References
- Afsar A, Cetinkaya F. 2008. Studies on the degreasing of skin using enzyme in liming process. Indian J Chem Technol. 15(5):507–510.
- Alexander P, Hudson RF, Fox M. 1950. The reaction of oxidizing agents with wool. 1. The division of cystine into two fractions of widely differing reactivities. Biochem J. 46(1):27–32. doi:https://doi.org/10.1042/bj0460027
- Andrioli E, Petry L, Gutterres M. 2015. Environmentally friendly hide unhairing: enzymatic-oxidative unhairing as an alternative to use of lime and sodium sulfide. Process Saf Environ Prot. 93:9–17. doi:https://doi.org/10.1016/j.psep.2014.06.001
- Anzani C, Prandi B, Buhler S, Tedeschi T, Baldinelli C, Sorlini G, Dossena A, Sforza S. 2017. Towards environmentally friendly skin unhairing process: a comparison between enzymatic and oxidative methods and analysis of the protein fraction of the related wastewaters. J Clean Prod. 164:1446–1454. doi:https://doi.org/10.1016/j.jclepro.2017.07.071
- Asquith RS, Parkinson DC. 1966. The morphological origin and reactions of some keratin fractions. Text Res J. 36(12):1064–1071. doi:https://doi.org/10.1177/004051756603601206
- Balaji S, Kumar R, Sripriya R, Kakkar P, Ramesh DV, Reddy PNK, Sehgal PK. 2012. Preparation and comparative characterization of keratin–chitosan and keratin–gelatin composite scaffolds for tissue engineering applications. Mater Sci Eng C. 32(4):975–982. doi:https://doi.org/10.1016/j.msec.2012.02.023
- Barba C, Mendez S, Roddick-Lanzilotta A, Kelly R, Parra JL, Coderch L. 2008. Cosmetic effectiveness of topically applied hydrolysed keratin peptides and lipids derived from wool. Skin Res Technol. 14(2):243–248. doi:https://doi.org/10.1111/j.1600-0846.2007.00280.x
- Barone JR, Schmidt WF. 2006. Effect of formic acid exposure on keratin fiber derived from poultry feather biomass. Bioresour Technol. 97(2):233–242. doi:https://doi.org/10.1016/j.biortech.2005.02.039
- Costa J, Pitrez PR, Rocha C, Freitas OM, Crispim F, Delerue-Matos C, Gonçalves MP, Crispim A. 2011. Estudo da obtenção do hidrolisado queratínico do pêlo de bovino e sua aplicação como agente de recurtume. In: II Simpósio Int sobre Gerenciamento Resíduos Agropecuários e Agroindustriais, Foz do Iguaçu; p. 4.
- de Guzman RC, Merrill MR, Richter JR, Hamzi RI, Greengauz-Roberts OK, Van Dyke ME. 2011. Mechanical and biological properties of keratose biomaterials. Biomaterials. 32(32):8205–8217. doi:https://doi.org/10.1016/j.biomaterials.2011.07.054
- Dettmer A, Cavalli É, Ayub MAZ, Gutterres M. 2013. Environmentally friendly hide unhairing: enzymatic hide processing for the replacement of sodium sulfide and delimig. J Clean Prod. 47(3):11–18. doi:https://doi.org/10.1016/j.jclepro.2012.04.024
- Earland C, Raven DJ. 1961. Lanthionine formation in keratin. Nature. 191(4786):384. doi:https://doi.org/10.1038/191384a0
- Edwards B, Routh JI. 1944. Chemical studies on powdered keratins. J Biol Chem. 154:593–596.
- Fraser RDB, MacRae TP, Rogers GE. 1972. Keratins: their composition, structure and biosynthesis. Springfield (IL): Charles C. Thomas.
- Gousterova A, Nustorova M, Paskaleva D, Naydenov M, Neshev G, Vasileva-Tonkova E. 2011. Assessment of feather hydrolysate from thermophilic actinomycetes for soil amendment and biological control application. Int J Environ Res. 5(4):1065–1070.
