Abstract
Keratin is a kind of natural polymer that is abundant in feathers, wool, and hair. Being one of the natural biomolecules, keratin has excellent biological activity, biocompatibility, biodegradability, favorable material mechanical properties, and natural abundance, which exhibit significant biological and biomedical application potentials. At present, the strategies commonly used for preparing keratin from hair, feathers, wool, etc. include physical, chemical, and enzymatic methods. The present article mainly reviews the structure, classification, preparation methods, and the main biological applications of keratin, and these applications cover wound healing, hemostasis, targeted release of tissue engineering drugs, and so on. It is expected to lay the foundations for its future in-depth investigations and wide applications of keratin biomaterials.
Key points
• There are several pathways to prepare biologically active keratin from wool, feathers, and human hair, etc
• Promoting blood coagulation by keratin is related to the adhesion and activation of platelets and the aggregation of fibrin
• The biological applications of keratin, including wound healing and tissue engineering, are summarized
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References
Abdel-Fattah AM, El-Gamal MS, Ismail SA, Emran MA, Hashem AM (2018) Biodegradation of feather waste by keratinase produced from newly isolated Bacillus licheniformis ALW1. J Genet Eng Biotechnol 16(2):311–318. https://doi.org/10.1016/j.jgeb.2018.05.005
Akanda MR, Kim HY, Park M, Kim IS, Ahn D, Tae HJ, Park BY (2017) Hair growth promoting activity of discarded biocomposite keratin extract. J Biomater Appl 32(2):230–241. https://doi.org/10.1177/0885328217717076
Alahyaribeik S, Ullah A (2020) Methods of keratin extraction from poultry feathers and their effects on antioxidant activity of extracted keratin. Int J Biol Macromol 148:449–456. https://doi.org/10.1016/j.ijbiomac.2020.01.144
Alejandro B-E, Redondo PC, Lopez E, Albarran L, Rosado JA (2013) Molecular interplay between platelets and the vascular wall in thrombosis and hemostasis. Curr Vasc Pharmacol 11(4):409–430
Alexander P (1951) The macromolecular structure of keratin fibers. J R Soc Med 44(5):389–392. https://doi.org/10.1177/003591575104400510
Apel PJ, Garrett JP, Sierpinski P, Ma JJ, Atala A, Smith TL, Koman A, Van Dyke ME (2008) Peripheral nerve regeneration using a keratin-based scaffold: long-term functional and histological outcomes in a mouse model. J Hand Surg-Am 33A(9):1541–1547. https://doi.org/10.1016/j.jhsa.2008.05.034
Barba C, Marti M, Roddick-Lanzilotta A, Manich A, Carilla J, Parra J, Coderch L (2011) Water sorption of nails treated with wool keratin proteins and peptides. J Therm Anal Calorim 104(1):323–329. https://doi.org/10.1007/s10973-010-1209-7
Barone JR, Schmidt WF (2006) Effect of formic acid exposure on keratin fiber derived from poultry feather biomass. Bioresource Technol 97(2):233–242. https://doi.org/10.1016/j.biortech.2005.02.039
Bertini F, Canetti M, Patrucco A, Zoccola M (2013) Wool keratin-polypropylene composites: properties and thermal degradation. Polym Degrad Stab 98(5):980–987. https://doi.org/10.1016/j.polymdegradstab.2013.02.011
Bhari R, Kaur M, Singh RS (2019) Thermostable and halotolerant keratinase from Bacillus aerius NSMk2 with remarkable dehairing and laundary applications. J Basic Microbiol 59(6):555–568. https://doi.org/10.1002/jobm.201900001
Bloise N, Patrucco A, Bruni G, Montagna G, Caringella R, Fassina L, Tonin C, Visai L (2020) In vitro production of calcified bone matrix onto wool keratin scaffolds via osteogenic factors and electromagnetic stimulus. Materials 13(14):21. https://doi.org/10.3390/ma13143052
Borrelli M, Reichl S, Feng YQ, Schargus M, Schrader S, Geerling G (2013) In vitro characterization and ex vivo surgical evaluation of human hair keratin films in ocular surface reconstruction after sterilization processing. J Mater Sci-Mater M 24(1):221–230. https://doi.org/10.1007/s10856-012-4774-4
