N. Huda
Fish and Meat Processing Laboratory, Food Technology Programme, School of Industrial Technology, Universiti Sains Malaysia, Minden-11800, Penang, Malaysia
E.K. Seow
Fish and Meat Processing Laboratory, Food Technology Programme, School of Industrial Technology, Universiti Sains Malaysia, Minden-11800, Penang, Malaysia
M.N. Normawati
Fish and Meat Processing Laboratory, Food Technology Programme, School of Industrial Technology, Universiti Sains Malaysia, Minden-11800, Penang, Malaysia
N.M. Nik Aisyah
Fish and Meat Processing Laboratory, Food Technology Programme, School of Industrial Technology, Universiti Sains Malaysia, Minden-11800, Penang, Malaysia
ABSTRACT
Duck feet collagen was extracted using 5% lactic acid and examined for their physicochemical properties (chemical composition and amino acid, yield, pH and swelling percentage, color and Fourier Transform Infrared (FTIR) spectroscopy). Chemical composition of duck feet collagen such as moisture, protein, fat and ash content was 5.85, 29.11, 35.43 and 28.60%, respectively. 17 amino acids were detected in duck feet collagen and included 20.46% glysine, 7.73% hydroxyproline and 10.24% proline. The yield of collagen obtained from this treatment was 28.37%. The collagen extracted was light in color with a pH 2.67 (soaking period) and the swelling percentage was 240.50%. Duck feet collagen (DC) possessed similar bands (Amide A, Amide I, Amide II and Amide III) with commercial Fish Collagen (FC) and commercial Cow Collagen (CC) for the FTIR.
PDF References Citation
How to cite this article
N. Huda, E.K. Seow, M.N. Normawati and N.M. Nik Aisyah, 2013. Preliminary Study on Physicochemical Properties of Duck Feet Collagen. International Journal of Poultry Science, 12: 615-621.
DOI: 10.3923/ijps.2013.615.621
URL: https://scialert.net/abstract/?doi=ijps.2013.615.621
DOI: 10.3923/ijps.2013.615.621
URL: https://scialert.net/abstract/?doi=ijps.2013.615.621
REFERENCES
- Abe, Y. and S. Krimm, 1972. Normal vibrations of crystalline polyglycine I. Biopolymers, 11: 1817-1839.
CrossRefDirect Link - Ahmad, M., S. Benjakul and S. Nalinanon, 2010. Compositional and physicochemical characteristics of acid solubilized collagen extracted from the skin of unicorn leatherjacket (Aluterus monoceros). Food Hydrocolloids, 24: 588-594.
CrossRef - AOAC., 2000. Official Methods of Analysis of AOAC International. 17th Edn., Association of Official Analytical Chemists, Gaithersburg, Maryland.
Direct Link - Benjakul, S., W. Visessanguan, C. Thongkaew and M. Tanaka, 2005. Effect of frozen storage on chemical and gel forming properties of fish commonly used for surimi production in Thailand. Food Hydrocolloids, 19: 197-207.
CrossRef - Cheng, F.Y., F.W. Hsu, H.S. Chang, L.C. Lin and R. Sakata, 2009. Effect of different acids on the extraction of pepsin-solubilised collagen containing melanin from silky fowl feet. Food Chem., 113: 563-567.
CrossRef - Cheow, C.S., M.S. Norizah, Z.Y. Kyaw, N.K. Howell and S.M. Cho, 2007. Preparation and characterisation of gelatins from the skins of sin croaker (Johnius dussumieri) and shortfin scad (Decapterus macrosoma). Food Chem., 101: 386-391.
CrossRef - Doyle, B.B., E.G. Bendit and E.R. Blout, 1975. Infrared spectroscopy of collagen and collagenālike polypeptides. Biopolymers, 14: 937-957.
CrossRefDirect Link - Duan, R., J. Zhang, X. Dua, X. Yao and K. Konno, 2009. Properties of collagen from skin, scale and bone of carp (Cyprinus carpio). Food Chem., 112: 702-706.
CrossRefDirect Link - Farrell Jr, H.M., E.D. Wickham, J.J. Unruh, P.X. Qi and P.D. Hoagland, 2001. Secondary structural studies of bovine caseins: Temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. Food Hydrocolloids, 15: 341-354.
CrossRef - Gimenez, B., J. Turnay, M.A. Lizarbe, P. Montero and M.C. Gomez-Guillen, 2005. Use of lactic acid for extraction of fish skin gelatin. Food Hydrocolloids, 19: 941-950.
