Keratin hydrolyzed

It is a hydrolysate of keratin protein derived from acid, enzyme, and other method of hydrolysis, which has been applied in many areas including feed and food industry, pharmacy, fertilizers, pesticides, environmental protection, leather industry, and cosmetics. Specifically, this substance can be mixed with polyamide 6 blend to prepare nanofibres for adsorption of chromium (Ⅵ).¹ Moreover, this compound may act as an effective component to fabricate shampoo, bath, and shower gel.² In addition, this chemical can be used as an effective ingredient to produce odor-removing and deodorizing composition.³ Besides, this substance has been demonstrated to function as an useful agent for hair fixatives.⁴

1. Aluigi, A.; Tonetti, C.; Vineis, C.; Varesano, A.; Tonin, C.; Casasola, R., Study on the Adsorption of Chromium (VI) by Hydrolyzed Keratin/Polyamide 6 Blend Nanofibres. J. Nanosci. Nanotechnol. 2012, 12, 7250-7259.
2. Eugene Puchalski; Emil F. Schneider; Judith A. Cohee; El-Menshawy, E.-S., Shampoo and bath and shower gel US Patent 4690818 1987.
3. S. Naito; Nemoto, T., Odor-removing and deodorizing composition employing hydrolysate of keratin material. US Patent 4591497 1986.
4. Issei Yoshioka; Kamimura, Y., Keratin hydrolyzate useful as hair fixatives US Patent 4279996 1981.

Hydrolyzed keratin is a large protein molecule that is broken down after a chemical process in a manner such that it can penetrate the hair cuticle. It is sourced from a larger keratin molecule.Keratin is broken down by splitting its bond with the addition of hydrogen and hydroxide (water). At the end of the chemical process, the keratin is reduced into smaller fragments that the hair can absorb, thanks to its lower molecular weight.

hydrolyzed keratin is a processed form of keratin that facilitates its use in skin care formulations.

Keratin hydrolyzed is prepared from chicken feathers by alkaline-enzymatic hydrolysis followed by dialysis purification, or produced from raw feathers using the keratinolytic bacterium Vibrio sp. strain kr2[2][3]. Sheep wool serves as a substrate for producing hydrolysate through optimized alkaline hydrolysis using hybrid response surface methodology with Box-Behnken design[1]. Microbial keratinase hydrolysis yields a product rich in soluble proteins without loss of essential amino acids[2].

Hydrolyzed keratin is a compound that can reverse the damage done to keratin. It is found in many hair care products and helps rejuvenate, strengthen, and moisturize the hair. In addition, this protein increases the smoothness of the hair.

Hydrolyzed protein can repair and condition damaged hair. These protein hydrolysates strengthen hair fibers and reduce hair breakage.Protein hydrolysates are often added to hair coloring products for even color absorption.Hydrolyzed protein protects the hair from the damaging effects of permanent bleaching, waving, and straightening products.It improves the texture and natural structure of the hair and forms a protective coating to shield the strands.

Keratin Hydrolyzed sourced from sheep wool and hoof meal was non-toxic in oral studies in rats (i.e. the LD50 was greater than 40 ml/kg in a 20% solution). Keratin (MW = 8000 Da and 33,000 Da; buffalo horn/hoof source) and Hydrolyzed Keratin (MW = 310 Da; sheep wool source) were non-toxic in intravenous studies in mice.

[1]Metomo, F. N. N. N., Tayi, F., Younes, E., Amadine, O., & Zahouily, M. (2024). Production of sheep wool keratin hydrolysate and evaluation of its effectiveness in promoting maize cultivation. Journal of Environmental Management, 366, 121648. https://doi.org/10.1016/j.jenvman.2024.121648
[2]Mokrejš, P., Huťťa, M., Pavlačková, J., & Egner, P. (2017). Preparation of Keratin Hydrolysate from Chicken Feathers and Its Application in Cosmetics. Journal of Visualized Experiments, 129(129). https://doi.org/10.3791/56254
[3]Grazziotin, A., Pimentel, F. A., Sangali, S., de Jong, E. V., & Brandelli, A. (2007). Production of feather protein hydrolysate by keratinolytic bacterium Vibrio sp. kr2. Bioresource Technology, 98(16), 3172–3175. https://doi.org/10.1016/j.biortech.2006.10.034