Borrelli M, Joepen N, Reich S, Finis D, Schoppe M, Geerling G, Schrader S (2015) Keratin films for ocular surface reconstruction: evaluation of biocompatibility in an in-vivo model. Biomaterials 42:112–120. https://doi.org/10.1016/j.biomaterials.2014.11.038
Burnett LR, Rahmany MB, Richter JR, Aboushwareb TA, Eberli D, Ward CL, Orlando G, Hantgan RR, Van Dyke ME (2013) Hemostatic properties and the role of cell receptor recognition in human hair keratin protein hydrogels. Biomaterials 34(11):2632–2640. https://doi.org/10.1016/j.biomaterials.2012.12.022
Cal F, Arslan TS, Derkus B, Kiran F, Cengiz U, Arslan YE (2021) Synthesis of silica-based boron-incorporated collagen/human hair keratin hybrid cryogels with the potential bone formation capability. ACS Appl Bio Mater 4(9):7266–7279. https://doi.org/10.1021/acsabm.1c00805
Cao Y, Yao YQ, Li Y, Yang XX, Cao ZJ, Yang G (2019) Tunable keratin hydrogel based on disulfide shuffling strategy for drug delivery and tissue engineering. J Colloid Interface Sci 544:121–129. https://doi.org/10.1016/j.jcis.2019.02.049
Carvalho CR, Costa JB, Costa L, Silva-Correia J, Moay ZK, Ng KW, Reis RL, Oliveira JM (2019) Enhanced performance of chitosan/keratin membranes with potential application in peripheral nerve repair. Biomater Sci 7(12):5451–5466. https://doi.org/10.1039/c9bm01098j
Chahal S, Kumar A, Hussian FSJ (2019) Development of biomimetic electrospun polymeric biomaterials for bone tissue engineering. A Review J Biomat Sci-Polym E 30(14):1308–1355. https://doi.org/10.1080/09205063.2019.1630699
Chen Y, Li Y, Yang X, Cao Z, Nie H, Bian Y, Yang G (2021) Glucose-triggered in situ forming keratin hydrogel for the treatment of diabetic wounds. Acta Biomater. https://doi.org/10.1016/j.actbio.2021.02.035
Cheon YW, Lee WJ, Baek HS, Lee YD, Park JC, Park YH, Ki CS, Chung KH, Rah DK (2010) Enhanced chondrogenic responses of human articular chondrocytes onto silk fibroin/wool keratose scaffolds treated with microwave-induced argon plasma. Artif Organs 34(5):384–392. https://doi.org/10.1111/j.1525-1594.2009.00871.x
Church JS, Poole AJ, Woodhead AL (2010) The Raman analysis of films cast from dissolved feather keratin. Vib Spectrosc 53(1):107–111. https://doi.org/10.1016/j.vibspec.2010.02.011
Cohen DJ, Hyzy SL, Haque S, Olson LC, Boyan BD, Saul JM, Schwartz Z (2018) Effects of tunable keratin hydrogel erosion on recombinant human bone morphogenetic protein 2 release, bioactivity, and bone induction. Tissue Eng Pt A 24(21–22):1616–1630. https://doi.org/10.1089/ten.tea.2017.0471
Daroit DJ, Brandelli A (2014) A current assessment on the production of bacterial keratinases. Crit Rev Biotechnol 34(4):372–384. https://doi.org/10.3109/07388551.2013.794768
de Medeiros IP, Rozental S, Costa AS, Macrae A, Hagler AN, Ribeiro JRA, Vermelho AB (2016) Biodegradation of keratin by Trichosporum loubieri RC-S6 isolated from tannery/leather waste. Int Biodeterior Biodegrad 115:199–204. https://doi.org/10.1016/j.ibiod.2016.08.006
Du JS, Wu Q, Li YM, Liu PC, Han X, Wang LJ, Yuan J, Meng XW, Xiao YH (2020) Preparation and characterization of keratin-PEG conjugate-based micelles as a tumor microenvironment-responsive drug delivery system. J Biomater Sci Polym Ed 31(9):1163–1178. https://doi.org/10.1080/09205063.2020.1747044
Du JS, Wang LJ, Han X, Dou J, Jiang XF, Yuan J (2021) Polydopamine/keratin complexes as gatekeepers of mesoporous silica nanoparticles for pH and GSH dual responsive drug delivery. Mater Lett 293:4. https://doi.org/10.1016/j.matlet.2021.129676
Eslahi N, Dadashian F, Nejad NH (2013) An investigation on keratin extraction from wool and feather waste by enzymatic hydrolysis. Prep Biochem BiotechInol 43(7):624–648. https://doi.org/10.1080/10826068.2013.763826