CrossRef - Gomez-Guilloen, M.C. and P. Montero, 2001. Extraction of gelatin from megrim (Lepidorhombus boscii) skins with several organic acids. J. Food Sci., 66: 213-216.
CrossRef - Gomez-Guillen, M.C., J. Turnay, M.D. Fernandez-Diaz, N. Ulmo, M.A. Lizarbe and P. Montero, 2002. Structural and physical properties of gelatin extracted from different marine species: A comparative study. Food Hydrocolloid, 16: 25-34.
CrossRef - Gudmunsson, M. and H. Hafsteinsson, 1997. Gelatin from cod skins as affected by chemical treatments. J. Food Sci., 62: 37-39.
Direct Link - Jackson, M., L. Choo, P.H. Watson, W.C. Halliday and H.H. Mantsch, 1995. Beware of connective tissue proteins: Assignment and implications of collagen absorptions in infrared spectra of human tissues. Biochimica et Biophysica Acta (BBA)-Mol. Basis Dis., 1270: 1-6.
CrossRef - Jamilah, B., K.W. Tan, M.R. Umi Hartina and A. Azizah, 2011. Gelatins from three cultured freshwater fish skins obtained by liming process. Food Hydrocolloids, 25: 1256-1260.
CrossRefDirect Link - Kittiphattanabawon, P., S. Benjakul, W. Visessanguan, T. Nagai and M. Tanaka, 2005. Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chem., 89: 363-372.
CrossRefDirect Link - Li, H., B.L. Liu, L.Z. Gao and H.L. Chen, 2004. Studies on bullfrog skin collagen. Food Chem., 84: 65-69.
CrossRef - Liu, D.C., Y.K. Lin and M.T. Chen, 2001. Optimum condition of exracting collagen from chicken feet and its characteristics. Aust. J. Anim. Sci., 14: 1638-1644.
Direct Link - Norziah, M.H., A. Al-Hassan, A.B. Khairulnizam, M.N. Mordi and M. Norita, 2009. Characterization of fish gelatin from surimi processing wastes: Thermal analysis and effect of transglutaminase on gel properties. Food Hydrocolloids, 23: 1610-1616.
CrossRefDirect Link - Pati, F., B. Adhikari and S. Dhara, 2010. Isolation and characterization of fish scale collagen of higher thermal stability. Bioresour. Technol., 101: 3737-3742.
CrossRef - Payne, K.J. and A. Veis, 1988. Fourier transform ir spectroscopy of collagen and gelatin solutions: Deconvolution of the amide I band for conformational studies. Biopolymers, 27: 1749-1760.
CrossRefPubMedDirect Link - Prayitno, 2007. Extraction of collagen from chicken feet with various acidic solutions and soaking time. Anim. Prod., 9: 99-104.
Direct Link - Rodziewicz-Motowidlo, S., A. Sladewska, E. Mulkiewicz, A. Kolodziejczyk, A. Aleksandrowicz, J. Miszkiewicz and P. Stepnowski, 2008. Isolation and characterization of a thermally stable collagen preparation from the outer skin of the silver carp Hypophthalmichthys molitrix. Aquaculture, 285: 130-134.
CrossRefDirect Link - Sadowska, M., I. Kolodziejska and C. Niecikowska, 2003. Isolation of collagen from the skins of Baltic cod (Gadus morhua). Food Chem., 81: 257-262.
CrossRefDirect Link - Sai, K.P. and M. Babu, 2001. Studies on Rana tigerina skin collagen. Comparat. Biochem. Physiol. Part B, 128: 81-90.
CrossRefDirect Link - Sankar, S., S. Sekar, R. Mohan, S. Rani, J. Sundaraseelan and T.P. Sastry, 2008. Preparation and partial characterization of collagen sheet from fish (Lates calcarifer) scales. Int. J. Biol. Macromol., 42: 6-9.
CrossRef - Singh, P., S. Benjakul, S. Maqsood and H. Kishimura, 2011. Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chem., 124: 97-105.
CrossRef - Surewicz, W.K. and H.H. Mantsch, 1988. New insight into protein secondary structure from resolution enhanced infrared spectra. Biochimica Biophysica Acta, 952: 115-130.
Direct Link - Wangtueai, S. and A. Noomhornm, 2009. Processing optimization and characterization of gelatin from lizardfish (Saurida spp.) scales. LWT-Food Sci. Technol., 42: 825-834.
CrossRef - Woo, J.W., S.J. Yu, S.M. Cho, Y.B. Lee and S.B. Kim, 2008. Extraction optimization and properties of collagen from yellowfin tuna (Thunnus albacares) dorsal skin. Food Hydrocolloids, 22: 879-887.
CrossRef