich in essential amino acids from chicken feathers. Purified keratinase showed a specific activity of 38.

Sustainable Applications of Animal Waste Proteins.

Currently, the growth of the global population leads to an increase in demand for agricultural products. Expanding the obtaining and consumption of food products results in a scale up in the amount of by-products formed, the development of processing methods for which is becoming an urgent task of modern science. Collagen and keratin make up a significant part of the animal origin protein waste, and the potential for their biotechnological application is almost inexhaustible.