Eslahi N, Simchi A, Mehrjoo M, Shokrgozar MA, Bonakdar S (2016) Hybrid cross-linked hydrogels based on fibrous protein/block copolymers and layered silicate nanoparticles: tunable thermosensitivity, biodegradability and mechanical durability. RSC Adv 6(67):62944–62957. https://doi.org/10.1039/c6ra08563f
Esparza Y, Ullah A, Wu JP (2018) Molecular mechanism and characterization of self-assembly of feather keratin gelation. Int J Biol Macromol 107:290–296. https://doi.org/10.1016/j.ijbiomac.2017.08.168
Fang Z, Zhang J, Du GC, Chen J (2017) Rational protein engineering approaches to further improve the keratinolytic activity and thermostability of engineered keratinase KerSMD. Biochem Eng J 127:147–153. https://doi.org/10.1016/j.bej.2017.08.010
Feroz S, Dias G (2021) Hydroxypropylmethyl cellulose (HPMC) crosslinked keratin/hydroxyapatite (HA) scaffold fabrication, characterization and in vitro biocompatibility assessment as a bone graft for alveolar bone regeneration. Heliyon 7(11):10. https://doi.org/10.1016/j.heliyon.2021.e08294
Gao F, Li W, Deng J, Kan J, Guo T, Wang B, Hao S (2019a) Recombinant human hair keratin nanoparticles accelerate dermal wound healing. Acs Appl Mater Interfaces 11(20):18681–18690. https://doi.org/10.1021/acsami.9b01725
Gao JY, Zhang L, Wei YS, Chen TY, Ji XY, Ye K, Yu JH, Tang B, Sun XC, Hu JB (2019b) Human hair keratins promote the regeneration of peripheral nerves in a rat sciatic nerve crush model. J Mater Sci-Mater M 30(7) https://doi.org/10.1007/s10856-019-6283-1
Gobel K, Eichler S, Wiendl H, Chavakis T, Kleinschnitz C, Meuth SG (2018) The coagulation factors fibrinogen, thrombin, and factor XII in inflammatory disorders - a systematic review. Front Immunol 9:14. https://doi.org/10.3389/fimmu.2018.01731
Gong JS, Ye JP, Tao LY, Su C, Qin J, Zhang YY, Li H, Li H, Xu ZH, Shi JS (2020a) Efficient keratinase expression via promoter engineering strategies for degradation of feather wastes. Enzyme Microb Technol 137.https://doi.org/10.1016/j.enzmictec.2020a.109550
Gong XY, Dang GY, Guo J, Liu YF, Gong YM (2020b) A sodium alginate/feather keratin composite fiber with skin-core structure as the carrier for sustained drug release. Int J Biol Macromol 155:386–392. https://doi.org/10.1016/j.ijbiomac.2020.03.224
Hassan MA, Taha TH, Hamad GM, Hashem M, Alamri S, Mostafa YS (2020) Biochemical characterisation and application of keratinase from Bacillus thuringiensis MT1 to enable valorisation of hair wastes through biosynthesis of vitamin B-complex. Int J Biol Macromol 153:561–572. https://doi.org/10.1016/j.ijbiomac.2020.03.032
He Y, Qu Q, Luo TT, Gong YH, Hou ZK, Deng J, Xu YQ, Wang BC, Hao SL (2019) Human hair keratin hydrogels alleviate rebleeding after intracerebral hemorrhage in a rat model. ACS Biomater Sci Eng 5(2):1113–1122. https://doi.org/10.1021/acsbiomaterials.8b01609
He JH, Xu D, Li JY, Li LF, Li WB, Cui WG, Liu KS (2020) Highly efficient extraction of large molecular-weight keratin from wool in a water/ethanol co-solvent. Text Res J 90(9–10):1084–1093. https://doi.org/10.1177/0040517519885022
Idris A, Vijayaraghavan R, Rana UA, Fredericks D, Patti AF, MacFarlane DR (2013) Dissolution of feather keratin in ionic liquids. Green Chem 15(2):525–534. https://doi.org/10.1039/c2gc36556a
Ji YM, Chen JY, Lv JX, Li ZL, Xing LY, Ding SY (2014) Extraction of keratin with ionic liquids from poultry feather. Sep Purif Technol 132:577–583. https://doi.org/10.1016/j.seppur.2014.05.049
Jiang SQ, Zhang L, Wu H, Chi G (2017) Study on effective extraction of keratin from human hair wastes. Integr Ferroelectr 180(1):102–107. https://doi.org/10.1080/10584587.2017.1338506
Jull A, Wadham A, Bullen C, Parag V, Waters J (2018) Wool-derived keratin dressings versus usual care dressings for treatment of slow-healing venous leg ulceration: study protocol for a randomised controlled trial (Keratin4VLU). BMJ Open 8(2):e020319. https://doi.org/10.1136/bmjopen-2017-020319
