Extraction of Collagen from Cattle Skin and Synthesis of Collagen Based Flame Retardant Composition and Introduction into Cellulosic Textile Material by Graft Copolymerization

Nabijon, Nabiev; Ahmed, Md. Raju; Adkham, Rafikov; Heng, Quan

doi:10.14233/ajchem.2017.20776

Cited by 15 publications

(4 citation statements)

References 15 publications

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“…Alkalis have a tendency to hydrolyze collagen fibrils [ 71 ] and the amino acids cysteine, histidine, serine, and threonine may be destroyed in the process [ 52 , 76 ]. The use of alkali hydrolysis appears to be mostly confined to extracting collagen from leather processing waste [ 71 , 77 ], however, a collagen-based flame retardant has been produced from collagen obtained by alkaline extraction of otherwise untreated cattle skin [ 78 ].…”

Section: Collagen Extraction Processmentioning

confidence: 99%

Collagen Extraction from Animal Skin

Matinong

Chisti

Pickering

et al. 2022

Biology

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Collagen is the most abundant structural protein in animals. It is the major component of skin. It finds uses in cosmetics, medicine, yarn production and packaging. This paper reviews the extraction of collagen from hides of most consumed animals for meat with the focus on literature published since 2000. The different pretreatment and extraction techniques that have been investigated for producing collagen from animal skins are reviewed. Pretreatment by enzymatic, acid or alkaline methods have been used. Extraction by chemical hydrolysis, salt solubilization, enzymatic hydrolysis, ultrasound assisted extraction and other methods are described. Post-extraction purification methods are also explained. This compilation will be useful for anyone wishing to use collagen as a resource and wanting to further improve the extraction and purification methods.

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Section: Collagen Extraction Processmentioning

confidence: 99%

Collagen Extraction from Animal Skin

Matinong

Chisti

Pickering

et al. 2022

Biology

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“…To eliminate this drawback, it is proposed to mix collagen with plasticizing additives, for example, glycerol or PAD. Graft copolymers of collagen with AA and methylmethacrylate have been synthesized in the presence of PP, 36,37 collagen grafting to cellulose imparts specific properties to the textile material. 38 Collagen/PAA/MXene grafted hydrogels have high mechanical strength and adhesive properties.…”

Section: Introductionmentioning

confidence: 99%

Graft copolymers of collagen and acrylic monomers—Reagents for sizing of cotton yarn

Rafikov,

Ibodulloyev,

Yasinskaya

et al. 2024

Polymer Engineering & Sci

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A new highly effective sizing reagent based on grafted collagen copolymers has been proposed for cotton yarn. The copolymers were synthesized by reacting an aqueous solution of collagen with acrylic monomers—acrylic, matacrylic acids, and their amides in the presence of potassium persulfate. Based on Scanning electron microscopy ‐ Energy dispersive (SEM‐EDS) analysis data, the composition of the copolymers was determined. Unsaturated acids are more actively grafted onto collagen than their amides. When a polymer film is formed from a solution of a collagen copolymer with (meth)acrylic acid, microcracks appear on the surface of the sample; microcracks are absent in films of copolymers with (meth)acrylamide. Films of copolymers, especially methacrylamide, are quite flexible and contribute to a significant improvement in the properties of the yarn. The tensile strength of yarn sized with copolymers increases by 20%–65% compared to unsized yarn, and by 13%–38% compared to yarn sized with a starch solution. At the same time, the relative tensile elongation of the experimental yarn improves by 14%–58%, while this property of starch‐size yarn deteriorates by 14%–22% compared to unsized yarn. The complete removal of graft copolymers from the surface of the yarn in the process of biochemical desizing using the enzyme protease is shown.Highlights Graft copolymerization of (meth)acrylamide with collagen was carried out. Grafting is initiated by the interaction of collagen with potassium persulfate. The synthesized copolymers are effective sizing reagents for cotton yarn. The copolymer with poly(meth)acrylamide forms a flexible and stable film. The protease enzyme completely removes the size from the surface of the yarn.

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“…Collagen and gelatin are used in cosmetics [ 2 ], medical and pharmaceutical products [ 3 ], and food formulation and packaging [ 4 ]. Methods used to extract collagen from tissue [ 5 ] include hydrolysis with acids [ 6 ] and alkalis [ 7 ], solubilization with salts [ 8 ], and enzymatic hydrolysis [ 9 ]. Often, these chemical treatments are assisted with ultrasound [ 10 ] and microwaves [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

Gelatin and Collagen from Sheepskin

Matinong,

Pickering,

Waterland

et al. 2024

Polymers

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Abattoirs dispose of sheepskins as solid waste due to low price and poor demand for sheepskin leather. In principle, as an alternative to being disposed of in landfill, sheepskins can serve as a source of the protein collagen or the hydrolysis product, gelatin. In this research, sheepskins collected from abattoirs were used as a source of collagen. Three extraction methods were compared: acid extraction, acid with enzymes, and alkali extraction. The extracted material was characterized using scanning electron microscopy (SEM) and Fourier-transform infrared spectroscopy (FTIR), small angle X-ray scattering (SAXS), and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The collagen and gelatin extraction yield ranged from 3.1% to 4.8% with the product purity determined by hydroxyproline, ranging from 7.8% for the alkali process to 59% and 68% for the acid and acid-enzyme processes. SDS PAGE showed that the acid process produced fragments with molecular weights in the range 100 to >250 kDa, while acid–enzyme resulted in smaller fragments, below 30 kDa. The FTIR region of the amide I band at 1800–1550 cm−1, which was used as an indicator of the collagen and gelatin content, showed that the gelatin dominated in the acid extracts, and the alkaline extract contained a large portion of keratin. SAXS was found to be a sensitive method for showing the presence of intact collagen fibrils in materials from all of the extraction methods, albeit at low concentrations. Herein, sheepskin is shown to be a useful source for collagen–gelatin material of varying molecular weights.

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Extraction of Collagen from Cattle Skin and Synthesis of Collagen Based Flame Retardant Composition and Introduction into Cellulosic Textile Material by Graft Copolymerization

Cited by 15 publications

References 15 publications

Collagen Extraction from Animal Skin

Collagen Extraction from Animal Skin

Graft copolymers of collagen and acrylic monomers—Reagents for sizing of cotton yarn

Gelatin and Collagen from Sheepskin

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