Keratins extracted from Merino wool and Brown Alpaca fibres as potential fillers for PLLA-based biocomposites
Source abstract
Abstract
This paper reports on the promising perspectives of using keratins extracted by sulphitolysis reaction from Merino wool (KM) and Brown Alpaca fibres (KA) in poly (l-lactide) (PLLA)-based biomaterials. Both types of keratin were dispersed in chloroform (CHCl3) and tetrahydrofuran (THF), and optimisation of dispersion methods and parameters using the two selected solvents was considered. The extraction yield, as well as supermolecular structures, morphology and thermal behaviour of the two proteins before and after the regeneration in CHCl3 was investigated. The results indicated that the supermolecular structures and thermal behaviour of the two proteins were affected by the interaction with CHCl3, producing decrease of the amount of α-helix structures in KM and an increase for KA, a slight decrease of β-sheet structures and a reduced thermal stability of α-crystallites for both keratins. Biocomposite films based on PLLA polymer matrix and two different contents of Merino wool and Brown Alpaca keratins (1 % and 5 % wt) were successfully developed by solvent casting in chloroform and the resulting morphologies after incorporation of different keratins (as a function of content and source) give evidence of different surface topographies, with a random distribution of keratin in flask-like structure. PLLA/5KA and PLLA/5KM samples with 1 % and 5 % wt of keratins show a specific pore-like surface microstructure, induced by solvent evaporation.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Dyeing and Modifying Textile Fibers · Silk-based biomaterials and applications · Textile materials and evaluations
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (45)
Show source-provided references
1. Dowling LM, Crewther WG, Parry DAD (1986) Secondary structure of component 8c-1 of a-keratin: analysis of the amino acid sequence. Biochem J 236(3):705–71210.1042/bj2360705 ↗
2. Lv L, Yu Y, Zhou J (2010) Establishment of data base of evaluation system on recycling of waste textile fiber material. Tekstil 59(5):201–207
3. Barone JR (2009) Lignocellulosic fibre-reinforced Keratin polymer composites. J Polym Environ 17(2):143–15110.1007/s10924-009-0131-1 ↗
4. Li J, Li Y, Li L, Mak AFT, Ko F, Qin L (2009) Fabrication and degradation of poly (l-lactic acid) scaffolds with wool keratin. Compos B 40:664–66710.1016/j.compositesb.2009.04.012 ↗
5. Williams GI, Wool RP (2000) Composites from natural fibers and soy oil resins. Appl Compos Mater 7:421–43210.1023/A:1026583404899 ↗
6. Thielemans W, Can E, Morye SS, Wool RP (2002) Novel applications of lignin in composite materials. J Appl Polym Sci 83(2):323–33110.1002/app.2247 ↗
7. Gupta AP, Kumar V (2007) New emerging trends in synthetic biodegradable polymers–Polylactide: a critique. Eur Polym J 43(10):4053–407410.1016/j.eurpolymj.2007.06.045 ↗
8. Cai Q, Yang JA, Bei JZ, Wang SG (2002) A novel porous cells scaffold made of polylactide-dextran blend by combining phase-separation and particle-leaching techniques. Biomaterials 23(23):4483–449210.1016/S0142-9612(02)00168-0 ↗
9. Armentano I, Bitinis N, Fortunati E, Mattioli S, Rescignano N, Verdejo R, Lopez-Manchado MA, Kenny JM (2013) Multifunctional nanostructured PLA materials for packaging and tissue engineering. Prog Polym Sci 38(10–11):1720–174710.1016/j.progpolymsci.2013.05.010 ↗
