Keratin 10 Triple Pack

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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. Maneli MH, et al. (2014). Elevated formaldehyde concentration in "Brazilian keratin type" hair-straightening products: A cross-sectional study. DOI: 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.

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

Your hair may also become healthier and stronger since you can air dry it more often, saving it from heat damage. Hair growth Guangdong Provincial Engineering Laboratory of Biomass High Value Utilization, Institute of Bioengineering, Guangdong Academy of Sciences, Guangzhou, China It has been noted that recombinant techniques are still needed for producing keratinases with a high purity, keratinases with mutations, and keratinases originated from a pathogenic microorganism ( Liu et al., 2014). Recombinant protein expression systems and host and gene cloning strategies need to be explored ( Gong et al., 2020). As the recombinant protein is critical for exploring the function of keratinases, it is useful in studying the function and activity of the enzymes. Application of Keratinases 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. 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).The It's A 10 Miracle Leave-In Plus Keratin spray claims to smooth the hair for a frizz-free style. Benefits of getting a professional keratin treatment or doing one at home can include: Smooth, shiny hair 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.

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

Couto AC, et al. (2013). Pregnancy, maternal exposure to hair dyes, and hair straightening cosmetics, and early age leukemia. DOI: It is important to improve the enzymatic characteristics of the keratinase while caution has to be taken when the whole-cell-based mutagenesis is used. All the mutant strains should meet the safety requirement from certain authorities. Compared with random mutagenesis, structure-guided protein engineering is of great interest as the mutation is well managed. To carry out such studies efficiently, the amino acid sequence and structures need to be known. Recombinant protein production is therefore a strategy to play an important role in this process. Researchers have to make sure that the strains with modified genes are acceptable in industrial applications. Conclusion 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. Accumulated studies have shown that the crude microbial culture exhibited higher keratin degradation efficiency than the purified enzymes. A keratinase-degrading system can be developed by carefully analyzing the components or enzymes that are critical for keratin degradation. The crude culture of a microorganism is a mixture of enzymes which can be used in keratin treatment. Therefore, a mixture of enzymes can be readily obtained by exploring the effects of cultural conditions on keratin degradation. Two important elements are important in this strategy. One is to have a good strain to work with and the other is to have an optimized fermentation condition to produce an enzymatic system for keratin degradation. Structure of Keratinase Pierce JS, et al. (2011). Characterization of formaldehyde exposure resulting from the use of four professional hair straightening products. DOI:

Mechanism of Action for Keratinase

Recombinant techniques are applied to the production of keratinases ( Descamps et al., 2003; Liu et al., 2013b; Fang et al., 2014; Yong et al., 2020; Yahaya et al., 2021). This method is particularly meaningful for keratinases that are produced by pathogenic microorganisms ( Muhammed et al., 2021) and the mutants with an improved enzymatic activity and stability ( Zhang et al., 2020). The recombinant production of keratinases does not require the application of keratin as the carbon and nitrogen sources. It is possible to purify the recombinant enzymes in a fast way when an affinity purification tag is introduced. Several studies demonstrate that it is feasible to produce recombinant keratinases. Keratinases from bacteria can be produced in Escherichia coli ( Tiwary and Gupta, 2010a). It has been shown that the gene kerA encoding a keratinase from Bacillus licheniformis was expressed in Escherichia coli and Bacillus subtilis while the yield was lower than that of the wild type. An improved yield was observed by integration of multiple copies of kerA into the chromosome ( Wang et al., 2004). Therefore, producing keratinases using recombinant techniques is of great interest while extensive studies are still needed to obtain the recombinant keratinase with an improved activity. Basit A, et al. (2018). Health improvement of human hair and their reshaping using recombinant keratin K31. DOI:

10 Best Keratin Treatments for Hair in 2023 - Beauty Mag The 10 Best Keratin Treatments for Hair in 2023 - Beauty Mag

Although many keratinase producers have been isolated and identified ( Cavello et al., 2020; Jagadeesan et al., 2020; Moridshahi et al., 2020; Nnolim et al., 2020b; Reis et al., 2020), the isolation and characterization of keratinase-producing microorganisms are still an important task. The keratin degradation efficiency can be improved when more keratinases are applied ( Peng et al., 2019). Therefore, a mixture of microorganism-microbial consortia might have great potential in converting keratin-rich waste into valuable products ( Kang et al., 2020; Nasipuri et al., 2020). It is challenging to have a microbial consortium because the amount of the organism in the system will be affected under different conditions. It is also possible to set up a microbial consortium to improve keratin degradation by mixing several microorganisms which have been well characterized. This is a feasible method in industrial applications. Keratin Degradation by Keratinases You can use the It's A 10 Miracle Leave-In Plus Keratin spray as a styling cream or conditioning mask.Tinoco A, et al. (2018). Keratin-based particles for protection and restoration of hair properties.DOI: Though the It’s A 10 Miracle Leave-In Plus Keratin runs on the pricier side, it’s worth every penny to me because of how much time it saves me and how healthy it makes my hair look and feel.

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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.

Conclusion

This research was supported by funds from the “Hundred-Talent Program” (Grant Nos. 2020GDASYL-20200102010 and 2020GDASYL-20200102009), Guangdong Academy of Sciences, China. Conflict of Interest As long as you care for a keratin treatment by not washing your hair too frequently (2 to 3 times a week is enough), then your keratin treatment can last up to 6 months. More manageable hair