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Biotechnology: Characterization of Collagen From Eggshell Membrane

This research article characterized collagen extracted from eggshell membrane. Analysis showed the collagen contained high amounts of glycine, proline, and hydroxyproline and consisted of two types of alpha chains. Fourier transform infrared spectroscopy identified characteristic amide peaks. Differential scanning calorimetry found the thermal denaturation temperature to be 55.10°C, indicating the collagen retained intermolecular crosslinks after extraction. The study concluded collagen from eggshell membrane is type I collagen that could have applications in foods, cosmetics, medicine, and pharmaceuticals.

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58 views2 pages

Biotechnology: Characterization of Collagen From Eggshell Membrane

This research article characterized collagen extracted from eggshell membrane. Analysis showed the collagen contained high amounts of glycine, proline, and hydroxyproline and consisted of two types of alpha chains. Fourier transform infrared spectroscopy identified characteristic amide peaks. Differential scanning calorimetry found the thermal denaturation temperature to be 55.10°C, indicating the collagen retained intermolecular crosslinks after extraction. The study concluded collagen from eggshell membrane is type I collagen that could have applications in foods, cosmetics, medicine, and pharmaceuticals.

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angeleekaye abelinde
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Biotechnology

Volume 8 (2): 254-258, 2009

Research Article

Characterization of Collagen from Eggshell


Membrane
Yu-Hong Zhao and Yu-Jie Chi
Abstract
Collagen was extracted by acid-pepsin digestion and isolated by salt
precipitation from eggshell membrane. The characteristics of
eggshell membrane collagen were investigated with amino acid
analysis, sodium dodecyl sulphate-polyacrylamide gel
electrophoresis, Fourier transforms infrared spectroscopy and
differential scanning calorimetry. The amino acid composition of
the eggshell membrane collagen is rich in glycine, proline and
hydroxyproline. Electrophoresis revealed two different α (α 1 and α2 )
chains. FTIR showed regions of amides A, B, I, II and III were
3325, 2926, 1653, 1550 and 1240 cm -1, respectively. Analysis of
differential scanning calorimetry revealed that thermal denaturation
temperature of eggshell membrane collagen was 55.10°C and
collagen of eggshell membrane retains intermolecular crosslinks
after extraction process. Collagen of eggshell membrane was typical
type I collagen and may be applicable to variety of usage including
functional food, cosmetic, biomedical and pharmaceutical
industries.

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