2020
DOI: 10.1016/j.scp.2020.100267
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Optimization of keratin protein extraction from waste chicken feathers using hybrid pre-treatment techniques

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Cited by 52 publications
(29 citation statements)
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“…By focusing on the physical and chemical structures and properties of feather keratin, researchers might be able to develop some economically feasible applications for the increasingly large amount of chicken feather waste generated daily 13 , 14 . Functional keratin has been extracted from chicken feather using various methods ranging from chemical 15 , 16 , enzymatic 17 and with ionic solutions 18 . The properties of the extracted keratin has been shown to be a function of the method of extraction method.…”
Section: Introductionmentioning
confidence: 99%
“…By focusing on the physical and chemical structures and properties of feather keratin, researchers might be able to develop some economically feasible applications for the increasingly large amount of chicken feather waste generated daily 13 , 14 . Functional keratin has been extracted from chicken feather using various methods ranging from chemical 15 , 16 , enzymatic 17 and with ionic solutions 18 . The properties of the extracted keratin has been shown to be a function of the method of extraction method.…”
Section: Introductionmentioning
confidence: 99%
“…In the range of wave number 2800 ÷ 3000 cm −1 , there are bands from of stretching vibrations within a group–CH in the soft segments formed from polyols [ 56 , 57 , 58 ].…”
Section: Resultsmentioning
confidence: 99%
“…In all analyzed samples were also observed bands derived from bond vibrations of C = O (1728, 1711, 1664, 1658, and 1650 cm −1 ), C = C from aromatic ring (1597 cm −1 ) bending and deformation vibrations derived from N–H bonds within HNC = O (1534 and 1512 cm −1 ), H3C–C (1450 cm −1 ), –O–CH2 (1411 cm −1 ) and νasym CO/sym within the group–NCO–O (1230 and 921 cm −1 ) in–C–O–C–group [ 56 ]. In the range around 756 cm −1 , the band represents a C–H bond from the aromatic ring.…”
Section: Resultsmentioning
confidence: 99%
“…The high stability, resistance, and insolubility of keratin are due to the network structure created by the numerous strong, covalent disulfide bonds between thiol (-SH) groups contained in cysteine residues, within and between polypeptides of keratin [ 10 , 23 , 29 , 30 , 31 ]. The formed structure induces compactness to keratin, because of the network created by the adjacent polypeptides and sulfur–sulfur cross-links [ 17 , 32 , 33 ]. On the other hand, these disulfide linkages avoid releasing some helpful amino acids and short peptides found in keratin [ 34 , 35 ].…”
Section: Composition and Structure Of Keratinmentioning
confidence: 99%
“…Transforming the ovine skins and bovine hides into leather caused about 2 × 10 5 tons of hair and 5.6 × 10 4 tons of wool per year [ 15 , 16 ], while domains such as textile and apparels generate 2.5 million tons of keratinous wastes yearly, in the form of waste and used wool materials [ 12 ]. Among keratinous materials, the most abundant and sustainable in nature is the chicken feather waste [ 17 ]. Globally quantity of feathers produced by poultry processing, as a by-product, was estimated at ~8.5 billion tons per year [ 1 , 18 ], while annual worldwide production of poultry encounters a continuous increase, anticipating reaching more than 24.8 billion animals in 2030 and 37.0 billion in 2050, respectively [ 10 , 19 ].…”
Section: Introductionmentioning
confidence: 99%