2012
DOI: 10.4236/msa.2012.312129
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Physical and Morphological Structure of Chicken Feathers (Keratin Biofiber) in Natural, Chemically and Thermally Modified Forms

Abstract: Because of the constant challenge to preserve the environment and the search for new materials, a comparative study was carried out using keratin fiber, a fibrous protein, found in the chicken feathers. Five different samples of the feather were analyzed by Scanning Electron Microscopy (SEM) and X-ray diffractometer (XRD). First in their natural form Keratin Fiber (KF); the second treated with sodium hydroxide (KFNaOH); the third and fourth samples were semi carbonized at 220℃ in an oven without atmospheric co… Show more

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Cited by 29 publications
(23 citation statements)
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“…The keratin degradation mechanism includes sulfitolysis, proteolysis and followed by deamination, although pattern of degradation is not clear till date [6]. As the feather has b-pleated sheet structure consists of 20 amino acids, mainly of cysteine and its structural configuration comprises of a central carbon linked to functional groups (amine, -NH 2 , and carboxylic acid, -COOH), the hydrogen atoms and the group R further twisted and cross linked by disulfide bridges to form a cable-like structures [7]. Enzymatic degradation of the feather entails the mutual characteristic actions of two enzymes disulphide reductase and keratinase [8].…”
Section: Introductionmentioning
confidence: 99%
“…The keratin degradation mechanism includes sulfitolysis, proteolysis and followed by deamination, although pattern of degradation is not clear till date [6]. As the feather has b-pleated sheet structure consists of 20 amino acids, mainly of cysteine and its structural configuration comprises of a central carbon linked to functional groups (amine, -NH 2 , and carboxylic acid, -COOH), the hydrogen atoms and the group R further twisted and cross linked by disulfide bridges to form a cable-like structures [7]. Enzymatic degradation of the feather entails the mutual characteristic actions of two enzymes disulphide reductase and keratinase [8].…”
Section: Introductionmentioning
confidence: 99%
“…By comparing the percentage of water absorbed by neat resins with that absorbed by the biocomposites with CFP and CFM (~24-26 %WA), one can observe that the water absorption increases two times for the last one. According to the literature (Belarmino et al, 2012;Ana Laura Martínez-Hernández & Carlos Velasco-Santos, 2012;Reddy & Yang, 2007;Staron et al, 2011), the high water gain of the composites with feathers compared with that of resins is mainly attributed to the high hygroscopic character of keratin from feathers. The results obtained are in agreement with the results already published (Aranberri et al, 2018(Aranberri et al, , 2017Colom, Rahalli, Cañavate, & Carrillo, 2015;Hong & Wool, 2005), in which the addition of CFP's increases significantly the water absorption in a composite irrespective of the nature of the polymeric matrix.…”
Section: Water Absorptionmentioning
confidence: 99%
“…The surface morphology of CF was characterised by using SEM analysis to determine the porosity and texture of the sorbent. According to Figure 1, chicken feathers have hollow structures of knots and hooks [7]. These hollow structures contribute to the available pore spaces for binding with the oil adsorbates.…”
Section: A Surface Morphologymentioning
confidence: 99%