Bioplastics from Feather Quill

Abstract

Poultry feather quills have been extruded in a twin screw extruder with sodium sulfite treatment as a reducing agent. The effect of four different plasticizers (ethylene glycol, propylene glycol, glycerol, and diethyl tartrate) on the thermoplastic properties was then investigated. Conformational changes and plasticizer-protein interactions in the extruded resins were assessed by Fourier transform infrared spectroscopy (FTIR), while viscoelastic behavior of the quill keratin plasticized with different plasticizers was investigated by dynamic mechanical analysis (DMA). Differential scanning calorimetry (DSC) was used to determine the effect of different plasticizers on protein denaturation. Thermal degradation patterns of the extrudates were studied by thermogravimetric analysis (TGA). The effect of plasticizers on the mechanical properties of resins was also assessed by tensile strength measurements. Results indicated that ethylene glycol was able to interact more effectively with quill keratin at the molecular level, exhibiting only one sharp glass transition, better mechanical properties, and higher transparency compared to other plasticized resins. The two phases found in glycerol plasticized material were attributed to glycerol-rich and protein-rich zones. Propylene glycol and diethyl tartrate exhibited lower H-bonding interactions and showed wide transition regions in DMA profiles during heating, suggesting weak and heterogeneous interactions between quill keratin and these plasticizers.

Valorization of rendering industry wastes and co-products for industrial chemicals, materials and energy: review

“…Plastic materials based on animal protein can be adequately formulated with specific modifiers to produce seeding trays, planting pots and mulching films that are cost competitive with petroleum-based plastics for similar applications Lukubira & Ogale, 2013;Ullah et al, 2011;Ullah & Wu, 2013). Plasticizers are incorporated to improve process-ability, reduce brittleness and modify the properties of the final structure (Hernandez-Izquierdo & Krochta, 2008;Mekonnen et al, 2013c).…”

“…Blood meal 5.7 251 53 Plasticized with 20% Tri (ethylene glycol) Meat and bone meal (Lukubira & Ogale, 2013) 3.96 341 2.1 Plasticized with 30% glycerol Chicken feathers protein extract (Ullah & Wu, 2013) 22.3 811.2 7.6 Plasticized with 30% propylene glycol Chicken feathers protein extract (Ullah & Wu, 2013) 17.8 354 43.8 Plasticized with 30% ethylene glycol Feather quill protein extract (Ullah et al, 2011) 20.5 529.5 11.2 Plasticized with 30% propylene glycol SRM hydrolyzate protein extract 58.56 1463 4.34 Used as epoxy crosslinker (30%) Native chicken feather (Jin et al, 2011b) 55.7 4400 14.2 Grafted with methyl acrylate, and plasticized with 30% plasticizer Native chicken feather (Jin et al, 2011b) 206.3 28,800 1.1 Grafted with methyl acrylate, no plasticizer TS -Tensile strength at break; "elongation at break. plasticization efficiency (Ullah & Wu, 2013).…”

“…plasticization efficiency (Ullah & Wu, 2013). Dynamic mechanical analysis (DMA) and Fourier transform infrared spectroscopy (FTIR) studies (Ullah et al, 2011) exhibited that ethylene glycol, being a smaller molecule, has higher ability to reduce polymer-polymer associations and interact with the protein polypeptide chains through hydrogen bonds compared to propylene glycol. Thermosetting protein-based plastics developed from crosslinking of hydrolyzed SRM protein extracts with epoxy resin exhibited a different set of mechanical performance compared to the thermoplastic proteins.…”

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“…The new approach is cost effective and alternative to commonly used coatings for example, collagen and fibronectin [81]. Recently, several researchers developed films from native keratin, by using reducing agents and different plasticizers, either via compression molding [82] or extrusion and subsequent compression molding [11,83] leading to improved mechanical properties.…”

“…Therefore, from economic and environmental point of views, it is quite desirable to mechanize lucrative and effective process to use these kind of sources in green chemistry [9]. Feather keratins are small proteins, uniform in size, with a molecular weight around 10 kDa [10,11]. They constitute cysteine, hydrophobic residues and β-sheet conformations [8,12,13].…”