10. Suh H, Hwang YS, Lee JE, Han CD, Park JC (2001) Behavior of osteoblasts on a type I atelocollagen grafted ozone oxidized poly-l-lactic acid membrane. Biomaterials 22(2):219–23010.1016/S0142-9612(00)00177-0 ↗
11. Quirk AR, Chan WC, Davis MC, Tendler SJB, Shakesheff KM (2001) Poly (l-lysine)–GRGDS as a biomimetic surface modifier for poly (lactic acid). Biomaterials 22:865–86710.1016/S0142-9612(00)00250-7 ↗
12. Li JS, Mak AFT (2007) Transfer of collagen coating from progen to scaffold: collagen coating within poly (DL-lactic-co-glycolic acid) scaffold. Compos B 38:317–32310.1016/j.compositesb.2006.06.009 ↗
13. Zhu H, Feng X, Zhang H, Guo Y, Zhang J, Chen J (2009) Structural characteristics and properties of silk fibroin/poly (lactic acid) blend films. J Biomater Sci Polym Ed 20(9):1259–127410.1163/156856209X452980 ↗
14. Li JS, Li Y, Liu X, Zhang J, Zhang Y (2013) Strategy to introduce an hydroxyapatite-keratin nanocomposite into a fibrous membrane for bone tissue engineering. J Mater Chem B 1:432–43710.1039/C2TB00460G ↗
15. Kim BS, Park KE, Parkand 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. doi: 10.1088/1748-6041/8/4/045006
16. Rouse JG, Van Dyke M (2010) A review of keratin-based biomaterials for biomedical applications. Materials 3:999–101410.3390/ma3020999 ↗
17. Kirsner RS, Cassidy S, Marsh C, Vivas A, Kelly RJ (2012) Use of a keratin-based wound dressing in the management of wounds in a patient with recessive dystrophic epidermolysis bullosa Adv. Skin Wound Care 25:400–40310.1097/01.ASW.0000419404.44947.de ↗
18. Reichl S (2009) Films based on human hair keratin as substrates for cell culture and tissue engineering. Biomaterials 30:6854–686610.1016/j.biomaterials.2009.08.051 ↗
19. Tachibana A, Furuta Y, Takeshima H, Tanabe T, Yamauchi K (2002) Fabrication of wool keratin sponge scaffolds for long-term cell cultivation. J Biotechnol 93:165–17010.1016/S0168-1656(01)00395-9 ↗
20. Aluigi A, Tonetti C, Tonin C, Casasola R, Ferrero F (2012) Wool keratin nanofibres for copper (II) adsorption. J Biobased Mater Bio 6:230–23610.1166/jbmb.2012.1204 ↗
21. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–68510.1038/227680a0 ↗
22. Aluigi A, Zoccola M, Vineis C, Tonin C, Ferrero F, Canetti M (2007) Study on the structure and properties of wool keratin regenerated from formic acid. Int J Biol Macromol 41(3):266–27310.1016/j.ijbiomac.2007.03.002 ↗
23. Wang H, Liu X, Wang X (2005) Internal structure and pigment granules in colored Alpaca fibres. Fibres and Polymers 6(3):263–26810.1007/BF02875652 ↗
24. Cardamone JM, Nuñez A, Garcia RA, Aldema-Ramos M (2009) Characterizing wool keratin. Lett Mater Sci. doi: 10.1155/2009/147175
25. Cardamone JM (2010) Investigating the microstructure of keratin extracted from wool: peptide sequence (MALDI-TOF/TOF) and protein conformation (FTIR). J Mol Struct 969:97–10510.1016/j.molstruc.2010.01.048 ↗
26. Leertouwer HL, Wilts BD, Stavenga DG (2011) Refractive index and dispersion of butterfly scale chitin and bird feather keratin measured by interference microscopy. Opt Express 19:24061–2406610.1364/OE.19.024061 ↗
27. Zoccola M, Aluigi A, Tonin C (2009) Characterisation of keratin biomass from butchery and wool industry wastes. J Mol Struct 938:35–4010.1016/j.molstruc.2009.08.036 ↗
