Food Science of Animal Resources (한국축산식품학회지)

Korean Society for Food Science of Animal Resources (한국축산식품학회)
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Compositions, Protease Inhibitor and Gelling Property of Duck Egg Albumen as Affected by Salting

  • Quan, Tran Hong (Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University) ;
  • Benjakul, Soottawat (Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University)
  • Received : 2017.09.20
  • Accepted : 2017.11.25
  • Published : 2018.02.28
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Abstract

Chemical compositions, trypsin inhibitory activity, and gelling properties of albumen from duck egg during salting of 30 days were studied. As the salting time increased, moisture content decreased, the salt content and surface hydrophobicity increased (p<0.05). Trypsin inhibitory activity and specific activity were continuously decreased throughout the salting time of 30 days (p<0.05). This coincided with the decrease in band intensity of inhibitor with molecular weight of 44 kDa as examined by inhibitory activity staining. Nevertheless, no differences in protein patterns were observed in albumen during the salting of 30 days. Based on texture profile analysis, hardness, springiness, gumminess, chewiness, and resilience of albumen gel decreased with increasing salting time. Conversely, salted albumen gels exhibited higher cohesiveness and adhesiveness, compared to those of fresh albumen. Scanning electron microscopic study revealed that gel of salted albumen showed the larger voids and less compactness. In general, salting lowered trypsin inhibitory activity and gelling property of albumen from duck egg to some extent. Nevertheless, the salted albumen with the remaining inhibitor could be an alternative additive for surimi or other meat products to prevent proteolysis.

