한국식품영양과학회지 (Journal of the Korean Society of Food Science and Nutrition)

  • 제35권10호
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  • Pages.1394-1398
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  • 2006
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  • 1226-3311(pISSN)
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  • 2288-5978(eISSN)
한국식품영양과학회 (The Korean Society of Food Science and Nutrition)
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건조 어육 단백질 분말의 식품학적 기능성

Food Functionalities of Dried Fish Protein Powder

  • 최경임 (경상대학교 해양생명과학부/해양산업연구소) ;
  • 홍유미 (경상대학교 해양생명과학부/해양산업연구소) ;
  • 이근우 (군산대학교 식품공학과) ;
  • 최영준 (경상대학교 해양생명과학부/해양산업연구소)
  • Choi, Gyeong-Lim (Division of Marine Life Science/Institute of Marine Industry Gyeongsang National University) ;
  • Hong, Yu-Mi (Division of Marine Life Science/Institute of Marine Industry Gyeongsang National University) ;
  • Lee, Keun-Woo (Major in Food Biotechology, Kunsan National University) ;
  • Choi, Young-Joon (Division of Marine Life Science/Institute of Marine Industry Gyeongsang National University)
  • 발행 : 2006.12.29
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초록

pH 전이공정에 따라 어육 단백질을 회수하고 드럼건조하여 분말 단백질을 제조한 후, 이들 단백질의 몇 가지 식품학적 기능성을 측정하였다. 건조 어육 단백질 분말의 용해도는 pH 7.0으로 조절한 단백질이 PH 5.5에 비하여 높았다. 유화활성지표는 $0.035\sim0.043m^2/g-protein$(pH 5.5 단백질 분말)로 비교적 낮았다. 그리고 유화안정성, 거품능 및 거품안정성은 관측되지 않았다. 점도 값은 수리미 단백질의 1/10에 불과한 $50,200\sim39,000\;cP$의 범위였다. 수분과 지방흡착능력은 각각 $2.63\sim2.89g-water/g$과 $2.13\sim2.17g-oil/g$이었고, 입자의 크기와 pH에 따른 영향은 없었다. 이 같은 실험 결과는 지방흡착을 위한 육의 대체제로 patty 제품 등에 건조 어육 단백질을 적용할 수 있을 것으로 보인다.

Functionalities of drum-dried fish muscle protein from pH shifting process have been investigated by determining solubility, emulsion activity, rehydration, fat-adsorption capacity, viscosity, and color. Solubility was higher in recovered protein at pH 7.0 than that at pH 5.5, and not dependent on ionic strength. Solubility of the dried protein recovered at pH 7.0 depended on pH of solvent, and lowest in the range of pH 3 to pH 6. The dried protein showed relatively low emulsion capacity in all the samples. Emulsion stability, foam capacity and foam stability were not observed in the samples. Viscosity was in the range of $50,200\sim39,000cP$. Rehydration and fat-binding capacities were $2.63\sim2.89g$-water/g and $2.13\sim2.17g$-oil/g, respectively, and not dependent on particle size and pH. Drum-dried fish muscle protein has a potential application as an ingredient of meat patty products.