- Grazziotin A, Pimentel FA, de Jong EV, Brandelli A. 2006. Nutritional improvement of feather protein by treatment with microbial keratinase. Anim Feed Sci Technol. 126(1-2):135–144. doi:https://doi.org/10.1016/j.anifeedsci.2005.06.002
- Hashem MA, Nur-A-Tomal MS, Mondal NR, Rahman MA. 2017. Hair burning and liming in tanneries is a source of pollution by arsenic, lead, zinc, manganese and iron. Environ Chem Lett. 15(3):501–506. doi:https://doi.org/10.1007/s10311-017-0634-2
- Jones LN, Simon M, Watts NR, Booy FP, Steven AC, Parry DAD. 1997. Intermediate filament structure: Hard α-keratin. Biophys Chem. 68(1–3):83–93. doi:https://doi.org/10.1016/S0301-4622(97)00013-6
- Kakkar P, Verma S, Manjubala I, Madhan B. 2014. Development of keratin-chitosan-gelatin composite scaffold for soft tissue engineering. Mater Sci Eng C Mater Biol Appl. 45:343–347. doi:https://doi.org/10.1016/j.msec.2014.09.021
- Korniłłowicz-Kowalska T, Bohacz J. 2011. Biodegradation of keratin waste: theory and practical aspects. Waste Manag. 31(8):1689–1701. doi:https://doi.org/10.1016/j.wasman.2011.03.024
- Lipton SH, Bodwell CE, Coleman AH. 1977. Amino acid analyzer studies of the products of peroxide oxidation of cystine, lanthionine, and homocystine. J Agric Food Chem. 25(3):624–628. doi:https://doi.org/10.1021/jf60211a050
- Marmer WN, Dudley RL. 2006. The oxidative degradation of keratin (wool and bovine hair). J Am Leather Chem Assoc. 101(11):408–415.
- Marsal A, Morera JM, Bartoli E, Borras MD. 2000. Study on an unhairing process with hydrogen peroxide and amines. J Am Leather Chem Assoc. 95:1–10.
- Mokrejs P, Huťťa M, Pavlačková J, Egner P. 2017. Preparation of keratin hydrolysate from chicken feathers and its application in cosmetics. J Vis Exp. 129:e56254.
- Mokrejs P, Hutta M, Pavlackova J, Egner P, Benicek L. 2017. The cosmetic and dermatological potential of keratin hydrolysate. J Cosmet Dermatol. 16(4):e21–e27. doi:https://doi.org/10.1111/jocd.12319
- Morera JM, Bartolí E, Gavilanes RM. 2016. Hide unhairing: achieving lower pollution loads, decreased wastewater toxicity and solid waste reduction. J Clean Prod. 112:3040–3047. doi:https://doi.org/10.1016/j.jclepro.2015.11.028
- Ogawa S, Takeda Y, Kaneyama K, Joko K, Arai K. 2009. Characterization of permanent wave and straight hairs using high pressure differential scanning calorimetry. Sen-i Gakkaishi. 65(1):24–33. doi:https://doi.org/10.2115/fiber.65.24
- Popescu C, Hocker H. 2007. Hair-the most sophisticated biological composite material. Chem Soc Rev. 36(8):1282–1291. doi:https://doi.org/10.1039/b604537p
- Reichl S. 2009. Films based on human hair keratin as substrates for cell culture and tissue engineering. Biomaterials. 30(36):6854–6866. doi:https://doi.org/10.1016/j.biomaterials.2009.08.051
- Rogers GE. 1988. Synthesis and cross-linking in the structure and growth of hair keratins. Clin Dermatol. 6(4):26–31. doi:https://doi.org/10.1016/0738-081x(88)90062-4
- Rouse JG, Van Dyke ME. 2010. A review of keratin-based biomaterials for biomedical applications. Materials (Basel). 3(2):999–1014. doi:https://doi.org/10.3390/ma3020999
- Seifter S, Gallop PM. 1966. Keratins. In: Neurath H, editor. The proteins: composition, structure, and function, Vol. 4. 2nd ed. New York (NY): Academic Press; p. 304–342.
