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Isolation and Characterization of Collagen from Chicken Feet

Authors: P. Hashim, M. S. Mohd Ridzwan, J. Bakar


Collagen was isolated from chicken feet by using papain and pepsin enzymes in acetic acid solution at 4°C for 24h with a yield of 18.16% and 22.94% by dry weight, respectively. Chemical composition and characteristics of chicken feet collagen such as amino acid composition, SDS-PAGE patterns, FTIR spectra and thermal properties were evaluated. The chicken feet collagen is rich in the amino acids glycine, glutamic acid, proline and hydroxyproline. Electrophoresis pattern demonstrated two distinct α-chains (α1 and α2) and β chain, indicating that type I collagen is a major component of chicken feet collagen. The thermal stability of collagen isolated by papain and pepsin revealed stable denaturation temperatures of 48.40 and 53.35°C, respectively. The FTIR spectra of both collagens were similar with amide regions in A, B, I, II and III. The study demonstrated that chicken feet collagen using papain isolation method is possible as commercial alternative ingredient. 

Keywords: Chicken feet, collagen, papain, pepsin.

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[1] R. Perez-Tamayo, "Pathology of Collagen Degradation”, American J. of Pathol., pp. 509–566, 1978.
[2] I. Bae, K. Osatomi, A. Yoshida, K. Osako, A. Yamaguchi, and K. Hara, "Biochemical Properties of Acid-Soluble Collagens Extracted from the Skins of Underutilised Fishes”, Food Chem., vol. 108, pp. 49–54, 2008.
[3] A. Aberoumand, "Comparative Study between Different Methods of Collagen Extraction from Fish and Its Properties”, World Applied Sci. J., vol. 16, pp. 316–319, 2012.
[4] F. Y. Cheng, F. W. Hsu, H. S. Chang, L. C. Lin, and R. Sakata, "Effect of Different Acids on the Extraction of Pepsin-Solubilised Collagen Containing Melanin from Silky Fowl Feet”, Food Chem., vol. 113, 563–567, 2009.
[5] Department of Statistics Malaysia, "Selected Agricultural Indicators 2012”, Malaysia, 2012, pp. 1–74.
[6] B. Jamilah, K. W. Tan, M. R. Umi Hartina, and A. Azizah, "Gelatins from Three Cultured Freshwater Fish Skins Obtained by Liming Process”, Food Hydrocolloids, vol. 25, pp. 1256–1260, 2011.
[7] A.O.A.C., "Official Methods of Analysis”, Association of Official Analytical Chemist. Arlington, VA., USA, 1999.
[8] U. K. Laemmli, "Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4”, Nature, vol. 227, pp. 680–685, 1970.
[9] Y. K. Lin, and D. C. Liu, "Comparison of Physical–Chemical Properties of Type I Collagen from Different Species”, Food Chem., vol. 99, pp. 244–251, 2006.
[10] J. Muyonga, C. G. Cole, and K. Duodu, "Extraction and Physico-Chemical Characterisation of Nile Perch (Lates niloticus) Skin and Bone Gelatin”, Food Hydrocolloids, vol. 18, pp. 581–592, 2004.
[11] Y. K. Lin, and D. C. Liu, "Effects of Pepsin Digestion at Different Temperatures and Times on Properties of Telopeptide-Poor Collagen from Bird Feet”, Food Chem., vol. 94, pp. 621–625, 2006.
[12] D. C. Liu, Y. K. Lin, and M. T. Chen, "Optimum Condition of Extracting Collagen from Chicken Feet and Its Characteristics”, Asian-Aust. J. Animal Sci., vol. 14, pp. 1638-1644, 2001.
[13] B. Giménez, J. Turnay, M. A. Lizarbe, P. Montero, and M. C. Gómez-Guillén, "Use of Lactic Acid for Extraction of Fish Skin Gelatin”, Food Hydrocolloids, vol. 19, pp. 941–950, 2005.
[14] F. Li, D. Jia, and K. Yao, "Amino Acid Composition and Functional Properties of Collagen Polypeptide from Yak (Bos grunniens) Bone”, LWT - Food Sci. and Tech., vol. 42, pp. 945–949, 2009.
[15] Y. K. Lin, T. Y. Lin, and H. P. Su, "Extraction and Characterisation of Telopeptide-Poor Collagen from Porcine Lung”, Food Chem., vol. 124, pp. 1583–1588, 2001.
[16] D. Liu, L. Liang, J. M. Regenstein, and P. Zhou, "Extraction and Characterisation of Pepsin-Solubilised Collagen from Fins, Scales, Skins, Bones and Swim Bladders of Bighead Carp (Hypophthalmichthys nobilis)”, Food Chem., vol. 133, pp. 1441–1448, 2012.
[17] T. Potaros, N. Raksakulthai, and J. Runglerdkreangkrai, "Characteristics of Collagen from Nile Tilapia (Oreochromis niloticus) Skin Isolated by Two Different Methods”, Nat. Sci., vol. 43, pp. 584–593, 2009..
[18] D. R. Doerscher, J. L. Briggs, and S. M. Lonergan, "Effects of Pork Collagen on Thermal and Viscoelastic Properties of Purified Porcine Myofibrillar Protein Gels”, Meat Sci., vol. 66, pp. 181–188, 2004.
[19] K. Matmaroh, S. Benjakul, T. Prodpran, A. B. Encarnacion, and H. Kishimura, "Characteristics of Acid Soluble Collagen and Pepsin Soluble Collagen from Scale of Spotted Golden Goatfish (Parupeneus heptacanthus)”, Food Chem., vol. 129, pp. 1179–1186, 2001.
[20] J. Muyonga, C. G. Cole, and K. Duodu, "Fourier Transform Infrared (FTIR) Spectroscopic Study of Acid Soluble Collagen and Gelatin from Skins and Bones of Young and Adult Nile Perch (Lates niloticus)”, Food Chem., vol. 86, pp. 325–332, 2004.