키워드

참고문헌

  1. Powrie WD. 1973. Characteristics of food myo-system and their behavior during freeze-preservation. In Low temperature preservation of foods and living matter. Fennema OR, Powrie WD, Marth EH, eds. Marcel Dekker, New York. p 598
  2. Matsumoto JJ. 1979. Denaturation of fish muscle proteins during frozen storage. In Proteins at low temperature. Fennema OR, ed. American Chemical Society, Washington, DC. p 205-226
  3. Mastumoto JJ. 1980. Chemical deterioration of muscle proteins during frozen storage. In Chemical deterioration of proteins. Whitaker JR, Fujimaki M, ed. Americal Chemical Society, Washington, DC. p 95-124
  4. Park JW, Lanier TC, Keeton JT, Hamann DD. 1987. Use of cryoprotectants to stabilize functional properties of pre-rigor salted beef during frozen storage. J Food Sci 52: 537-542 https://doi.org/10.1111/j.1365-2621.1987.tb06669.x
  5. Park JW, Lanier TC. 1987. Combined effects of phosphate and sugar or polyol on protein stabilization of fish myofibrils. J Food Sci 52: 1509-1513 https://doi.org/10.1111/j.1365-2621.1987.tb05866.x
  6. Sikorski Z, Olley J, Kostuch S. 1976. Protein changes in frozen fish. Crit Rev Food Sci Nutr 8: 97-121 https://doi.org/10.1080/10408397609527218
  7. Shenouda SYK. 1980. Theories of protein denaturation during frozen storage of fish flesh. In Advances in food research. Chichester CO, Mark EM, Stewart GF, eds. Academic press, New York. Vol 26, p 275-311
  8. Park JW. 1994. Cryoprotection of muscle proteins by carbohydrates and polyalcohols- a review. J Aquatic Food Prod Technol 3: 23-41 https://doi.org/10.1300/J030v03n03_03
  9. Carpenter JF, Crowe JH, Arakawa T. 1989. Comparison of solute-induced protein stabilization in aqueous solution and the in the frozen and dried states. J Dairy Sci 73: 3627-3636 https://doi.org/10.3168/jds.S0022-0302(90)79065-0
  10. Carpenter JF, Arakawa T, Crowe JH. 1991. Interactions of stabilizing additives with proteins during freeze-thawing and freeze-drying. Develop Biol Standard 74: 225-239
  11. Niki H, Matsuda Y, Suzuki T. 1992. Dried froms of surimi. In Surimi technology. Lanier TC, Lee CM, eds. Marcel Dekker, New York. p 209-242
  12. Reynolds J, Park JW, Choi YJ. 2002. Physicochemical properties of Pacific whiting surimi as affected by various freezing and storage conditions. J Food Sci 67: 2072-2078 https://doi.org/10.1111/j.1365-2621.2002.tb09503.x
  13. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. 1951. Protein measurement with Folin phenol reagent. J Biol Chem 193: 256-275
  14. Pearce KN, Kinsella JE. 1978. Emulsifying properties of proteins: evaluation a turbidimeter technique. J Agric Food Chem 26: 716-723 https://doi.org/10.1021/jf60217a041
  15. SAS. 2002. JMP, version 5, Staistics and graphics guide. SAS Institute, Cary, NC, USA. p 87-122
  16. Choi YJ, Park JW. 2002. Acid-aided protein recovery from enzyme-rich Pacific whiting. J Food Sci 67: 2962-2967 https://doi.org/10.1111/j.1365-2621.2002.tb08846.x
  17. Park JD, Jung C-H, Kim J-S, Cho D-M, Cho MS, Choi YJ. 2003. Surimi processing using acid and alkali solubilization of fish muscle protein. J Korean Soc Food Sci Nutr 32: 400-405 https://doi.org/10.3746/jkfn.2003.32.3.400
  18. Voutsinas LP, Cheung E, Nakai S. 1983. Relationship of hydrophobicity to emulsifying properties of heat denaurated proteins. J Food Sci 48: 26-32 https://doi.org/10.1111/j.1365-2621.1983.tb14781.x
  19. Kawai Y, Hatano M, Zama K. 1987. Effect of heat treatment on the emulsifying properties of carp myosin. Nippon Suisan Gakkaishi 53: 665-671 https://doi.org/10.2331/suisan.53.665
  20. Nakai S. 1983. Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. J Agric Food Chem 32: 676-683
  21. Townsend A-A, Nakai S. 1983. Relationships between hydrophobicity and foaming characteristics of food proteins. J Food Sci 48: 588-594 https://doi.org/10.1111/j.1365-2621.1983.tb10796.x
  22. Jung CH, Kim J-S, Jin S-K, Kim IS, Jung K-J, Choi YJ. 2004. Gelation properties and industrial application of functional protein from fish muscle-1. Effect of pH on chemical bonds during thermal denaturation. J Korean Soc Food Sci Nutr 33: 1668-1675 https://doi.org/10.3746/jkfn.2004.33.10.1668
  23. Barbut S. 1996. Determining and fat holding. In Methods of testing protein functionality. Hall GM, ed. Blackie Academic & Professional, New York. p 186-225
  24. Schenz TW, Morr CV. 1996. Viscosity. In Methods of testing protein functionality. Hall GM, ed. Blackie Academic & Professional, New York. p 61-75
  25. Park JW. 1994. Functional protein additives in surimi gels. J Food Sci 59: 525-527 https://doi.org/10.1111/j.1365-2621.1994.tb05554.x
  26. Choi YJ, Cho MS, Park JW. 2000. Effect of hydration time and salt addition on gelation properties of major protein additives. J Food Sci 65: 1338-1342 https://doi.org/10.1111/j.1365-2621.2000.tb10608.x