Keratin 10 Triple Pack

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Dmello C, Srivastava SS, Tiwari R, Chaudhari PR, Sawant S, Vaidya MM. Dmello C, et al. J Biosci. 2019 Jun;44(2):33. J Biosci. 2019. PMID: 31180046 Review.

Structure, Application, and Biochemistry of Frontiers | Structure, Application, and Biochemistry of

The process involves getting your hair washed, then having a stylist brush the treatment onto wet hair where it will sit for about 30 minutes. Keratin is a naturally occurring protein in the hair. In fact, it is the main ingredient of hair. Whilst highly durable, keratin can be damaged through chemical processes such as colouring and thermal hair processes such as the use of hair straighteners, curling tongs and even hairdryers. 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 MORECallegaro, K., Welter, N., and Daroit, D. J. (2018). Feathers as bioresource: microbial conversion into bioactive protein hydrolysates. Process Biochem. 75, 1–9. doi: 10.1016/j.procbio.2018.09.002 Wu, W.-L., Chen, M.-Y., Tu, I. F., Lin, Y.-C., EswarKumar, N., Chen, M.-Y., et al. (2017). The discovery of novel heat-stable keratinases from Meiothermus taiwanensis WR-220 and other extremophiles. Sci. Rep. 7:4658. doi: 10.1038/s41598-017-04723-4

KERATIN 10 – Extreme Rehydration TREATMENT BUTTER 500ml KERATIN 10 – Extreme Rehydration TREATMENT BUTTER 500ml

Moridshahi, R., Bahreini, M., Sharifmoghaddam, M., and Asoodeh, A. (2020). Biochemical characterization of an alkaline surfactant-stable keratinase from a new keratinase producer, Bacillus zhangzhouensis. Extremophiles 24, 693–704. doi: 10.1007/s00792-020-01187-9 Jeevana Lakshmi, P., Kumari Chitturi, C. M., and Lakshmi, V. V. (2013). Efficient degradation of feather by keratinase producing Bacillus sp. Int. J. Microbiol. 2013:7. doi: 10.1155/2013/608321 Han W, Hu C, Fan ZJ, Shen GL. Han W, et al. Sci Rep. 2021 Jan 13;11(1):1023. doi: 10.1038/s41598-020-80336-8. Sci Rep. 2021. PMID: 33441834 Free PMC article. The keratin in these treatments may be derived from wool, feathers, or horns. Certain shampoos and conditioners contain keratin, but you’ll typically get the greatest benefits from a salon treatment done by a professional. QL appreciates the support from Institute of Bioengineering, Guangdong Academy of Sciences, China. Footnotes

Nasipuri, P., Herschend, J., Brejnrod, A. D., Madsen, J. S., Espersen, R., Svensson, B., et al. (2020). Community-intrinsic properties enhance keratin degradation from bacterial consortia. PLoS One 15:e0228108. doi: 10.1371/journal.pone.0228108 Healthline has strict sourcing guidelines and relies on peer-reviewed studies, academic research institutions, and medical associations. We avoid using tertiary references. You can learn more about how we ensure our content is accurate and current by reading our editorial policy. Ramnani, P., Singh, R., and Gupta, R. (2005). Keratinolytic potential of Bacillus licheniformis RG1: structural and biochemical mechanism of feather degradation. Can. J. Microbiol. 51, 191–196. doi: 10.1139/w04-123 Protein 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). Papadopoulos, M. C. (1989). Effect of processing on high-protein feedstuffs: a review. Biol. Wastes 29, 123–138. doi: 10.1016/0269-7483(89)90092-X

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Fang, N., Zhong, C.-Q., Liang, X., Tang, X.-F., and Tang, B. (2010). Improvement of extracellular production of a thermophilic subtilase expressed in Escherichia coli by random mutagenesis of its N-terminal propeptide. Appl. Microbiol. Biotechnol. 85, 1473–1481. doi: 10.1007/s00253-009-2183-5Fang, Z., Zhang, J., Liu, B., Du, G., and Chen, J. (2016b). Enhancement of the catalytic efficiency and thermostability of Stenotrophomonas sp. keratinase KerSMD by domain exchange with KerSMF. Microb. Biotechnol. 9, 35–46. doi: 10.1111/1751-7915.12300

Keratin 10 Surface-Exposed Residues Mutations Affecting Keratin 10 Surface-Exposed Residues

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 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. Lin, X., Lee, C.-G., Casale, E. S., and Shih, J. C. H. (1992). Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis Strain. Appl. Environ. Microbiol. 58, 3271–3275.Li, Q. (2019). Progress in microbial degradation of feather waste. Front. Microbiol. 10:2717. doi: 10.3389/fmicb.2019.02717