Publikace UTB
Repozitář publikační činnosti UTB

Preparation of keratin hydrolysate from chicken feathers and its application in cosmetics

Repozitář DSpace/Manakin

Zobrazit minimální záznam


dc.title Preparation of keratin hydrolysate from chicken feathers and its application in cosmetics en
dc.contributor.author Mokrejš, Pavel
dc.contributor.author Huťťa, Matouš
dc.contributor.author Pavlačková, Jana
dc.contributor.author Egner, Pavlína
dc.relation.ispartof Journal of Visualized Experiments
dc.identifier.issn 1940-087X Scopus Sources, Sherpa/RoMEO, JCR
dc.date.issued 2017
utb.relation.volume 2017
utb.relation.issue 129
dc.type article
dc.language.iso en
dc.publisher Journal of Visualized Experiments
dc.identifier.doi 10.3791/56254
dc.relation.uri https://www.jove.com/video/56254/preparation-keratin-hydrolysate-from-chicken-feathers-its-application
dc.subject Alkaline-enzyme hydrolysis en
dc.subject Biochemistry en
dc.subject Chicken feathers en
dc.subject Cosmetic formulation en
dc.subject Humectant en
dc.subject Hydration en
dc.subject Issue 129 en
dc.subject Keratin en
dc.subject Keratin hydrolysate en
dc.subject Ointment base en
dc.subject Transepidermal water loss en
dc.description.abstract Keratin hydrolysates (KHs) are established standard components in hair cosmetics. Understanding the moisturizing effects of KH is advantageous for skin-care cosmetics. The goals of the protocol are: (1) to process chicken feathers into KH by alkaline-enzymatic hydrolysis and purify it by dialysis, and (2) to test if adding KH into an ointment base (OB) increases hydration of the skin and improves skin barrier function by diminishing transepidermal water loss (TEWL). During alkaline-enzymatic hydrolysis feathers are first incubated at a higher temperature in an alkaline environment and then, under mild conditions, hydrolyzed with proteolytic enzyme. The solution of KH is dialyzed, vacuum dried, and milled to a fine powder. Cosmetic formulations comprising from oil in water emulsion (O/W) containing 2, 4, and 6 weight% of KH (based on the weight of the OB) are prepared. Testing the moisturizing properties of KH is carried out on 10 men and 10 women at time intervals of 1, 2, 3, 4, 24, and 48 h. Tested formulations are spread at degreased volar forearm sites. The skin hydration of stratum corneum (SC) is assessed by measuring capacitance of the skin, which is one of the most world-wide used and simple methods. TEWL is based on measuring the quantity of water transported per a defined area and period of time from the skin. Both methods are fully non-invasive. KH makes for an excellent occlusive; depending on the addition of KH into OB, it brings about a 30% reduction in TEWL after application. KH also functions as a humectant, as it binds water from the lower layers of the epidermis to the SC; at the optimum KH addition in the OB, up to 19% rise in hydration in men and 22% rise in women occurs. © 2017 Journal of Visualized Experiments. en
utb.faculty Faculty of Technology
dc.identifier.uri http://hdl.handle.net/10563/1007683
utb.identifier.obdid 43877045
utb.identifier.scopus 2-s2.0-85037647244
utb.identifier.wok 000417688700036
utb.source j-scopus
dc.date.accessioned 2018-01-15T16:31:39Z
dc.date.available 2018-01-15T16:31:39Z
utb.contributor.internalauthor Mokrejš, Pavel
utb.contributor.internalauthor Huťťa, Matouš
utb.contributor.internalauthor Pavlačková, Jana
utb.contributor.internalauthor Egner, Pavlína
utb.fulltext.affiliation Pavel Mokrejš1, Matouš Huťťa1, Jana Pavlačková2, Pavlína Egner2 1 Department of Polymer Engineering, Faculty of Technology, Tomas Bata University in Zlín 2 Department of Fat, Tenside and Cosmetics Technology, Faculty of Technology, Tomas Bata University in Zlín Correspondence to: Pavel Mokrejš at mokrejs@ft.utb.cz
utb.fulltext.dates Date Published: 11/27/2017
utb.fulltext.references 1. Poultry Slaughter, 2016 Summary. United States Department of Agriculture - National Agricultural Statistics Services. February (2017). 2. McGovern, V. Recycling poultry feathers: more bang for the cluck. Environ.Health Perspect. 108 (8), A336-A339, (2000). 3. Gousterova, A., et al. Degradation of keratin and collagen containing wastes by newly isolated thermoactinomycetes or by alkaline hydrolysis. Lett. Appl. Microbiol. 40 (5), 335-340, (2005). 4. Yamauchi, K., Yamauchi, A., Kusunoki, T., Khoda, A., Konishi, Y. Preparation of stable aqueous solution of keratins, and physiochemical and biodegradational properties of films. Biomed. Mater. Res. 31 (4), 439-444, (1996). 5. Schrooyen, P.M.M., Dijkstra, P.J., Oberthur, R.C., Bantjes, A., Feijen, J. Partially carboxymethylated feather keratins. 2. Thermal and mechanical properties of films. J. Agric. Food Chem. 49 (1), 221-230, (2001). 