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Physicochemical Properties of Isolated Peptides from Hwangtae (yellowish dried pollack) Protein Hydrolysate

  • Cho, San-Soon (Department of Food Science and Technology, Kongju National University) ;
  • Lee, Hyo-Ku (Department of Food Science and Technology, Kongju National University) ;
  • Han, Chi-Won (Department of Food Science and Technology, Kongju National University) ;
  • Seong, Eun-Soo (Division of Applied Plants Science, Kangwon National University) ;
  • Yu, Chang-Yeon (Division of Applied Plants Science, Kangwon National University) ;
  • Kim, Myong-Jo (Division of Applied Plants Science, Kangwon National University) ;
  • Kim, Na-Young (Department of Food and Nutrition, Kyunghee University) ;
  • Kang, Wie-Soo (Department of Plant Biotechnology, Kangwon National University) ;
  • Ko, Sang-Hoon (Department of Food Science and Technology, Sejong University) ;
  • Son, Eun-Hwa (Department of Herbal Medicine Resource, Kangwon National University) ;
  • Choung, Myoung-Gun (Department of Herbal Medicine Resource, Kangwon National University) ;
  • Lim, Jung-Dae (Department of Herbal Medicine Resource, Kangwon National University)
  • Published : 2008.09.30

Abstract

Fish protein hydrolysates (FPHs) with different degrees of hydrolysis by treatment with alcalase, pronase, flavourzyme and trypsin and isolated peptide were prepared from Hwangtae (yellow dried pollack, Theragra chalcogramma). Hwangtae protein hydrolysate was fractionated according to the molecular weight into six major types of APO1 (1.3 kDa), APO2 (1 kDa), APO3 (<1 kDa), APACE (<1 kDa), APG1 (70 kDa) and APG2 (70 kDa) isolated from the hydrolysate using consecutive chromatographic methods. Soluble peptide were produced from Hwangtae and evaluated for their nutritional and functional properties. Some functional properties of FPHs were assessed and compared with those of egg albumin or the soybean protein. APO2 had the highest nitrogen solubility value (94.2%), emulsion capacity and emulsion stability of the Alaska Pollack peptide ranged from 12.4 to 39.5 (mL of oil per 200 mg of protein) and 44.0% to 77.5%, respectively. Highest and lowest fat adsorption values were observed for APG1 (9.9 mL of oil per gram of protein) and APO3 (3.8 mL of oil per gram of protein), respectively.

