Keratin 10 Triple Pack

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With the help of the leave-in spray and a paddle brush, I can blowdry my hair in about 15 minutes to get it somewhat straight and smooth—enough so that I can run through it with a flat iron for about 30 minutes after and have it look pin straight (my preferred style). In total, I can style my hair in 45 minutes or less when I use the It’s A 10 Miracle Leave-In Plus Keratin.

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

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. 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 It's A 10 Miracle Leave-In Plus Keratin spray claims to smooth the hair for a frizz-free style. Villa ALV, et al. (2013). Feather keratin hydrolysates obtained from microbial keratinases: Effect on hair fiber.

Gum Hair - Keratin 10 - GUM HAIR SALON LIMITED

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). 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. Pierce JS, et al. (2011). Characterization of formaldehyde exposure resulting from the use of four professional hair straightening products. DOI: If I have time, I like to let my hair air-dry about 75% then dive into styling it with a blowdryer followed by a flat iron, as my hair seems to dry smoother and straighter this way. In a pinch, though, I’ll go straight to the blowdryer (mine is the Conair 1875 Watt Style and Shine Hair Dryer).

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 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. 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

keratin 10 end domains in - PubMed An unexpected role for keratin 10 end domains in - PubMed

Benefits of getting a professional keratin treatment or doing one at home can include: Smooth, shiny hairCouto AC, et al. (2013). Pregnancy, maternal exposure to hair dyes, and hair straightening cosmetics, and early age leukemia. DOI: 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 Application of keratinases in industry requires a large amount of enzymes. Therefore, fermentation is essential to produce these enzymes in a large scale to meet the demands from industry ( Zaghloul et al., 2011). Fermentation parameters such as carbon source, nitrogen source, temperature, and others need to be optimized as these parameters have an impact on the production of the keratinase. Wastes from industries such as feathers can be added into the cultural medium ( Deniz et al., 2021). In addition, other wastes such as wheat and soy beans can be used as a substrate for producing keratinases ( Syed et al., 2009; Prakash et al., 2010a). Interestingly, a study showed that glucose and ammonium nitrate are not good sources for growing Stenotrophomonas maltophilia to degrade feathers ( Qu et al., 2018). Accumulated studies suggest that different microorganisms require various fermentation conditions for large-scale production, indicating that careful exploratory studies are necessary prior to the large-scale production of the enzymes ( Jagadeesan et al., 2020; de Menezes et al., 2021; Deniz et al., 2021; Sharma and Kango, 2021). It was demonstrated that the solid-state fermentation increased keratinase production compared with the commonly used submerged fermentation ( Inácio et al., 2018). In addition to feathers and human hair used in solid-state fermentation, other low-cost resources from agriculture can be considered in fermentation ( Awad et al., 2011). 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: