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Studies On The Preparation And Modification Of Feather Keratin Film

Posted on:2015-07-14Degree:MasterType:Thesis
Country:ChinaCandidate:X W DengFull Text:PDF
GTID:2181330434960595Subject:Biochemical Engineering
Abstract/Summary:PDF Full Text Request
Keratin is biodegradability, biocompatibility, non-toxic, inexpensive et al. It has a largerecycling value that can be used as bio-medical, food packaging and pharmaceuticalcontrolled release material. Currently, every year a large number of keratin resources arediscarded in our country, such as poultry feathers and non-industrial textile value wool,resulting in a huge waste of resources and environment pollution.In this paper, the chicken feathers was collected on the market for raw materials and usehydrogen peroxide to disconnect disulfide bonds in feather to extract feather keratin, thenadd glycerol to prepare feather keratin film. The structure of the feather keratin films werecharacterized by FTIR, XRD and DSC, and investigate the effects of glycerol content on theproperties of the feather keratin membrane. The results showed that the amide I band andamide II band of oxidized feather keratin shift and the absorption peak of sulfonic acid groupemerge, the peak intensity of crystallography and crystal melting peak temperature drop. Thethickness of feather keratin film decreases with increasing glycerol content, the surface of thefilm is smooth, the transmittance, the water vapor permeation and the equilibrium moisturecontent are gradually increased. With increasing glycerol content, the tensile strength offeather keratin membrane decreases, while the elongation at break first increases and thendecreases.The feather keratin after hydrogen peroxide oxidation has good processingperformance. However, the feather keratin film is low mechanical strength and high waterabsorption limiting the scope of application of feather keratin film. Cross-linkingmodification can improve the mechanical strength and water resistance of the feather keratinfilms. The morphology and structure were characterized by FTIR, SEM and TG, andinvestigate the effect of the amount of glutaraldehyde on the properties of the feather keratinmembrane. The results showed that: glutaraldehyde crosslink modification can effectivelyimprove the thermal stability, mechanical properties, water vapor permeability and waterabsorption, but the carbonyl groups in the cross-linking agents react with the amino groups inFK under an alkaline and heated environment, resulting in the formation of an imine group(-C=N-) which can absorb visible light and ultraviolet light, so the transmittance of the modified feather keratin membrane decreases.The feather keratin-silica hybrid films were successfully prepared by Solvent casting inthe presence of glycerol and γ-glycidoxypropyltrimethoxysilane (KH560). KH560reactedonto feather keratin chains through the amino-oxirane addition reaction. Simultaneously themethoxysilane groups (Si-O-CH3) hydrolyzed to form silanol groups (Si-OH) and thecondensation reaction of the silanol group (Si-OH) would form Si-O-Si linkages to result in across-linked structure. The structure and properties of the feather keratin-silica hybrid filmswere characterized by means of FTIR、TG、SEM,the mechanical properties and the surfaceand bulk hydrophobicity. The results showed that: The decomposition temperature of thehybrid films increases, the equilibrium water absorption and the diffusion coefficient of watermolecules in the membrane is reduced, reducing the tensile strength increases first increasesand then decreases, when the amount of KH560is6%, the tensile strength of the film reachesits maximum11.32MPa, much higher than not plus KH5605.35MPa.The topic is extracting feather keratin from discarded feathers. after cross-linkingmodification, the feather keratin films is better mechanical properties, low water absorptionand biodegradable, which could be used in bio-medical film, packaging film and drugdelivery film et al.
Keywords/Search Tags:Feather Keratin, Glutaraldehyde, γ-glycidoxypropyltrimethoxysilane(KH560), Cross-linking
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