6. Mark, H.F., Gaylord, N.G., Bikales, N.M. Encyclopedia of Polymer Science Technology: vol. 8: Keratin to Modacrylic Fibers. New York, WileyInterscience (1968). 7. Bertsch, A., Cello, N. A biotechnological process for treatment and recycling poultry feathers as a feed ingredient. Bioresour. Technol. 96 (15), 1703-1708, (2005). 8. Grazziotin, A., Pimentel, F.A., de Jong, E.V., Brandelli, A. Nutritional improvement of feather protein by treatment with microbial keratinase. Animal Feed Sci. Technol. 126 (1-2), 135-144 (2006). 9. Brandelli, A. Bacterial keratinases: useful enzymes for bioprocessing agroindustrial wastes and beyond. Food Bioprocess Technol. 1 (2), 105-116, (2008). 10. Gusta, R., Ramnani, P. Microbial keratinases and their prospective applications: an overview. Appl.Microbiol. Biotechnol. 70 (1), 21-33, (2006). 11. Vasileva-Tonkova, E., Gousterova, A., Neshev, G. Ecologically safe method for improved feather wastes biodegradation. International Biodeterior. Biodegradation. 63 (8), 1008-1012 (2009). 12. Lodén, M. Hydrating Substance. In: Barel, A.O., Paye, M., Maibach, H.I. (eds). Handbook of Cosmetic Science and Technology. New York: Informa, Healthcare, pp. 107-119 (2009). 13. Teglia, A., Secchi, G. Proteins in Cosmetics. In: Goddard, E.D., Gruber, J.V. (eds). Principles of Polymer Science and Technology in Cosmetics and Personal Care. New York, Marcel Dekker, Chapter 9 (1999). 14. Magdassi, S. Delivery systems in cosmetics. Colloids and Surfaces A: Physicochem. Engin. Aspects. 123-124, 671-679, (1997). 15. Dahms, G., Jung, A. Method for producing a protein hydrolysate. U.S. Patent 20140323702 (2014). 16. Pons, R., Carrera, I., Erra, P., Kunieda, G, Solans, C. Novel preparation methods for highly concentrated water-in-oil emulsions. Colloids and Surfaces A: Physicochem. Engin. Aspects. 91 (3), 259-266, (1994). 17. Mokrejs, P., Hrncirik, J., Janacova, D., Svoboda, P. Processing of keratin waste of meat industry. Asian J. Chem. 24 (4), 1489-1494 (2012). 18. Mokrejs, P., Svoboda, P., Hrncirik, J. Processing poultry feathers into keratin hydrolysate through alkaline-enzymatic hydrolysis. Waste Manage. Res. 29 (3), 260-267, (2011). 19. Mokrejs, P., Krejci, O., Svoboda, P. Producing keratin hydrolysates from sheep wool. Orient. J. Chem. 27 (4), 1303-1309 (2011). 20. Mokrejs, P., Krejci, O., Svoboda P., Vasek, V. Modeling technological conditions for breakdown of waste sheep wool. Rasayan J. Chem. 4 (4), 728-735 (2011). 21. Polaskova, J., Pavlackova, J., Vltavska, P., Mokrejs, P., Janis, R. Moisturizing effect of topical cosmetic products applied to dry skin. J. Cosmet. Sci. 64 (5), 329-340 (2013). 22. Polaskova, J., Pavlackova, J., Egner, P. Effect of vehicle on the performance of active moisturizing substances. Skin Res. Technol. 21 (4), 403-412, (2015). 23. Verdier-Sévrain, S., Bonté, F. Skin hydration: a review on its molecular mechanisms. J. Cosmet. Dermatol. 6 (2), 75-82, (2007). 24. Darlenski, R., Sassning, S., Tsankov, N., Fluhr, J.W. Non-invasive in vivo methods for investigation of the skin barrier physical properties. Eur. J. Pharm. Biopharm. 72 (2), 295-303, (2009). 25. Berardesca, E. EEMCO guidance for assessment of stratum corneum hydration: electrical methods. Skin Res. Technol. 3 (2): 126-132, (1997). 26. Rogiers, V. EEMCO guidance for the assessment of transepidermal water loss in cosmetic sciences. Skin Pharmacol. Appl. Skin Physiol. 14 (2), 117-128, 56341 (2001). 27. Ali, S.M., Yosipovitch, G. Skin pH: from basic science to basic skin care. Acta Derm. Venereol. 93 (3), 261-2177, (2013). 28. Agache, P., Humbert, P. Measuring the Skin. Berlin, Springer-Verlag (2004). 29. International Ethical Guidelines for Biomedical Research Involving Human Subjects. Council for International Organizations of Medical Sciences, Geneva (2002). 30. Ruland, J.K. Transdermal permeability and skin accumulation of amino acids. Int. J. Pharm. 72 (2), 149-155 (1991). 31. Draelos, Z.D. Therapeutic moisturizers. Dermatol. Clin. 18 (4), 597-607 (2000). 32. Information and Operating Instructions for the Multi probe Adapter MPA and its Probe. Courage and Khazaka Electronic GmbH, Technical Charges (2013).
utb.fulltext.sponsorship This article was written with support of the project IGA/FT/2017/007 of Tomas Bata University in Zlin.
utb.wos.affiliation [Mokrejs, Pavel; Hut't'a, Matous] Tomas Bata Univ Zlin, Fac Technol, Dept Polymer Engn, Zlin, Czech Republic; [Pavlackova, Jana; Egner, Pavlina] Tomas Bata Univ Zlin, Fac Technol, Dept Fat Tenside & Cosmet Technol, Zlin, Czech Republic
utb.scopus.affiliation Department of Polymer Engineering, Faculty of Technology, Tomas Bata University in Zlín, Czech Republic; Department of Fat, Tenside and Cosmetics Technology, Faculty of Technology, Tomas Bata University in Zlín, Czech Republic
utb.fulltext.projects IGA/FT/2017/007
Find Full text

Soubory tohoto záznamu

Zobrazit minimální záznam