Isolation and characterization of thermostable collagen from the marine eel-fish (Evenchelys macrura)

•Skin waste of eel fish Evenchelys macrura as a cheap source.•Commercially collagen found non-edible and dumped as the waste of fishes.•It is might can be used as an alternative source of natural mammalian collagen.•Isolated collagen is high thermal stability in comparison to the other skin sources....

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Veröffentlicht in:Process biochemistry (1991) 2013-10, Vol.48 (10), p.1592-1602
Hauptverfasser: Veeruraj, Anguchamy, Arumugam, Muthuvel, Balasubramanian, Thangavel
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container_issue 10
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container_title Process biochemistry (1991)
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creator Veeruraj, Anguchamy
Arumugam, Muthuvel
Balasubramanian, Thangavel
description •Skin waste of eel fish Evenchelys macrura as a cheap source.•Commercially collagen found non-edible and dumped as the waste of fishes.•It is might can be used as an alternative source of natural mammalian collagen.•Isolated collagen is high thermal stability in comparison to the other skin sources.•It is useful for foods, cosmetics, pharmaceuticals commercial industrials export. Collagen is the most abundant protein found in animal body, which is widely used for biomedical and pharmaceutical applications. In the present study, acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin wastes of marine eel fish (Evenchelys macrura) were isolated and characterized. ASC and PSC extracted from eel fish skin showed the yields of 80 and 7.10 percent (based on dry weight), respectively. ASC and PSC comprising different α-chains (α1, α2 and α3) were characterized as type I and exhibited high solubility in acidic pH (1–4) and were soluble in the presence of NaCl at concentration up to 3.0 and 4.0 percent (w/v) for ASC and PSC, respectively. Amino acids analysis of both ASC and PSC contained imino acid of 190 and 200 residues per 1000 residues, respectively. The present results of ASC and PSC from eel fish skin exhibited higher thermal stability of 39°C and 35°C, respectively. Similar, Fourier transform infrared (FTIR) spectra of ASC and PSC were observed and suggesting that pepsin hydrolysis did not affect the secondary structure of collagen, especially triple-helical structure. These results suggest that the marine eel fish skin collagen close to the Td (denaturation temperature) of mammalian collagen which could be used in the biomedical materials, food and pharmaceutical industries as an alternative source.
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Collagen is the most abundant protein found in animal body, which is widely used for biomedical and pharmaceutical applications. In the present study, acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin wastes of marine eel fish (Evenchelys macrura) were isolated and characterized. ASC and PSC extracted from eel fish skin showed the yields of 80 and 7.10 percent (based on dry weight), respectively. ASC and PSC comprising different α-chains (α1, α2 and α3) were characterized as type I and exhibited high solubility in acidic pH (1–4) and were soluble in the presence of NaCl at concentration up to 3.0 and 4.0 percent (w/v) for ASC and PSC, respectively. Amino acids analysis of both ASC and PSC contained imino acid of 190 and 200 residues per 1000 residues, respectively. The present results of ASC and PSC from eel fish skin exhibited higher thermal stability of 39°C and 35°C, respectively. Similar, Fourier transform infrared (FTIR) spectra of ASC and PSC were observed and suggesting that pepsin hydrolysis did not affect the secondary structure of collagen, especially triple-helical structure. 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Collagen is the most abundant protein found in animal body, which is widely used for biomedical and pharmaceutical applications. In the present study, acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin wastes of marine eel fish (Evenchelys macrura) were isolated and characterized. ASC and PSC extracted from eel fish skin showed the yields of 80 and 7.10 percent (based on dry weight), respectively. ASC and PSC comprising different α-chains (α1, α2 and α3) were characterized as type I and exhibited high solubility in acidic pH (1–4) and were soluble in the presence of NaCl at concentration up to 3.0 and 4.0 percent (w/v) for ASC and PSC, respectively. Amino acids analysis of both ASC and PSC contained imino acid of 190 and 200 residues per 1000 residues, respectively. The present results of ASC and PSC from eel fish skin exhibited higher thermal stability of 39°C and 35°C, respectively. Similar, Fourier transform infrared (FTIR) spectra of ASC and PSC were observed and suggesting that pepsin hydrolysis did not affect the secondary structure of collagen, especially triple-helical structure. 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Collagen is the most abundant protein found in animal body, which is widely used for biomedical and pharmaceutical applications. In the present study, acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin wastes of marine eel fish (Evenchelys macrura) were isolated and characterized. ASC and PSC extracted from eel fish skin showed the yields of 80 and 7.10 percent (based on dry weight), respectively. ASC and PSC comprising different α-chains (α1, α2 and α3) were characterized as type I and exhibited high solubility in acidic pH (1–4) and were soluble in the presence of NaCl at concentration up to 3.0 and 4.0 percent (w/v) for ASC and PSC, respectively. Amino acids analysis of both ASC and PSC contained imino acid of 190 and 200 residues per 1000 residues, respectively. The present results of ASC and PSC from eel fish skin exhibited higher thermal stability of 39°C and 35°C, respectively. 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subjects Acid soluble collagen
Amino acids
Biochemistry
biomedical materials
Collagen
Collagens
denaturation
Denaturation temperature
eel
Eel fish
fish skin
Fish skins
Fourier transform infrared spectroscopy
Fourier transforms
hydrolysis
imino acids
mammals
Marine
Pepsin
Pepsin soluble collagen
pharmaceutical industry
Pharmaceuticals
Residues
sodium chloride
solubility
temperature
thermal stability
UV absorption spectrum
wastes
yields
title Isolation and characterization of thermostable collagen from the marine eel-fish (Evenchelys macrura)
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