Physicochemical Properties of Duck Feet Collagen with Different Soaking Time and Its Application in Surimi

Chong Hui Theng, Nurul Huda, Nik Aisyah Nik Muhammad, Chatarina Wariyah, Haslaniza Hashim

Abstract


Duck feet are considered as waste products because people normally do not consume duck feet. It is highly available in Malaysia and thus has the high potential to be the alternative source to produce collagen other than fish, bovine or porcine. The main objective of this study is to evaluate the physicochemical properties of different treated duck feet collagen and its effect on the quality of sardine surimi. Duck feet was stirred and soaked in 5% lactic acid solution for different time (12, 24, 36 and 48 h) at 4ºC. Another treatment for the duck feet is demineralization. Duck feet collagen was demineralized by 0.5M EDTA solution for 24 h prior soaking in lactic acid solution for 24 h. Soaking time 24, 36 and 48 h has successfully decreased fat content of duck feet collagen significantly compared to 12 h. However, no differences in yield were observed for the samples. Prolong soaking time produced duck feet collagen with higher content of imino acid (hydroxyproline + proline). The intensity of lightness (L*) for the demineralized duck feet collagen is lower compared to duck feet collagen which was not treated by EDTA. Duck feet collagen has the ability to improve the quality of sardine surimi gel by enhancing its lightness, water holding capacity, gel strength and texture with low cooking loss and expressible moisture. The folding test score of sardine surimi gel has been increased from 3.00 to 5.00 by the addition of duck feet collagen. The gel strength for sardine surimi gel with the addition of duck feet collagen is in the range of 2625.90 g.mm to 2681.58 g.mm, which is approximately 9 times higher than the gel strength of sardine surimi without collagen (280.43 g.mm).

Keywords


duck feet; collagen; EDTA; sardine surimi

Full Text:

PDF

References


Department of Veterinary Services Malaysia. Available from: [Online]. http://agrolink.moa.my/jph/dvs/commodities/itik/duck-e.html [Accessed 5th March 2016].

Cheng, F.Y., Hsu, F.W., Chang, H.S., Lin, L.C. and Sakata, R. Effect of Different Acids on The extraction of Pepsin-solubilised Collagen Containing Melanin form Silky Fowl Feet. Food Chemistry. 113: 563-567. 2009.

Liu, D.C., Lin Y.K. and Chen, M.T. Optimum Condition of Extracting Collagen from Chicken Feet and its Characteristics. Australasian Journal of Animal Sciences. 14(11): 1638-1644. 2001.

Huda, N., Seow E. K., Normawati, M. N., Nik Aisyah, N.M., Fazilah, A. and Easa, A. M. Preliminary Study on Physicochemical Properties of Duck Feet Collagen. International Journal of Poultry Science. 2012..

Huda, N., Seow E. K., Normawati, M. N., Nik Aisyah, N.M., Fazilah, A. and Easa, A. M. Effect of Duck Feet Collagen Addition on the Physicochemical Properties of Surimi, International Food Research Journal. 20(2): 537-544. 2013.

Deyl, Z., Miksik, I. and Eckhardt, A. Preparative Procedures and Purity Assessment of Collagen Proteins. Journal of Chromatography B. 790: 245–275. 2003..

Pachence, J. M. Process for Extracting Type I Collagen from An Avian Source and Applications Therefor. US. Patent. 5138030. 1992.

Li, Shu-Tung. Collagen Biotechnology and Its Medical Application. Biomedical Engineering: Applications, Basis and Communication. 5: 646-657. 1993.

Pachence, J. M. Collagen-based Devices for Soft Tissue Repair. Journal of Biomedical Materials Research. 33: 35–40. 1996.

Angele, P. J., Abke, R., Kujat, H., Faltermerier, D., Schumann, M., Nerlich, B., Kinner, C. Englert, Z., Ruszczak, R., Mehrl and R. Mueller. Influence of Different Collagen Species on Physico-chemical Properties of Crosslinked Collagen Matrices. Biomaterials. 25: 2831–2841. 2004.

Lee, C. H., Singla, A. and Lee, Y. Biomedical Applications of Collagen. International Journal of Pharmaceutics. 221: 1–22. 2001.

Sadowska, M. I., Koodziejska, and Niecikowska, C. Isolation of Collagen from The Skins of Baltic Cod (Gadus morhua). Food Chemistry. 81(2): 257–262. 2003.

Zayas, J. F. Functionality of proteins in food. Berlin: Springer-Verlag: 6-22. 1997.

Gomez-Guillen, M. C., Gimenez, B., Lopez-Caballero, M. E. and Montero, M. P. Functional and Bioactive Properties of Collagen and Gelatin from Alternative sources: A review. Food Hydrocolloids. 25: 1813-1827. 2011.

