Keratin 10 Triple Pack

Product Information

The type of water on your hair matters. Swimming in chlorinated or salt water (basically a pool or an ocean) can shorten the life of your keratin treatment. You’ll also need to invest in shampoo and conditioner that are free of sodium chloride and sulfates, as these can both strip the treatments. The It’s A 10 Miracle Leave-In Plus Keratin is a spray that promises to moisturize and restore hair. It claims to make hair stronger and healthier by replacing lost keratin, a type of protein in hair, skin, and nails. This spray aims to add more keratin and also protect the natural keratin in hair by offering heat protection, hydration balance, detangling, defrizzing, and shine-boosting properties. I mostly rely on it as a heat protectant before styling, but it can also be used like any other styling cream on wet hair for adding shine or smoothing the hair. What’s it like to use the It’s A 10 Miracle Leave-In Plus Keratin? Awad, G. E. A., Esawy, M. A., Salam, W. A., Salama, B. M., Abdelkader, A. F., and El-diwany, A. (2011). Keratinase production by Bacillus pumilus GHD in solid-state fermentation using sugar cane bagasse: optimisation of culture conditions using a Box-Behnken experimental design. Ann. Microbiol. 61, 663–672. doi: 10.1007/s13213-010-0187-0 Busk, P. K., and Lange, L. (2015). Classification of fungal and bacterial lytic polysaccharide monooxygenases. BMC Genomics 16:368. doi: 10.1186/s12864-015-1601-6 Rodríguez-Villanueva J, Greenhalgh D, Wang XJ, Bundman D, Cho S, Delehedde M, Roop D, McDonnell TJ. Rodríguez-Villanueva J, et al. Oncogene. 1998 Feb 19;16(7):853-63. doi: 10.1038/sj.onc.1201610. Oncogene. 1998. PMID: 9484776

KERATIN 10 gum salon EXTREME REHYDRATION HAIR BUTTER 500ml KERATIN 10 gum salon EXTREME REHYDRATION HAIR BUTTER 500ml

Since I was a kid, I’ve had extremely curly hair that’s difficult to straighten. My curls are on the kinkier side, frizzy, and often unruly, meaning that blow-drying (and then flat-ironing) my hair could take up to 90 minutes. I used to carve out time during the week dedicated just to styling my hair. After a while of this, I began to look for ways to both speed up and simplify the process. Tork, 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 To improve the activity and thermal stability of keratinases, mutagenesis was applied ( Fang et al., 2010; Wang et al., 2015; de Paiva et al., 2018; Su et al., 2019). The mutagenesis studies were carried out by treating whole cells with reagents and modifying genes using molecular biology. In a study, ethyl methanesulfonate (EMS) was used to treat the whole cells of Bacillus subtilis LFB-FIOCRUZ 1266, and the resulting mutant strains exhibited higher feather hydrolysis compared with the wild-type strain ( de Paiva et al., 2018). Treatment of feather-degrading Deinococcus ficus with UV resulted in mutants with an improved and decreased keratinolytic activity ( Zeng et al., 2011). Other chemical reagents such as ethidium bromide (EtBr) and N-methy- N’-nitro- N-nitroso-guanidine (MNG) were also able to cause mutations in the genes, which affected the keratinase activity ( Cai et al., 2008; Vidmar and Vodovnik, 2018). Reis, S. V. D., Beys-da-Silva, W. O., Tirloni, L., Santi, L., Seixas, A., Termignoni, C., et al. (2020). The extremophile Anoxybacillus sp. PC2 isolated from Brazilian semiarid region (Caatinga) produces a thermostable keratinase. J. Basic Microbiol. 60, 809–815. doi: 10.1002/jobm.202000186 Aqua (Water), Cetearyl Alcohol, Propylene Glycol, Cetrimonium Chloride, Glycerin, Behentrimonium Chloride, Hydroxyethylcellulose, Parfum (Fragrance), PEG-60 Almond Glycerides, Hydrolyzed Keratin, Silicone Quaternium-22, Hydroxypropyl Guar Hydroxypropyltrimonium Chloride, Panthenol, Isopropyl Alcohol, Amodimethicone, Dipropylene Glycol, Polyglyceryl-3 Caprate, Coumarin, Citric Acid, Limonene, Linalool, Butylphenyl methylpropional, Cocamidopropyl Betaine, Triethylene Glycol, Benzyl Alcohol, Hexyl Cinnamal, Citronellol, Benzyl Salicylate, Phenoxyethanol, Geraniol, Palmitamidopropyltrimonium Chloride, Trideceth-12, Potassium Sorbate, Magnesium Nitrate, Magnesium Chloride, Methylchloroisothiazolinone, Sodium Benzoate, Methylisothiazolinone. Fragrance

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/s13568-020-01155-8 For anyone with curly, frizzy hair like mine—or if you just have a lot of hair that takes a long time to style—I recommend giving this leave-in spray a go.

