Benefits of getting a professional keratin treatment or doing one at home can include: Smooth, shiny hair

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Keratin smooths cells that overlap to form hair strands, which means more manageable hair and less frizz. This makes for hair that dries with little frizz and has a glossy, healthy look to it. Gradišar, H., Kern, S., and Friedrich, J. (2000). Keratinase of Doratomyces microsporus. Appl. Microbiol. Biotechnol. 53, 196–200. doi: 10.1007/s002530050008 However, it’s important to be mindful of keratin use because too much keratin (like everyday use) can actually damage your hair. “The results of too much keratin and not enough keratin are the same results of dry, brittle hair,” Dear warns. She says keratin leave-in sprays work best on coarse, frizzy hair that tends to be more porous, as this type allows the keratin to absorb better and add a boost of hydration. Bakhtiar, S., Estiveira, R. J., and Hatti-Kaul, R. (2005). Substrate specificity of alkaline protease from alkaliphilic feather-degrading Nesterenkonia sp. AL20. Enzyme Microb. Technol. 37, 534–540. doi: 10.1016/j.enzmictec.2005.04.003Tork, S. E., Shahein, Y. E., El-Hakim, A. E., Abdel-Aty, A. M., and Aly, M. M. (2016). Purification and partial characterization of serine-metallokeratinase from a newly isolated Bacillus pumilus NRC21. Int. J. Biol. Macromol. 86, 189–196. doi: 10.1016/j.ijbiomac.2016.01.060

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Demirkan, E., Kut, D., Sevgi, T., Dogan, M., and Baygin, E. (2020). Investigation of effects of protease enzyme produced by Bacillus subtilis 168 E6-5 and commercial enzyme on physical properties of woolen fabric. J. Textile Inst. 111, 26–35. doi: 10.1080/00405000.2019.1624069 Cavello, I., Urbieta, M. S., Cavalitto, S., and Donati, E. (2020). Bacillus cytotoxicus isolated from a pristine natural geothermal area reveals high keratinolytic activity. Microorganisms 8:796. Pinski, A., Zur, J., Hasterok, R., and Hupert-Kocurek, K. (2020). Comparative genomics of Stenotrophomonas maltophilia and Stenotrophomonas rhizophila revealed characteristic features of both species. Int. J. Mol. Sci. 21:4922. Zhang, M., Jiang, L., Li, F., Xu, Y., Lv, S., and Wang, B. (2019). Simultaneous dermatophytosis and keratomycosis caused by Trichophyton interdigitale infection: a case report and literature review. BMC Infect. Dis. 19:983. doi: 10.1186/s12879-019-4612-0 Nnolim, N. E., and Nwodo, U. U. (2021). Microbial keratinase and the bio-economy: a three-decade meta-analysis of research exploit. AMB Express 11:12. doi: 10.1186/s13568-020-01155-8Protein engineering was also applied to cause an augmentation of the keratinase activity ( Fang et al., 2019). When the amino acid sequence and structure of a keratinase are available, the rational protein design can play a role in improving the activity and thermal stability of a keratinase. When amino acids essential for the protease activity, metal binding, and thermal stability are identified, computer-based methods will enable researchers to design proteins with improved enzymatic activities and thermal stabilities. This strategy has been successfully applied to the keratinase of Bacillus licheniformis BBE11 ( Liu et al., 2013a). Four amino acid substitutions (N122Y, N217S, A193P, N160C) were designed, and the corresponding genes were expressed in Bacillus subtilis WB60. A mutant keratinase with the N122Y substitution exhibited an approximately 5.6-fold increase in catalytic efficiency, suggesting that this is an efficient strategy in improving activity and stability ( Liu et al., 2013a). Other methods such as PCR-based methods and direct evolution will play a role in obtaining more potent keratinases ( Vidmar and Vodovnik, 2018). When the regulatory mechanism of a keratinase is understood, the modification on other regions of the keratinase can also improve its activity and stability ( Fang et al., 2016b; Peng et al., 2021). In a study, the N- and C-terminal regions of KerSMD were replaced with those regions of a homogenous keratinase. Replacing the N-terminal region resulted in a mutant exhibiting more than a twofold catalytic activity toward casein catalytic efficiency. Replacing the C-terminal region improved keratinases activity using succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as a substrate in a biochemical assay. Replacing both N- and C-terminal regions resulted in a mutant with an improved thermal stability ( Fang et al., 2016b). De Azeredo, L. A. I., De Lima, M. B., Coelho, R. R. R., and Freire, D. M. G. (2006). Thermophilic protease production by Streptomyces sp. 594 in submerged and solid-state fermentations using feather meal. J. Appl. Microbiol. 100, 641–647. doi: 10.1111/j.1365-2672.2005.02791.x