Simpson, B. K. Food Biochemistry and Food Processing. John Willey and Sons, New Delhi. 2012.

Gomez-Guillen, M. C., and Montero, P. Extraction of Gelatine from Megrim (Lepidorhombus boscii) Skins with Several Organic Acids. Journal of Food Science. 66(2): 213-216. 2011.

Okada, M. History of Surimi Technology in Japan. In Surimi Technology, (T.C. Lanier and C.M. Lee, eds.) pp. 3-22, Marcel Dekker, New York. 1992.

Hall, G. Fish Processing: Sustainability and New Opportunities, John Wiley and Sons, New Delhi. 2011.

Mukundan, M. K., Suseela, Mathew and Gopakumar K. Nutrients and Nutritional Quality of Pink Perch (Nemiptterus japonicas): Mince and Their Fate on Surimi Manufacturer, In Nutrients and Bioactive Substances in Aquatic Organisms, Eds. K. Devadasan et al, Society of Fisheries Technologists (India), Kochi, India, 215. 1994.

Chaijan, M., Benjakul, S., Visessanguan, W. and Faustman, C. Characteristics and Gel Properties of Muscles from Sardine (Sardinella gibbosa) and Markerel (Rastrelliger kanagurta) Caught in Thailand. Food Research International. 37(10): 1021-1030. 2004.

Chen, H. H. Decoloration and Gel-forming Ability of Horse Mackerel Mince by Air-flotation Washing. Journal of Food Science. 67: 2970–2975. 2002.

Kudre, T., Benjakul, S. and Kishimura, H. Effect of Protein Isolates from Black Bean and Mungbean on Proteolysis and Gel Properties of Surimi from Sardine (Sardinella albella). Food Science and Technology. 50(2): 511-518. 2013.

Skierka, E., Sadowska, M. and Karwowska, A. Optimum Condition for Demineralization Baltic Cod (Gadus morhua) Backbone. Food Chemistry. 105: 215-218. 2007.

Nurkhoeriyati, T., Huda, N. and Ahmad, R. Gelation Properties of Spent Duck Meat Surimi-Like Material Produced Using Acid-Alkaline Solubilization Methods. Journal of Food Science. 76(1): 48-55. 2011.

Ockerman, W. H. Quality Control of Post-mortem Muscle Tissue. The Ohio State University, Ohio, USA, p. 51. 1984.

Association of Official Analytical Chemists (AOAC). Official Methods of Analysis. 17th Edition. Washington DC: Association of Official Analytical Chemists. 2000.

Sarwar, G., Christensen, D. A., Finalayson, A. J., Friedman, M., Hackler, L. R., Mackenzie, S. L., Pellett, P. L. and Tkachuk, R. . Inter- and Intra-Laboratory Variation in Amino Acid Analysis of Food Proteins. Journal of Food Science. 48: 526-531. 1983.

Woo, J., Yu, S., Cho, S., Lee, Y. and Kim, S. Extraction Optimization and Properties of Collagen from Yellofin Tuna (Thunnus albacares) Dorsal Skin. Food Hydrocolloids. 22: 879-887. 2008.

Lanier, T. C. Measurement of Surimi Composition and Functional Properties. In: Surimi Technology, (T.C. Larnier and C.M. Lee, Editors). Marcel Dekkel Inc, New York. 1992.

Pietrasik, Z., and Li-Chan, E. C. Y. Binding and Textural Properties of Beef Gels as Affected by Protein, K-carrageenan and Microbial Transglutaminase Addition. Food Research International. 35: 91-98. 2002.

Benjakul, S., Visessangun, W. and Srivilai, C. Gel Properties of Bigeye Snapper (Priacanthus tayenus) Surimi as Affected by Setting and Porcine Plasma Protein. Journal of Food Quality. 24: 453-471. 2001.

Benjakul, S., Vissessanguan, W. and Tueksuban, J. Changes in Physic-chemical Properties and Gel-forming Ability of Lizardfish (Saurida tumbil) during Post-mortem Storage in Ice. Food Chemistry. 80(4): 535-544. 2003.

Tabilo-Munizaga, G. and Barbosa-Canovas, G. V. Color and Textural Parameters of Pressurized and Heattreated Surimi Gels as Affected by Potato Starch and Egg White, Food Research International. 37: 767-775. 2004.

Wangtueai, S. and Noomhorm, A. Processing Optimization and Characterization of Gelatin from Lizardfish (Saurida spp.) Scales. Food Science and Technology. 42: 825–834. 2009.

Johnston-Banks, F. A. Gelatin. In Harris, P. (Eds.). Food Gelatin, p. 233-289. New York: Elsevier Applied Sciences. 1990.

Li, H., Liu, B. L., Gao, L. Z. and Chen, H. L. Studies on Bullfrog Skin Collagen. Food Chemistry. 84: 65–69. 2004.