Jung SJ, Pant B, Climans M, Shaw GC, Lee EJ, Kim N, Park M (2021) Transformation of electrospun keratin/PVA nanofiber membranes into multilayered 3D scaffolds: physiochemical studies and corneal implant applications. Int J Pharmaceut 610.https://doi.org/10.1016/j.ijpharm.2021.121228
Karthikeyan R, Balaji S, Chandrababu NK, Sehgal PK (2008) Horn meal hydrolysate-chromium complex as a high exhaust chrome tanning agent-pilot scale studies. Clean Technol Environ Policy 10(3):295–301. https://doi.org/10.1007/s10098-007-0119-2
Katoh K, Tanabe T, Yamauchi K (2004) Novel approach to fabricate keratin sponge scaffolds with controlled pore size and porosity. Biomaterials 25(18):4255–4262. https://doi.org/10.1016/j.biomaterials.2003.11.018
Khoshnevis N, Rezaei S, Forootanfar H, Faramarzi MA (2019) Efficient keratinolysis of poultry feather waste by the halotolerant KERATINASE from Salicola Marasensis. Iran J Pharm Res 18(4):1862–1870. https://doi.org/10.22037/ijpr.2019.111710.13312
Kim BS, Park KE, Park WH, Lee J (2013) Fabrication of nanofibrous scaffold using a PLA and hagfish thread keratin composite; its effect on cell adherence, growth, and osteoblast differentiation. Biomed Mater 8(4):9. https://doi.org/10.1088/1748-6041/8/4/045006
Kim SY, Park BJ, Lee Y, Park NJ, Park KM, Hwang Y-S, Park KD (2019) Human hair keratin-based hydrogels as dynamic matrices for facilitating wound healing. J Ind Eng Chem 73:142–151. https://doi.org/10.1016/j.jiec.2019.01.017
Konop M, Czuwara J, Klodzinska E, Laskowska AK, Sulejczak D, Damps T, Zielenkiewicz U, Brzozowska I, Sureda A, Kowalkowski T, Schwartz RA, Rudnicka L (2020) Evaluation of keratin biomaterial containing silver nanoparticles as a potential wound dressing in full-thickness skin wound model in diabetic mice. J Tissue Eng Regener Med 14(2):334–346. https://doi.org/10.1002/term.2998
Koupenova M, Clancy L, Corkrey HA, Freedman JE (2018) Circulating platelets as mediators of immunity, inflammation, and thrombosis. Circ Res 122(2):337–351. https://doi.org/10.1161/circresaha.117.310795
Lee H, Hwang YS, Lee HS, Choi S, Kim SY, Moon JH, Kim JH, Kim KC, Han DW, Park HJ, Bae H (2015) Human hair keratin-based biofilm for potent application to periodontal tissue regeneration. Macromol Res 23(3):300–308. https://doi.org/10.1007/s13233-015-3036-y
Li QX (2019) Progress in microbial degradation of feather waste. Front Microbiol 10.https://doi.org/10.3389/fmicb.2019.02717
Li M, Jin E, Zhang L (2016a) Effects of graft modification on the water solubility, apparent viscosity, and adhesion of feather keratin for warp sizing. J Text Inst 107(3):395–404. https://doi.org/10.1080/00405000.2015.1034931
Li YM, Wang YF, Ye JJ, Yuan J, Xiao YH (2016b) Fabrication of poly(epsilon-caprolactone)/keratin nanofibrous mats as a potential scaffold for vascular tissue engineering. Mater Sci Eng C 68:177–183. https://doi.org/10.1016/j.msec.2016.05.117
Li Y, Zhi X, Lin J, You X, Yuan J (2017) Preparation and characterization of DOX loaded keratin nanoparticles for pH/GSH dual responsive release. Mater Sci Eng C 73:189–197. https://doi.org/10.1016/j.msec.2016.12.067
Li Y, Song K, Cao Y, Peng C, Yang G (2018) Keratin-templated synthesis of metallic oxide nanoparticles as MRI contrast agents and drug carriers. ACS Appl Mater Interfaces 10(31):26039–26045. https://doi.org/10.1021/acsami.8b08555
Li Q-F, He Y, Wang R-M (2019a) A facile extraction of keratin from pig hair and its properties. Biologia 74(5):563–571. https://doi.org/10.2478/s11756-019-00210-5
Li WF, Gao FY, Kan JL, Deng J, Wang BC, Hao SL (2019b) Synthesis and fabrication of a keratin-conjugated insulin hydrogel for the enhancement of wound healing. Colloids Surf b: Biointerfaces 175:436–444. https://doi.org/10.1016/j.colsurfb.2018.12.020
Lin YC, Ramadan M, Van Dyke M, Kokai LE, Philips BJ, Rubin JP, Marra KG (2012) Keratin gel filler for peripheral nerve repair in a rodent sciatic nerve injury model. Plast Reconstr Surg 129(1):67–78. https://doi.org/10.1097/PRS.0b013e3182268ae0