KERATIN 10 - duo pack ****SPECIAL OFFER**** KERATIN 10 - duo pack ****SPECIAL OFFER****

Your hair may also become healthier and stronger since you can air dry it more often, saving it from heat damage. Hair growth Tiwary, E., and Gupta, R. (2010a). Extracellular expression of keratinase from Bacillus licheniformis ER-15 in Escherichia coli. J. Agric. Food Chem. 58, 8380–8385. doi: 10.1021/jf100803g 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. Dozie, I. N. S., Okeke, C. N., and Unaeze, N. C. (1994). A thermostable, alkaline-active, keratinolytic proteinase from chrysosporium keratinophilum. World J. Microbiol. Biotechnol. 10, 563–567. doi: 10.1007/BF00367668Keratin is a rich resource in nature, and the amount of keratin-rich wastes is increasing annually. Keratinases play important roles in keratin recycle and have diverse applications in different fields. Studies need to be carried out to obtain active enzymes and enlarge their applications. Microbiology, molecular biology, structural biology, computation and biochemistry will play important roles in the research field of keratinases. Author Contributions 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. Kim, J.-S., Kluskens, L. D., de Vos, W. M., Huber, R., and van der Oost, J. (2004). Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin. J. Mol. Biol. 335, 787–797. doi: 10.1016/j.jmb.2003.11.006 Your individual routine ultimately depends on a few factors: your natural texture, whether it’s been chemically processed, how you wear it on a daily… READ MORE

KERATIN 10 – Protein Smoothing CONDITIONER 1 litre KERATIN 10 – Protein Smoothing CONDITIONER 1 litre

Anbu, P., Hilda, A., Sur, H.-W., Hur, B.-K., and Jayanthi, S. (2008). Extracellular keratinase from Trichophyton sp. HA-2 isolated from feather dumping soil. Int. Biodeterior. Biodegradation 62, 287–292. doi: 10.1016/j.ibiod.2007.07.017 Bohacz, J. (2016). Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss. World J. Microbiol. Biotechnol. 33:13. doi: 10.1007/s11274-016-2177-2 Sharma, I., and Kango, N. (2021). Production and characterization of keratinase by Ochrobactrum intermedium for feather keratin utilization. Int. J. Biol. Macromol. 166, 1046–1056. doi: 10.1016/j.ijbiomac.2020.10.260 Thankaswamy, S. R., Sundaramoorthy, S., Palanivel, S., and Ramudu, K. N. (2018). Improved microbial degradation of animal hair waste from leather industry using Brevibacterium luteolum (MTCC 5982). J. Clean. Prod. 189, 701–708. doi: 10.1016/j.jclepro.2018.04.095 Lange, L., Huang, Y., and Busk, P. K. (2016). Microbial decomposition of keratin in nature-a new hypothesis of industrial relevance. Appl. Microbiol. Biotechnol. 100, 2083–2096. doi: 10.1007/s00253-015-7262-1Arokiyaraj, S., Varghese, R., Ali Ahmed, B., Duraipandiyan, V., and Al-Dhabi, N. A. (2019). Optimizing the fermentation conditions and enhanced production of keratinase from Bacillus cereus isolated from halophilic environment. Saudi J. Biol. Sci. 26, 378–381. doi: 10.1016/j.sjbs.2018.10.011 Keratinous wastes are rich in amino acids ( Qiu et al., 2020) and could affect the atmosphere, water sources, and soil if they are not treated properly ( Hassan et al., 2020). On the other hand, this type of wastes serves as a low-cost resource for amino acids or can be converted into animal feeds and fertilizers ( Pettett and Ipek, 2004; Gurav and Jadhav, 2013). Compared with other natural polymers such as cellulose, starch, and collagen, extraction of keratin is a challenging process. Quite a few strategies such as physical, chemical, and biological methods are applied in keratin extraction. Although chemical and physical treatments are efficient strategies to treat keratinous wastes, a large amount of energy is needed and amino acids were destroyed during treatment. As keratin does not accumulate in nature, microorganisms are playing the major role in its degradation and recycling. Therefore, keratinous wastes threatening the environment can be converted into value-added products by using microbial treatment ( de Menezes et al., 2021; Nnolim and Nwodo, 2021). Extensive studies have been carried out to search suitable microorganisms and obtain optimized processes to make full use of keratinous wastes ( Gradišar et al., 2000; Sangali and Brandelli, 2000; Kim et al., 2001; Rai and Mukherjee, 2011). It has been shown that wastes such as feathers can be degraded by bacteria and fungi to produce other important products such as amino acids or proteins with added values ( Callegaro et al., 2018; Shanmugasundaram et al., 2018; Bohacz, 2019; Tamreihao et al., 2019; Chaudhary et al., 2021). Therefore, conversion of the wastes using microorganisms is the most environmentally friendly method while more studies are still needed to improve the degradation efficiency of keratins. As the amount of keratin-containing wastes is increasing rapidly due to various reasons, keratin derived from the wastes should be fully utilized by serving as a source of proteins, amino acids, and a low-cost resource for producing other products. The purification of keratinases is important for enzymatic characterization and other application ( Brandelli et al., 2015). In waste treatment, the enzyme purification is not needed for reducing cost and improving efficiency. To obtain a keratinase with a high purity, several strategies can be utilized. Ammonium sulfate precipitation, gel filtration chromatography, and ion-exchange chromatography are commonly used methods in the purification ( Brandelli et al., 2015). For recombinant proteins, the affinity chromatography can be used in purification based on the affinity tag that is incorporated into the target protein. Keratinases from different bacteria have been purified for biochemical characterization. Techniques such as the aqueous two-phase system are applicable to obtain a large amount of enzymes ( Bach et al., 2012; Sala et al., 2014). A carefully experimental design is vital when a large quantity of pure enzymes is needed as the purification could be an expensive step. Syed, D. G., Lee, J. C., Li, W.-J., Kim, C.-J., and Agasar, D. (2009). Production, characterization and application of keratinase from Streptomyces gulbargensis. Bioresour. Technol. 100, 1868–1871. doi: 10.1016/j.biortech.2008.09.047 Zaraî Jaouadi, N., Rekik, H., Ben Elhoul, M., Zohra Rahem, F., Gorgi Hila, C., Slimene Ben Aicha, H., et al. (2015). A novel keratinase from Bacillus tequilensis strain Q7 with promising potential for the leather bating process. Int. J. Biol. Macromol. 79, 952–964. doi: 10.1016/j.ijbiomac.2015.05.038