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References

  1. Abeyrathne E, Lee H, Jo C, Suh J, Ahn D. 2015. Enzymatic hydrolysis of ovomucoid and the functional properties of its hydrolysates. Poultry Sci 94:2280-2287. https://doi.org/10.3382/ps/pev196
  2. Abeyrathne EDNS, Lee HY, Ahn DU. 2013. Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents-A review. Poultry Sci 92:3292-3299. https://doi.org/10.3382/ps.2013-03391
  3. AOAC. 2000. Official Methods of Analysis of AOAC International. Gaithersburg, MD, USA pp 5.
  4. Benjakul S, Visessanguan W. 2000. Pig plasma protein: potential use as proteinase inhibitor for surimi manufacture; inhibitory activity and the active components. J Sci Food Agric 80:1351-1356. https://doi.org/10.1002/1097-0010(200007)80:9<1351::AID-JSFA647>3.0.CO;2-I
  5. Benjakul S, Visessanguan W, Srivilai C. 2001. Porcine plasma protein as proteinase inhibitor in bigeye snapper (Priacanthus Tayenus) muscle and surimi. J Sci Food Agric 81:1039-1046. https://doi.org/10.1002/jsfa.887
  6. Cardamone M, Puri N. 1992. Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem J 282:589-593. https://doi.org/10.1042/bj2820589
  7. Cegielska-Radziejewska R, Lesnierowski G, Kijowski J. 2008. Properties and application of egg white lysozyme and its modified preparations-a review. Pol J Food Nutr Sci 58:5-10.
  8. Chandra M, Shamasundar B. 2015. Texture profile analysis and functional properties of gelatin from the skin of three species of fresh water fish. Int J Food Prop 18:572-584. https://doi.org/10.1080/10942912.2013.845787
  9. Chi SP, Tseng KH. 1998. Physicochemical properties of salted pickled yolks from duck and chicken eggs. J Food Sci 63: 27-30. https://doi.org/10.1111/j.1365-2621.1998.tb15668.x
  10. Hu S, Qiu N, Liu Y, Zhao H, Gao D, Song R, Ma M. 2016. Identification and comparative proteomic study of quail and duck egg white protein using 2-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry analysis. Poultry Sci 95:1137-1144. https://doi.org/10.3382/ps/pew033
  11. Huang JJ, Tsai JS, Pan BS. 1999. Pickling time and electrodialysis affects functional properties of salted duck egg white. J Food Biochem 23:607-618. https://doi.org/10.1111/j.1745-4514.1999.tb00589.x
  12. Iwashita K, Inoue N, Handa A, Shiraki K. 2015. Thermal aggregation of hen egg white proteins in the presence of salts. Protein J 34:212-219. https://doi.org/10.1007/s10930-015-9612-3
  13. Ji L, Liu H, Cao C, Liu P, Wang H, Wang H. 2013. Chemical and structural changes in preserved white egg during pickled by vacuum technology. Food Sci Technol Int 19:123-131. https://doi.org/10.1177/1082013212442186
  14. Kaewmanee T, Benjakul S, Visessanguan W. 2009. Changes in chemical composition, physical properties and microstructure of duck egg as influenced by salting. Food Chem 112:560-569. https://doi.org/10.1016/j.foodchem.2008.06.011
  15. Kaewmanee T, Benjakul S, Visessanguan W. 2011a. Effect of NaCl on thermal aggregation of egg white proteins from duck egg. Food Chem 125:706-712. https://doi.org/10.1016/j.foodchem.2010.09.072
  16. Kaewmanee T, Benjakul S, Visessanguan W. 2011b. Effects of salting processes and time on the chemical composition, textural properties, and microstructure of cooked duck egg. J Food Sci 76:139-147. https://doi.org/10.1111/j.1750-3841.2010.01975.x
  17. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. https://doi.org/10.1038/227680a0
  18. Lau M, Tang J, Paulson A. 2000. Texture profile and turbidity of gellan/gelatin mixed gels. Food Res Int 33:665-671. https://doi.org/10.1016/S0963-9969(00)00111-3
  19. Mmadi M, Amza T, Wang YC, Zhang M. 2014. Effect of desalination on physicochemical and functional properties of duck (Anas Plotyrhyncus) egg whites. Adv J Food Sci Technol 6:784-791. https://doi.org/10.19026/ajfst.6.111
  20. Qiu N, Ma M, Zhao L, Liu W, Li Y, Mine Y. 2012. Comparative proteomic analysis of egg white proteins under various storage temperatures. J Agric Food Chem 60:7746-7753. https://doi.org/10.1021/jf302100m
  21. Ren Y, Wu J, Renema R. 2010. Nutritional and health attributes of eggs. In I. Guerrero-Legarreta (Ed.), Handbook of Poultry Science and Technology. Hoboken, New Jersey: John Wiley & Sons Inc, pp 533-578.
  22. Robinson HW, Hogden CG. 1940. The biuret reaction in the determination of serum proteins. 1. A study of the conditions necessary for the production of a stable color which bears a quantitative relationship to the protein concentration. J Biol Chem 135:707-725.
  23. Rossi M, Nys Y, Anton M, Bain M, De Ketelaere B, De Reu K, Dunn I, Gautron J, Hammershoj M, Hidalgo A. 2013. Developments in understanding and assessment of egg and egg product quality over the last century. World Poultry Sci J 69:414-429. https://doi.org/10.1017/S0043933913000408
  24. Saxena I, Tayyab S. 1997. Protein proteinase inhibitors from avian egg whites. Cell Mol Life Sci 53:13-23. https://doi.org/10.1007/PL00000575
  25. Takenawa T, Takahashi K, Le-Chang S, Okazaki E, Osako K. 2015 The effect of ovalbumin on the protease activity. Int. Symposium Aqua. Product Process. Bogor, Indonesia. Vol. 1, pp 39-41.
  26. Wang TH. 2016. Salting yolks directly using fresh duck egg yolks with salt and maltodextrin. J Poult Sci 54:97-102.
  27. Woodward SA. 1990. Egg protein gels. In P. Harris (Ed.), Food gels. Netherlands: Springer, pp 175-199.
  28. Yang N, Jin Y, Xu Y, Bin Y, Xu X. 2016. Effect of pressure cooking on physicochemical properties of salted eggs. RSC Adv 6:97089-97095. https://doi.org/10.1039/C6RA18737D
  29. Yilmaz MT, Karaman S, Dogan M, Yetim H, Kayacier A. 2012. Characterization of O/W model system meat emulsions using shear creep and creep recovery tests based on mechanical simulation models and their correlation with texture profile analysis (TPA) parameters. J Food Eng 108:327-336. https://doi.org/10.1016/j.jfoodeng.2011.08.005

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