Lin CW, Chen YK, Tang KC, Yang KC, Cheng NC, Yu J (2019) Keratin scaffolds with human adipose stem cells: physical and biological effects toward wound healing. J Tissue Eng Regen M 13:1044–1058. https://doi.org/10.1002/term.2855
Liu PC, Wu Q, Li YM, Li PF, Yuan J, Meng XW, Xiao YH (2019) DOX-conjugated keratin nanoparticles for pH-sensitive drug delivery. Colloids Surf b: Biointerfaces 181:1012–1018. https://doi.org/10.1016/j.colsurfb.2019.06.057
Luo TT, Hao SL, Chen XL, Wang J, Yang Q, Wang YZ, Weng YL, Wei HM, Zhou J, Wang BC (2016) Development and assessment of kerateine nanoparticles for use as a hemostatic agent. Mater Sci Eng, C 63:352–358. https://doi.org/10.1016/j.msec.2016.03.007
Lv XG, Li Z, Chen SY, Xie MK, Huang JW, Peng XF, Yang RX, Wang HP, Xu YM, Feng C (2016) Structural and functional evaluation of oxygenating keratin/silk fibroin scaffold and initial assessment of their potential for urethral tissue engineering. Biomaterials 84:99–110. https://doi.org/10.1016/j.biomaterials.2016.01.032
Malik A, Rehman FU, Shah KU, Naz SS, Qaisar S (2021) Hemostatic strategies for uncontrolled bleeding: a comprehensive update. J Biomed Mater Res B:1–13. https://doi.org/10.1002/jbm.b.34806
Mo R, Gu Z (2016) Tumor microenvironment and intracellular signal-activated nanomaterials for anticancer drug delivery. Mater Today 19(5):274–283. https://doi.org/10.1016/j.mattod.2015.11.025
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. https://doi.org/10.1111/jocd.12319
Navarro J, Swayambunathan J, Lerman M, Santoro M, Fisher JP (2019) Development of keratin-based membranes for potential use in skin repair. Acta Biomater 83:177–188. https://doi.org/10.1016/j.actbio.2018.10.025
Navone L, Moffitt K, Hansen KA, Blinco J, Payne A, Speight R (2020) Closing the textile loop: enzymatic fibre separation and recycling of wool/polyester fabric blends. Waste Manage 102:149–160. https://doi.org/10.1016/j.wasman.2019.10.026
Nunez F, Trach S, Burnett L, Handa R, Van Dyke M, Callahan M, Smith T (2011) Vasoactive properties of keratin-derived compounds. Microcirculation 18(8):663–669. https://doi.org/10.1111/j.1549-8719.2011.00135.x
Pace LA, Plate JF, Smith TL, Van Dyke ME (2013) The effect of human hair keratin hydrogel on early cellular response to sciatic nerve injury in a rat model. Biomaterials 34(24):5907–5914. https://doi.org/10.1016/j.biomaterials.2013.04.024
Pace LA, Plate JF, Mannava S, Barnwell JC, Koman LA, Li ZY, Smith TL, Van Dyke M (2014) A human hair keratin hydrogel scaffold enhances median nerve regeneration in nonhuman primates: an electrophysiological and histological study. Tissue Eng Pt A 20(3–4):507–517
Papadopoulos M, Boushy AE, Roodbeen A, Ketelaars E (1986) Effects of processing time and moisture content on amino acid composition and nitrogen characteristics of feather meal. Anim Feed Sci Technol 14(3–4):279–290
Park M, Kim B-S, Shin HK, Park S-J, Kim H-Y (2013) Preparation and characterization of keratin-based biocomposite hydrogels prepared by electron beam irradiation. Mater Sci Eng, C 33(8):5051–5057. https://doi.org/10.1016/j.msec.2013.08.032
Park M, Shin HK, Kim B-S, Kim MJ, Kim I-S, Park B-Y, Kim H-Y (2015) Effect of discarded keratin-based biocomposite hydrogels on the wound healing process in vivo. Mater Sci Eng, C 55:88–94. https://doi.org/10.1016/j.msec.2015.03.033
Peng Z, Xu P, Song Y, Du GC, Zhang J, Chen J (2021) Cysteine-mediated cyclic metabolism drives the microbial degradation of keratin. ACS Sustainable Chem Eng 9(29):9861–9870. https://doi.org/10.1021/acssuschemeng.1c02627
Periayah MH, Halim AS, Mat Saad AZ (2017) Mechanism action of platelets and crucial blood coagulation pathways in hemostasiS. Int J of Hematol-Oncol and Stem Cell Res 11(4):319–327
Polari L, Alam CM, Nystrom JH, Heikkila T, Tayyab M, Baghestani S, Toivola DM (2020) Keratin intermediate filaments in the colon: guardians of epithelial homeostasis. Int J Biochem Cell Biol 129:105878. https://doi.org/10.1016/j.biocel.2020.105878