Palpandi, C., Ramasamy, P. and Pajinikanth, T. Extraction of Collagen from Mangrove archeaogastropod Nerita (Dostia) crepidularia Lamarck. American-Eurasian Journal of Scientific Research. 5(1): 23-30. 2010.

Andriana, A. and Gabi. D. Rapid Characterization of Peptide Secondary Structure by FT-IR Spectroscopy, Revue. Roumaine de. Chimie. 56(8): 783-791. 2011.

Botta, J.R. Evaluation of Seafood Freshness Quality, New York: VCH Publisher, Inc. 1995.

Hsu, S. Y. Optimation of the Surimi Processing System with a Central Composite Design Method. Journal of Food Engineering. 24(1): 101-111. 1995.

Prabhu, G.A., Doerscher, D.R. and Hull, D.H. Utilization of Pork Collagen Protein in Emulsified and Whole Muscle Meat Products. Journal of Food Science. 69: 388-389. 2004.

Shaviklo, G.Z. Quality Assessment of Fish Protein Isolates Using Surimi Standard Methods. The United Nations University, Fisheries Training Programme. Ice Land. 2006.

Webster, J. D., Ledward, D. A. and Lawrie, R. A. Protein Hydrolysates from Meat Industry by-products. Meat Science. 7: 147–67. 1982.

Chaijan, M., Benjakul, S., Visessanguan, W. and Fautsman, C. Physichochemical Properties, Gel-forming Ability and Myoglobin Content of Sardine (Sardinella gibbosa) and Mackerel (Rastrelliger kanagurta) Surimi Produced by Conventional Method and Alkaline Solubilisation Process. European Food Research Technology. 222(1-2): 58-63. 2006.

Karthikeyan, M., Shamasundar, B.A., Mathew, S., Kumar, P.R. and Prakash, V. Physico-chemical and Functional Properties of Proteins from Pelagic Fatty Fish (Sardinella longiceps) as A Function of Water Washing. International Journal of Food Properties. 7: 353-365. 2004.

Schilling, M.W., Mink, L.E., Gochenour, P.S., Marriot, N.G. and Alvarado, C.Z. Utilization of Pork Collagen for Functionality Improvement of Boneless Cured Ham Manufactured from Pale, Soft, and Exudative Pork. Meat Science. 65: 547-5532003..

Ensoy, U., Kolsarici, N. and Candogan, K. Quality Characteristics of Spent Layer Surimi during Frozen Storage. European Food Research and Technology. 219(1): 14-19. 2004.

Sen, D.P. Advances in Fish Processing Technology. Allied publishers PVT. LTD, New Delhi. 2005.

Pan. J, Shen. H. and Luo. Y. Cryoprotective Effects of Trehalose on Grass Carp (Ctenopharyngodon idellus) Surimi during Frozen Storage. Journal of Food Processing Preservation. 34(4): 715-727. 2010.

Benjakul, S., Visessanguan, W., Riebroy, S., Ishizaki, S. and Tanaka, M. Gel-forming properties of Surimi Produced from Bigeye Snapper, Priacanthus Tayenus and P. Macracanthus, Stored in Ice. Journal of the Science of Food and Agriculture. 82(13): 1442–1451. 2002.

Martinez, I. Water Retention Properties and Solubility of the Myofibrillar Proteins: Interrelationships and Possible Values as Indicators of the Gel Strength in Cod Surimi by a Multivariate Data Analysis. Journal of the Science of Food and Agriculture. 46(4): 469-479. 1989.

Luo, X., Yang, R., Zhao, W., Cheng, Z. and Jiang, X. Gelling Properties of Spanish Mackerel (Scomberomorus niphonius) Surimi as Affected by Washing Process and High Pressure. International Journal of Food Engineering. 6(4): 1-17. 2010.

Nopianti, R., Huda, N., Fazilah, A., Ismail, N., and Easa, A. M. Effect of Different Types of Low Sweetness Sugar on Physicochemical Properties of Threadfin Bream Surimi (Nemipterus spp.) during Frozen Storage. International Food Research Journal. 19(3): 1011-1021. 2012.

Burden, M., Sylvia, G. and Kolbe, E. Optimal Storage Temperature Design Frozen Seafood Inventories: Application to Pacific Whiting Surimi. In: Proceedings of the Twelfth Biennial Conference of the International Institute of Fisheries Economics and Trade, July 21-30, 2004, Tokyo, Japan, pp. 1-13. 2004.

Yoon, W. B., Park, J. W. and Kim, B. Y. Linear Programming in Blending Various Components of Surimi Seafood. Journal Food Science. 62: 561–567. 1997.




DOI: http://dx.doi.org/10.18517/ijaseit.8.3.2670

Refbacks

  • There are currently no refbacks.



Published by INSIGHT - Indonesian Society for Knowledge and Human Development