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Keratin 10 Triple Pack

£18£36.00Clearance
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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. Fang, 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 Jaouadi, B., Abdelmalek, B., Fodil, D., Ferradji, F. Z., Rekik, H., Zaraî, N., et al. (2010). Purification and characterization of a thermostable keratinolytic serine alkaline proteinase from Streptomyces sp. strain AB1 with high stability in organic solvents. Bioresour. Technol. 101, 8361–8369. doi: 10.1016/j.biortech.2010.05.066 Yamamura, S., Morita, Y., Hasan, Q., Yokoyama, K., and Tamiya, E. (2002). Keratin degradation: a cooperative action of two enzymes from Stenotrophomonas sp. Biochem. Biophys. Res. Commun. 294, 1138–1143. doi: 10.1016/S0006-291X(02)00580-6 This is the best treatment I have found yet. After having my hair burnt at a salon a year ago, there was nothing that would disguise the dry and brittle blonde strands in my hair, so spent most part of the year with my hair up. I came across this mask and it is the ONLY thing that has saved my hair. I had stay away for work and regrettably did not take this with me. Again, my hair was straight up in a bun after it was washed. This is the best thing I have used and will also try the leave in treatment. I am excited to think it will make my hair even more silkier!

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

Hassan, M. A., Abol-Fotouh, D., Omer, A. M., Tamer, T. M., and Abbas, E. (2020). Comprehensive insights into microbial keratinases and their implication in various biotechnological and industrial sectors: a review. Int. J. Biol. Macromol. 154, 567–583. doi: 10.1016/j.ijbiomac.2020.03.116 Cai, C.-G., Lou, B.-G., and Zheng, X.-D. (2008). Keratinase production and keratin degradation by a mutant strain of Bacillus subtilis. J. Zhejiang Univ. Sci. B 9, 60–67. doi: 10.1631/jzus.B061620Zeng, Y.-H., Shen, F.-T., Tan, C.-C., Huang, C.-C., and Young, C.-C. (2011). The flexibility of UV-inducible mutation in Deinococcus ficus as evidenced by the existence of the imuB–dnaE2 gene cassette and generation of superior feather degrading bacteria. Microbiol. Res. 167, 40–47. doi: 10.1016/j.micres.2011.02.008 Fang, Z., Zhang, J., Liu, B., Jiang, L., Du, G., and Chen, J. (2014). Cloning, heterologous expression and characterization of two keratinases from Stenotrophomonas maltophilia BBE11-1. Process Biochem. 49, 647–654. doi: 10.1016/j.procbio.2014.01.009 Kim, J. M., Lim, W. J., and Suh, H. J. (2001). Feather-degrading Bacillus species from poultry waste. Process Biochem. 37, 287–291. doi: 10.1016/S0032-9592(01)00206-0

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

Gurung, S. K., Adhikari, M., Kim, S. W., Bazie, S., Kim, H. S., Lee, H. G., et al. (2018). Discovery of two Chrysosporium species with keratinolytic activity from field soil in Korea. Mycobiology 46, 260–268. doi: 10.1080/12298093.2018.1514732 Yong, B., Fei, X., Shao, H., Xu, P., Hu, Y., Ni, W., et al. (2020). Recombinant expression and biochemical characterization of a novel keratinase BsKER71 from feather degrading bacterium Bacillus subtilis S1-4. AMB Express 10:9. doi: 10.1186/s13568-019-0939-6 Bouacem, K., Bouanane-Darenfed, A., Zaraî Jaouadi, N., Joseph, M., Hacene, H., Ollivier, B., et al. (2016). Novel serine keratinase from Caldicoprobacter algeriensis exhibiting outstanding hide dehairing abilities. Int. J. Biol. Macromol. 86, 321–328. doi: 10.1016/j.ijbiomac.2016.01.074 Qiu, J., Wilkens, C., Barrett, K., and Meyer, A. S. (2020). Microbial enzymes catalyzing keratin degradation: classification, structure, function. Biotechnol. Adv. 44:107607. doi: 10.1016/j.biotechadv.2020.107607 Tinoco A, et al. (2018). Keratin-based particles for protection and restoration of hair properties.DOI:Basit A, et al. (2018). Health improvement of human hair and their reshaping using recombinant keratin K31. 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. Mazotto, A. M., Couri, S., Damaso, M. C. T., and Vermelho, A. B. (2013). Degradation of feather waste by Aspergillus niger keratinases: comparison of submerged and solid-state fermentation. Int. Biodeterior. Biodegradation 85, 189–195. doi: 10.1016/j.ibiod.2013.07.003 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

KRT10 Gene - GeneCards | K1C10 Protein | K1C10 Antibody

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 Deniz, I., Demir, T., Oncel, S. S., Hames, E. E., and Vardar-Sukan, F. (2021). Effect of agitation and aeration on keratinase production in bioreactors using bioprocess engineering aspects. Protein J. doi: 10.1007/s10930-021-09978-5 Sala, L., Gautério, G. V., Younan, F. F., Brandelli, A., Moraes, C. C., and Kalil, S. J. (2014). Integration of ultrafiltration into an aqueous two-phase system in the keratinase purification. Process Biochem. 49, 2016–2024. doi: 10.1016/j.procbio.2014.07.013 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 Gurav, R. G., and Jadhav, J. P. (2013). A novel source of biofertilizer from feather biomass for banana cultivation. Environ. Sci. Pollut. Res. 20, 4532–4539. doi: 10.1007/s11356-012-1405-zGuangdong Provincial Engineering Laboratory of Biomass High Value Utilization, Institute of Bioengineering, Guangdong Academy of Sciences, Guangzhou, China Gong, J.-S., Ye, J.-P., Tao, L.-Y., Su, C., Qin, J., Zhang, Y.-Y., et al. (2020). Efficient keratinase expression via promoter engineering strategies for degradation of feather wastes. Enzyme Microb. Technol. 137:109550. doi: 10.1016/j.enzmictec.2020.109550

It’s A 10 Miracle Leave-In Plus Keratin review - Reviewed

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. Kluskens, L. D., Voorhorst, W. G., Siezen, R. J., Schwerdtfeger, R. M., Antranikian, G., van der Oost, J., et al. (2002). Molecular characterization of fervidolysin, a subtilisin-like serine protease from the thermophilic bacterium Fervidobacterium pennivorans. Extremophiles 6, 185–194. doi: 10.1007/s007920100239 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 Pierce JS, et al. (2011). Characterization of formaldehyde exposure resulting from the use of four professional hair straightening products. DOI:

Kang, D., Jacquiod, S., Herschend, J., Wei, S., Nesme, J., and Sørensen, S. J. (2020). Construction of simplified microbial consortia to degrade recalcitrant materials based on enrichment and dilution-to-extinction cultures. Front. Microbiol. 10:3010. doi: 10.3389/fmicb.2019.03010 QL appreciates the support from Institute of Bioengineering, Guangdong Academy of Sciences, China. Footnotes Wait to wash. You’ll have to wait 3 to 4 days post-keratin treatment to get your hair wet, so if you’re not a person who likes skipping wash day, then this treatment may not be right for you, and some people report a musty smell even after washing.

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