Poongodi R, Chen Y-L, Yang T-H, Huang Y-H, Yang KD, Lin H-C, Cheng J-K (2021) Bio-scaffolds as cell or exosome carriers for nerve injury repair. Int J Mol Sci 22(24). https://doi.org/10.3390/ijms222413347
Rahmany MB, Hantgan RR, Van Dyke M (2013) A mechanistic investigation of the effect of keratin-based hemostatic agents on coagulation. Biomaterials 34(10):2492–2500. https://doi.org/10.1016/j.biomaterials.2012.12.008
Rajabinejad H, Zoccola M, Patrucco A, Montarsolo A, Rovero G, Tonin C (2018) Physicochemical properties of keratin extracted from wool by various methods. Text Res J 88(21):2415–2424. https://doi.org/10.1177/0040517517723028
Ramya KR, Thangam R, Madhan B (2020) Comparative analysis of the chemical treatments used in keratin extraction from red sheep’s hair and the cell viability evaluations of this keratin for tissue engineering applications. Process Biochem 90:223–232. https://doi.org/10.1016/j.procbio.2019.11.015
Ranjit E, Hamlet S, George R, Sharma A, Love R (2021) Biofunctional approaches of wool-based keratin for tissue engineering. J Sci-Adv Mater Dev 7(1):1–12. https://doi.org/10.1016/j.jsamd.2021.10.001
Reichl S (2009) Films based on human hair keratin as substrates for cell culture and tissue engineering. Biomaterials 30(36):6854–6866. https://doi.org/10.1016/j.biomaterials.2009.08.051
Rousselle P, Braye F, Dayan G (2019) Re-epithelialization of adult skin wounds: cellular mechanisms and therapeutic strategies. Adv Drug Delivery Rev 146:344–365. https://doi.org/10.1016/j.addr.2018.06.019
Ruffin P, Andrieu S, Biserte G, Biguet J (1976) Sulphitolysis in keratinolysis. Biochemical Proof J Med Vet Mycol 14(2):181–184
Sabouraudia JK (1972) Keratin decomposition by dermatophytes: evidence of the sulphitolysis of the protein. Experientia 28(9):1025–1026
Saravanan S, Sameera DK, Moorthi A, Selvamurugan N (2013) Chitosan scaffolds containing chicken feather keratin nanoparticles for bone tissue engineering. Int J Biol Macromol 62:481–486. https://doi.org/10.1016/j.ijbiomac.2013.09.034
Schrooyen PMM, Dijkstra PJ, Oberthur RC, Bantjes A, Feijen J (2001) Stabilization of solutions of feather keratins by sodium dodecyl sulfate. J Colloid Interface Sci 240(1):30–39. https://doi.org/10.1006/jcis.2001.7673
Shanmugasundaram OL, Syed Zameer Ahmed K, Sujatha K, Ponnmurugan P, Srivastava A, Ramesh R, Sukumar R, Elanithi K (2018) Fabrication and characterization of chicken feather keratin/polysaccharides blended polymer coated nonwoven dressing materials for wound healing applications. Mater Sci Eng, C 92:26–33. https://doi.org/10.1016/j.msec.2018.06.020
Sharma LM, Love RM, Ali MA, Sharma A, Macari S, Avadhani A, Dias GJ (2017) Healing response of rat pulp treated with an injectable keratin hydrogel. J Appl Biomater Funct Mater 15(3):e244–e250. https://doi.org/10.5301/jabfm.5000346
Shavandi A, Carne A, Bekhit AA, Bekhit AEA (2017) An improved method for solubilisation of wool keratin using peracetic acid. J Environ Chem Eng 5(2):1977–1984. https://doi.org/10.1016/j.jece.2017.03.043
Sierpinski P, Garrett J, Ma J, Apel P, Klorig D, Smith T, Koman LA, Atala A, Van Dyke M (2008) The use of keratin biomaterials derived from human hair for the promotion of rapid regeneration of peripheral nerves. Biomaterials 29(1):118–128. https://doi.org/10.1016/j.biomaterials.2007.08.023
Singaravelu S, Ramanathan G, Muthukumar T, Raja MD, Nagiah N, Thyagarajan S, Aravinthan A, Gunasekaran P, Natarajan TS, Selva GVNG, Kim J-H, Sivagnanam UT (2016) Durable keratin-based bilayered electrospun mats for wound closure. J Mater Chem B 4(22):3982–3997. https://doi.org/10.1039/c6tb00720a
Singh R, Sarker B, Silva R, Detsch R, Dietel B, Alexiou C, Boccaccini AR, Cicha I (2016) Evaluation of hydrogel matrices for vessel bioplotting: vascular cell growth and viability. J Biomed Mater Res A 104(3):577–585. https://doi.org/10.1002/jbm.a.35590