Keywords

References

  1. Aspmo SI, Horn SJ, Eijsink VGH. 2005. Enzymatic hydrolysis of Atlantic cod (Gadus morhua L.) viscera. Process Biochem 40: 1957-1966 https://doi.org/10.1016/j.procbio.2004.07.011
  2. Shahidi F, Han XQ, Synowiecki J. 1995. Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chem 53: 285-293 https://doi.org/10.1016/0308-8146(95)93934-J
  3. Kristinsson HG, Rasco BA. 2000. Fish protein hydrolysates: Production, biochemical, and functional properties. Cri Rev Food Sci Nutr 40: 43-81 https://doi.org/10.1080/10408690091189266
  4. Shahidi F. 1994. Sea food processing by-products. In Seafoods Chemistry, Processing Technology and Quality. Shahidi F, Botta JR, eds. Blackie Academic & Professional, London, UK. p 321-334
  5. Phillips LG, Whitehead DM, Kinsella J. 1994. Structure Function Properties of Food Proteins. Academic Press, San Diego, California, USA
  6. Hall GM, Ahmad NH. 1992. Functional properties of fish protein hydrolysates. In Fish Processing Technology. G.M. Hall ed. Blackie Academic & Professional, New York, USA. p 249-265
  7. Panyam D, Kilara A. 1996. Enhancing the functionality of food proteins by enzymatic modification. Trends Food Sci Technol 7: 120-125 https://doi.org/10.1016/0924-2244(96)10012-1
  8. Cho SS, Lee HK, Yu CY, Kim MJ, Seong ES, Ghimire BK, Son EH, Choung MG, Lim JD. 2008. Isolation and Charaterization of bioactive peptides from Hwangtae (yellowish dried Alaska pollack) protein hydrolysate. J Food Sci Nutr 13: 196-203 https://doi.org/10.3746/jfn.2008.13.3.196
  9. AOAC. 1995. Official Methods of Analysis. $16^{th}$ ed. Association of Official Analytical Chemists, Arilington Virginia, USA
  10. Sathivel S, Betchtel PJ. 2006. Properties of soluble protein powders from Alaska pollock (Theragra chalcogramma). Int J Food Sci Tech 41: 520-529 https://doi.org/10.1111/j.1365-2621.2005.01101.x
  11. Sathivel S, Bechtel PJ, Babbitt J, Prinyawiwatkul W, Negulescu II, Reppond KD. 2004. Properties of protein powders from arrowtooth flounder (Atheresthes stomias) and herring (Clupea harengus) by-product. J Agric Food Chem 52: 5040-5046 https://doi.org/10.1021/jf0351422
  12. Je JY, Park PJ, Kim SK. 2005. Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Res Int 38: 45-50 https://doi.org/10.1016/j.foodres.2004.07.005
  13. Morr V, German B, Kinsella JE, 1985. A collaborative study to develop a standardized food protein soubility procedure. J Food Sci 50: 1715-1718 https://doi.org/10.1111/j.1365-2621.1985.tb10572.x
  14. Webb NB, Ivey FJ, Craig HB. 1970. The measurement of emulsifying capacity by electric resistance. J Food Sci 35: 501-504 https://doi.org/10.1111/j.1365-2621.1970.tb00969.x
  15. Yatsumatsu K, Sawada K, Moritaka S. 1972. Whipping and emulsifying properties of soybean products. Agric Biol Chem 36: 719-729 https://doi.org/10.1271/bbb1961.36.719
  16. Song GC, Mok JS. 2001. Study of edible film creation. Report of West sea fisheries research institute. p 119-253
  17. Karawita R, Heo SJ, Lee BJ, Kim SK, Song CB, Jeon YJ. 2006. Recovery of bioavailable calcium from Alaska pollack (Theragra chalcogramma) fish backbone by-product by pepsiolytic hydrolysis. J Food Sci Nutr 11: 120-126 https://doi.org/10.3746/jfn.2006.11.2.120
  18. Shiau SY. 1994. Seafood protein in human and animal nutrition. In Seafood Proteins. Sikorski ZE, Pan BS, Shahidi F, eds. Chapman & Hall, New York
  19. Korean Health Industry Development Institute. 2006. Report of Development of Nutrient Database, Amino acid Composition of foods. December 2006
  20. FAO/WHO. 1990. Protein Quality Evaluation. Report of a Joint FAO/WHO Expert Consultation
  21. Friedman K. 1996. Nutritional value of proteins from different food sources: a review. J Agric Food Chem 44: 6-29 https://doi.org/10.1021/jf9400167
  22. Venugopal V, Chawla, SP, Nair PM. 1996. Spray dried protein powder from threadfin beam: preparation, properties and comparison with FPC type-B. J Muscle Foods 7: 55-71 https://doi.org/10.1111/j.1745-4573.1996.tb00587.x
  23. Yanez E, Ballester D, Monckeberg F. 1976. Enzymatic fish protein hydrolyzate: chemical composition, nutritive value and use as a supplement to cereal protein. J Food Sci 41: 1289-1292 https://doi.org/10.1111/j.1365-2621.1976.tb01154.x
  24. Liu LL, Pigott GM. 1981. Preparation and use of inexpensive crude pepsin for enzyme hydrolysis of fish. J Food Sci 46: 1569-1572 https://doi.org/10.1111/j.1365-2621.1981.tb04223.x
  25. Cheftel C, Ahern M, Wang DIC, Tannenbaum SR. 1971. Enzymatic solubilization of fish protein concentrate: Batch studies applicable to continuous enzyme recycling processes. J Agric Food Chem 19: 155-161 https://doi.org/10.1021/jf60173a007
  26. Adler-Nissen J. 1986. Enzymic Hydrolysis of Food Proteins. Elsevier Applied Science Publishers, Barking, UK
  27. Clegg KM, McMillan AD. 1974. Dietary enzymic hydrolysates of protein with reduced bitterness. J Food Technol 9: 21-29 https://doi.org/10.1111/j.1365-2621.1974.tb01741.x
  28. Cogan V, Moshe M, Mokady S. 1981. Debittering and nutritional upgrading of enzymic casein hydrolysates. J Sci Food Agric 32: 459-466 https://doi.org/10.1002/jsfa.2740320506
  29. Wilding P, Lilliford PJ, Regenstain JM. 1984. Functional properties of proteins in food. J Chem Technol Biotechnol 34: 182-189 https://doi.org/10.1002/jctb.280340307
  30. Chobert JM, Bertrand HC, Nicolas MG. 1988. Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin. J Agric Food Chem 36: 883-892 https://doi.org/10.1021/jf00083a002
  31. Kuehler CA, Stine CM. 1974. Effect of enzymatic hydrolysis on some functional properties of whey protein. J Food Sci 39: 379-382 https://doi.org/10.1111/j.1365-2621.1974.tb02899.x
  32. Lee SW, Shimiuzu M, Kaminogawa S, Yamaguchi K. 1987. Emulsifying properties of a mixture of peptides derived from the enzymatic hydrolysates of b-casein. Agr Biol Chem 51: 161-166 https://doi.org/10.1271/bbb1961.51.161
  33. Spinelli J, Koury B, Miller R. 1972. Approaches to the utilization of fish for the preparation of protein isolates; enzymic modifications of myofibrillar fish proteins. J Food Sci 37: 604-608 https://doi.org/10.1111/j.1365-2621.1972.tb02703.x
  34. Groninger HS, Miller R. 1979. Some chemical and nutritional properties of acylated fish proteins. J Agric Food Chem 27: 948-955 https://doi.org/10.1021/jf60225a049
  35. Dubrow DL, Kramer A, McPhee AD. 1973. Effects of temperature on lipid extraction and functional properties of fish protein concentrate (FPC). J Food Sci 38: 1012-1015 https://doi.org/10.1111/j.1365-2621.1973.tb02136.x
  36. Kinsella JE. 1976. Functional properties of proteins in food: A survey. Crit Rev Food Sci Nutr 8: 219-280
  37. Kristinsson HG, Rasco BA. 2000. Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. J Agric Food Chem 48: 657-666 https://doi.org/10.1021/jf990447v
  38. Haque ZU. 1993. Influence of milk peptides in determining the functionality of milk proteins: A review. J Dairy Sci 76: 311-320 https://doi.org/10.3168/jds.S0022-0302(93)77352-X
  39. Kristinsson HG. 1998. Reaction kinetics, biochemical and functional properties of salmon muscle proteins hydrolyzed by different alkaline proteases. MS thesis. University of Washington, Seattle, WA