28. Kreplak L, Doucet J, Dumas P, Briki F (2004) New aspect of the α-helix to β-sheet transition in stretched hard α-keratin fibers. Biophys J 87:640–64710.1529/biophysj.103.036749 ↗
29. Erra P, Gomez N, Dolcet LM, Juliá MR, Lewis DM, Willoughby JH (1997) FTIR analysis to study chemical changes in wool following a sulfitolysis treatment. Text Res J 67(6):397–40110.1177/004051759706700602 ↗
30. Wetzel DL, Srivan P, Finney JR (2003) Revealing protein infrared spectral detail in a heterogeneous matrix dominated by starch. Vib Spectrosc 31:109–11410.1016/S0924-2031(02)00100-5 ↗
31. Pelton JT, McLean LR (2000) Spectroscopic Methods for Analysis of Protein Secondary Structure. Anal Biochem 277:167–17610.1006/abio.1999.4320 ↗
32. Vasconcelos A, Freddi G, Cavaco-Paulo A (2008) Biodegradable materials based on silk fibroin and keratin. Biomacromolecules 9:1299–130510.1021/bm7012789 ↗
33. Schmidt WF, Jayasundera S (2003) “Microcrystalline Keratin Fiber,”. In: Wallenberger F, Weston N (eds) Natural fibers plastics and composites–recent advances. Kluwer Academic Publishers, Norwell
34. Milczarek P, Zielinski M, Garcia ML (1992) The mechanism and stability of thermal transitions in hair keratin colloid. Polym Sci 270:1106–1115
35. Spei M, Holzem R (1987) Thermoanalytical investigations of extended and annealed keratins colloid. Polym Sci 265:965–970
36. El-Amoudy ES, Osman EM (2012) Thermal stability and fastness properties of wool fabric dyed with an ecofriendly natural dye “sambucus nigra” under the effect of different mordants. Elixir Appl Chem 44C:7080–7085
37. Wortmann FJ, Deutz H (1998) Thermal analysis of ortho- and para cortical cells isolated from wool fibres. J Appl Polym Sci 68:1991–199510.1002/(SICI)1097-4628(19980620)68:12<1991::AID-APP13>3.0.CO;2-V ↗
38. Popescu C, Augustin P (1999) Effect of chlorination treatment on the thermogravimetric behavior of wool fibres. J Therm Anal Calorim 57:509–51510.1023/A:1010124209852 ↗
39. Wang H, Liu X, Wang X (2005) Internal structure and pigment granules in colored alpaca fibers. Fibers polym 6(3):263–26810.1007/BF02875652 ↗
40. Hills AWD (1968) The mechanism of the thermal decomposition of calcium carbonate. Chem Eng Sci 23(4):297–32010.1016/0009-2509(68)87002-2 ↗
41. Sahoo A, Soren NM. (2011) Nutrition for Wool Production. WebmedCentral Nutrition 2(10):WMC002384.
42. Hatcher S, King AL, Millington KR (2011) Genetic variation in sulfur, calcium, magnesium, manganese and trace metal content of Merino wool and correlations with brightness, yellowness and photostability. Anim Prod Sci 52(7):463–47010.1071/AN11235 ↗
43. Engler AJ, Sen S, Sweeney HL, Discher DE (2006) Matrix elasticity directs stem cell lineage Specification. Cell 126:677–68910.1016/j.cell.2006.06.044 ↗
44. D’Angelo F, Armentano I, Cacciotti I, Quattrocelli M, Del Gaudio C, Fortunati E, Saino E, Tiribuzi R, Cerulli GG, Visai L, Kenny JM, Sampaolesi M, Bianco A, Martino S, Orlacchio A (2012) Tuning multi-/pluri-potent stem cell fate by electrospun poly (l-lactic acid)-calcium-deficient hydroxyapatite nanocomposite mats. Biomacromolecules 13:1350–136010.1021/bm3000716 ↗
45. Balaji S, Kumar R, Sripriya R, Rao U, Mandal A, Kakkar P, Reddy PN, Sehgal PK (2012) Characterization of keratin–collagen 3D scaffold for biomedical applications. Polym Adv Technol 23:500–507. doi: 10.1002/pat.190510.1002/pat.1905 ↗