Sinkiewicz I, Śliwińska A, Staroszczyk H, Kołodziejska I (2016) Alternative methods of preparation of soluble keratin from chicken feathers. Waste Biomass Valorization 8(4):1043–1048. https://doi.org/10.1007/s12649-016-9678-y
Song KL, Qian XN, Zhu XJ, Li XY, Hong XH (2020) Fabrication of mechanical robust keratin film by mesoscopic molecular network reconstruction and its performance for dye removal. J Colloid Interface Sci 579:28–36. https://doi.org/10.1016/j.jcis.2020.06.026
Su C, Gong JS, Qin JF, Li H, Li H, Xu ZH, Shi JS (2020a) The tale of a versatile enzyme: molecular insights into keratinase for its industrial dissemination. Biotechnol Adv 45.https://doi.org/10.1016/j.biotechadv.2020a.107655
Su C, Gong JS, Ye JP, He JM, Li RY, Jiang M, Geng Y, Zhang Y, Chen JH, Xu ZH, Shi JS (2020b) Enzymatic extraction of bioactive and self-assembling wool keratin for biomedical applications. Macromol Biosci 20(9):1–11. https://doi.org/10.1002/mabi.202000073
Su S, Bedir T, Kalkandelen C, Basar AO, Sasmazel HT, Ustundag CB, Sengor M, Gunduz O (2021) Coaxial and emulsion electrospinning of extracted hyaluronic acid and keratin based nanofibers for wound healing applications. Eur Polym J 142. https://doi.org/10.1016/j.eurpolymj.2020.110158
Sun Z, Chen XY, Ma XM, Cui XX, Yi Z, Li XD (2018) Cellulose/keratin-catechin nanocomposite hydrogel for wound hemostasis. J Mater Chem B 6(38):6133–6141. https://doi.org/10.1039/c8tb01109e
Tasaki K (2020) A novel thermal hydrolysis process for extraction of keratin from hog hair for commercial applications. Waste Manage 104:33–41. https://doi.org/10.1016/j.wasman.2019.12.042
Tian YK, Wu QT, Li F, Zhou YH, Huang D, Xie RJ, Wang XQ, Zheng ZZ, Li G (2021) A flexible and biocompatible bombyx mori silk fibroin/wool keratin composite scaffold with interconnective porous structure. Colloid Surf b: Biointerfaces 208:11. https://doi.org/10.1016/j.colsurfb.2021.112080
Valeika V, Sirvaityte J, Bridziuviene D, Svediene J (2019) An application of advanced hair-save processes in leather industry as the reason of formation of keratinous waste: few peculiarities of its utilisation. Environ Sci Pollut Res 26(6):6223–6233. https://doi.org/10.1007/s11356-019-04142-0
Vazquez N, Chacon M, Meana A, Menendez-Menendez Y, Ferrero-Gutierrez A, Cereijo-Martin D, Naveiras M, Merayo-Lloves J (2015) Keratin-chitosan membranes as scaffold for tissue engineering of human cornea. Histol Histopathol 30(7):813–821 https://doi.org/10.1467/0hh-11-585
Villanueva ME, Cuestas ML, Perez CJ, Campo Dall Orto V, Copello GJ (2019) Smart release of antimicrobial ZnO nanoplates from a pH-responsive keratin hydrogel. J Colloid Interface Sci 536:372–380. https://doi.org/10.1016/j.jcis.2018.10.067
Wang YX, Cao XJ (2012) Extracting keratin from chicken feathers by using a hydrophobic ionic liquid. Process Biochem 47(5):896–899. https://doi.org/10.1016/j.procbio.2012.02.013
Wang B, Yang W, McKittrick J, Meyers MA (2016a) Keratin: structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration. Prog Mater Sci 76:229–318. https://doi.org/10.1016/j.pmatsci.2015.06.001
Wang J, Hao S, Luo T, Yang Q, Wang B (2016b) Development of feather keratin nanoparticles and investigation of their hemostatic efficacy. Mater Sci Eng, C 68:768–773. https://doi.org/10.1016/j.msec.2016.07.035
Wang J, Hao S, Luo T, Cheng Z, Li W, Gao F, Guo T, Gong Y, Wang B (2017) Feather keratin hydrogel for wound repair: preparation, healing effect and biocompatibility evaluation. Colloids Surf b: Biointerfaces 149:341–350. https://doi.org/10.1016/j.colsurfb.2016.10.038
Wang D, Li WF, Wang YM, Yin HM, Ding Y, Ji JG, Wang BC, Hao SL (2019) Fabrication of an expandable keratin sponge for improved hemostasis in a penetrating trauma. Colloids Surf b: Biointerfaces 182:9. https://doi.org/10.1016/j.colsurfb.2019.110367