- Shavandi A, Silva TH, Bekhit AA, Bekhit AEDA. 2017. Keratin: dissolution, extraction and biomedical application. Biomater Sci. 5(9):1699–1735. doi:https://doi.org/10.1039/c7bm00411g
- Song N-B, Lee J-H, Al Mijan M, Song KB. 2014. Development of a chicken feather protein film containing clove oil and its application in smoked salmon packaging. LWT - Food Sci Technol. 57(2):453–460. doi:https://doi.org/10.1016/j.lwt.2014.02.009
- Souza FR, Gutterres M. 2012. Application of enzymes in leather processing: a comparison between chemical and coenzymatic processes. Braz. J. Chem. Eng. 29(3):473–482. doi:https://doi.org/10.1590/S0104-66322012000300004
- Sundaram M, Legadevi R, Afrin BN, Gayathri V, Palanisammi A. 2015. A study on anti bacterial activity of keratin nanoparticles from chicken feather waste against Staphylococcus aureus (bovine mastitis bacteria) and its anti oxidant activity. Eur J Biotechnol Biosci. 3:1–5.
- Teles FRR, Cabral JMS, Santos JAL. 2001. Enzymatic degreasing of a solid waste from the leather industry by lipases. Biotechnol Lett. 23(14):1159–1163. doi:https://doi.org/10.1023/A:1010596206857
- Thakur SS, Balaram P. 2009. Characterization of alkali induced formation of lanthionine, trisulfides, and tetrasulfides from peptide disulfides using negative ion mass spectrometry. J Am Soc Mass Spectrom. 20(5):783–791. doi:https://doi.org/10.1016/j.jasms.2008.12.019
- Valeika V, Beleška K, Valeikienė V, Kolodzeiskis V. 2009. An approach to cleaner production: from hair burning to hair saving using a lime-free unhairing system. J Clean Prod. 17(2):214–221. doi:https://doi.org/10.1016/j.jclepro.2008.04.010
- Vasconcelos A, Freddi G, Cavaco-Paulo A. 2008. Biodegradable materials based on silk fibroin and keratin. Biomacromolecules. 9(4):1299–1305. doi:https://doi.org/10.1021/bm7012789
- Veselá M, Friedrich J. 2009. Amino acid and soluble protein cocktail from waste keratin hydrolysed by a fungal keratinase of Paecilomyces marquandii. Biotechnol Bioproc E. 14(1):84–90. doi:https://doi.org/10.1007/s12257-008-0083-7
- Wagner M, Bailey DG. 1999. Structure of bovine skin and hair root: a scanning electron microscope investigation. J Am Leather Chem Assoc. 94(10):378–383.
- Washburn RG, Gilmore LO, Fechheimer NS. 1958. The chemical composition of cattle hair. I, the fat, ash and nitrogen content. Ohio J Sci. 58:150–152.
- Yang G, Yao Y, Wang X. 2018. Comparative study of kerateine and keratose based composite nanofibers for biomedical applications. Mater Sci Eng C Mater Biol Appl. 83:1–8. doi:https://doi.org/10.1016/j.msec.2017.07.057
- Yin X-C, Li F-Y, He Y-F, Wang Y, Wang R-M. 2013. Study on effective extraction of chicken feather keratins and their films for controlling drug release. Biomater Sci. 1(5):528–536. doi:https://doi.org/10.1039/c3bm00158j
- Zhang J, Li Y, Li J, Zhao Z, Liu X, Li Z, Han Y, Hu J, Chen A. 2013. Isolation and characterization of biofunctional keratin particles extracted from wool wastes. Powder Technol. 246:356–362. doi:https://doi.org/10.1016/j.powtec.2013.05.037