Wang XQ, Shi ZM, Zhao QL, Yun Y (2021) Study on the structure and properties of biofunctional keratin from rabbit hair. Materials 14(2):15. https://doi.org/10.3390/ma14020379
Wei W, Youbo D, Zhou Z, Xing W, Chunli Q, Libin G (2019) Preparation and characterization of protein/viscose fiber and its action in self-heating. J Appl Polym Sci 136(10). https://doi.org/10.1002/app.47146
Williams R, Lace R, Kennedy S, Doherty K, Levis H (2018) Biomaterials for regenerative medicine approaches for the anterior segment of the eye. Adv Healthc Mater 7(10). https://doi.org/10.1002/adhm.201701328
Xu S, Sang L, Zhang Y, Wang X, Li X (2013) Biological evaluation of human hair keratin scaffolds for skin wound repair and regeneration. Mater Sci Eng, C 33(2):648–655. https://doi.org/10.1016/j.msec.2012.10.011
Yang KC, Huang LP, Huang MC, Thyparambil AA, Wei Y (2020) Effect of thermal treatments on the structural change and the hemostatic property of hair extracted proteins. Colloids Surf b: Biointerfaces 190:7. https://doi.org/10.1016/j.colsurfb.2020.110951
Ye J-P, Gong J-S, Su C, Liu Y-G, Jiang M, Pan H, Li R-Y, Geng Y, Xu Z-H, Shi J-S (2020) Fabrication and characterization of high molecular keratin based nanofibrous membranes for wound healing. Colloids Surf b: Biointerfaces 194:111158. https://doi.org/10.1016/j.colsurfb.2020.111158
Yin X, Li F-Y, He Y-F, Yan W, Rong-Min. W (2013) Study on effective extraction of chicken feather keratins and their films for controlling drug release. Biomater Sci:528–536 https://doi.org/10.1039/c3bm00158j
Zhang HL, Liu JS (2013) Electrospun poly(lactic-co-glycolic acid)/wool keratin fibrous composite scaffolds potential for bone tissue engineering applications. J Bioact Compat Pol 28(2):141–153. https://doi.org/10.1177/0883911512472565
Zhang H, Liu P (2019) Bio-inspired keratin-based core-crosslinked micelles for pH and reduction dual-responsive triggered DOX delivery. Int J Biol Macromol 123:1150–1156. https://doi.org/10.1016/j.ijbiomac.2018.11.178
Zhang H, Pei M, Liu P (2019) Keratin-based drug-protein conjugate with acid-labile and reduction-cleavable linkages in series for tumor intracellular DOX delivery. J Ind Eng Chem 80:739–748. https://doi.org/10.1016/j.jiec.2019.05.041
Zhang YF, Tu H, Wu RH, Patil A, Hou C, Lin ZF, Meng ZH, Ma LY, Yu R, Yu WD, Liu XY (2020) Programing performance of silk fibroin superstrong scaffolds by mesoscopic regulation among hierarchical structures. Biomacromol 21(10):4169–4179. https://doi.org/10.1021/acs.biomac.0c00981
Zhao W, Yang RJ, Zhang YQ, Wu L (2012) Sustainable and practical utilization of feather keratin by an innovative physicochemical pretreatment: high density steam flash-explosion. Green Chem 14(12):3352–3360. https://doi.org/10.1039/c2gc36243k
Zhao XX, Lui YS, Choo CKC, Sow WT, Huang CL, Ng KW, Tan LP, Loo JSC (2015) Calcium phosphate coated Keratin-PCL scaffolds for potential bone tissue regeneration. Mat Sci Eng C-Mater 49:746–753. https://doi.org/10.1016/j.msec.2015.01.084
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This work was supported by the National Key Research and Development Program of China (No. 2021YFC2100400), the National Natural Science Foundation of China (No. 21978116), the Fundamental Research Funds for the Central Universities (No. JUSRP22047), and the Ningxia Hui Autonomous Region Key Research & Development Plan (No. 2019BCH01002).
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RRY and JSG conceived this review. RRY, CS, YLL, and JYQ collected all references. RRY wrote the manuscript draft. JSG, ZHX, and JSS edited the manuscript. All the authors read and approved the manuscript.
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Yan, RR., Gong, JS., Su, C. et al. Preparation and applications of keratin biomaterials from natural keratin wastes. Appl Microbiol Biotechnol 106, 2349–2366 (2022). https://doi.org/10.1007/s00253-022-11882-6
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DOI: https://doi.org/10.1007/s00253-022-11882-6