한국수산과학회지 (Korean Journal of Fisheries and Aquatic Sciences)

  • 제40권6호
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  • Pages.337-342
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  • 2007
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  • 0374-8111(pISSN)
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  • 2287-8815(eISSN)
한국수산과학회 (The Korean Society of Fisheries and Aquatic Science)
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알칼리 처리하여 회수한 냉동깡치 어육 단백질의 Lysinoalanine 함량

Lysinoalanine in Protein Recovered from Frozen Belanger's Croaker, Johnius grypotus, Using Alkaline Processing

  • 김건배 (군산대학교 식품공학과) ;
  • 이근우 (군산대학교 식품공학과) ;
  • 허성익 (경상대학교 해양생명과학부/해양산업연구소) ;
  • 최영준 (경상대학교 해양생명과학부/해양산업연구소)
  • Kim, Gun-Bae (Major in Food Biotechnology, Kunsan National University) ;
  • Lee, Keun-Woo (Major in Food Biotechnology, Kunsan National University) ;
  • Hur, Sung-Ik (Division of Marine Life Science/Institute of Marine Industry, Gyeongsang National University) ;
  • Choi, Yeung-Joon (Division of Marine Life Science/Institute of Marine Industry, Gyeongsang National University)
  • 발행 : 2007.12.31
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초록

The formation of lysinoalanine (LAL) in protein recovered from the belanger's croaker, Johnius grypotus, using a pH shifting process was measured by amino acid analysis. The LAL peak was detected at 49.24 min, between phenylalanine and histidine peaks in the amino acid analyzer. LAL was not detected in the fish muscle or in protein recovered using the alkaline pH shifting process. LAL was not formed in protein recovered after storage for up to 9 hrs at pH 11, but was detected in the soluble protein fraction at pH 11, followed heating at $90\;^{\circ}C$. The myosin heavy chain decreased with storage time at pH 11. The results suggest that the alkaline shifting process for recovering fish muscle protein is safe, and that no LAL forms.

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참고문헌

  1. Aymard, C., J.L. Cuq and J.C. Cheftel. 1978. Formation of lysinoalanine and lanthionine in various food proteins, heated at neutral or alkaline pH. Food Chem., 3, 1-5 https://doi.org/10.1016/0308-8146(78)90041-9
  2. Borak, Z. 1964. N${\varepsilon}$-(DL-2-amino-carboxyrthyl)-L-lysine, a new amino acid formed on alkaline treatment of proteins. J. BioI. Chem., 239, 2878-2887
  3. Choi, Y.J. and J.W. Park. 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
  4. Damodaran, S. 1996. Amino acids, peptifdes, and proteins. In Food Chemistry, Fennema, O.R., ed, Marcel Dekker Inc., New York, 321-429
  5. Friedman, M., J.C., Zahnley and P.M. Masters. 1981. Relationship between in vitro digestibility of casein and its content of lysinoalanine and D-amino acids. J. Food Sci., 46, 127-131 https://doi.org/10.1111/j.1365-2621.1981.tb14545.x
  6. Friedman, M., C.E. Levin and A.T. Noma AT. 1984. Factors governing lysinoalanine formation in soy proteins. J. Food Sci., 49, 1282-1288 https://doi.org/10.1111/j.1365-2621.1984.tb14970.x
  7. JMP. 2002. Standard least squares. In Statistics and Graphics Guide. SAS Institute, Cary, NC. 179-209
  8. Kim, Y.S., J W. Park and Y.I. Choi. 2003. New approaches for the effective recovery of fish proteins and their physicochemical characteristics. Fish. Sci., 69, 1231-1239 https://doi.org/10.1111/j.0919-9268.2003.00750.x
  9. Miller, R., J. Spinelli and J.K. Babbitt. 1983. Effect of heat and alkali on lysinoalanine formation in fish muscle. J. Food Sci., 48, 296-297 https://doi.org/10.1111/j.1365-2621.1983.tb14858.x
  10. Laemmli, U.K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, 227, 680-685 https://doi.org/10.1038/227680a0
  11. Lanier, T.C., K. Hart and R.E. Martin. 1991. A Manual of Standard Methods for Measuring and Specifying the Properties of Surimi. University of North Carolina Sea Grant College Program, Raleigh, NC, USA
  12. Liener, I.E. 1994. Implications of antinutritional components in soybean food. Crit. Rev. Food Sci. Nutr., 43, 31-67
  13. Lowry, O.H., N.J. Rosebrough, A.I. FaIT and R.I. Randall. 1951. Protein measurement with Folin phenol reagent. J. BioI. Chem., 193, 256-275
  14. Park, J.D., C.H. Jung, J.S. Kim, D.M. Cho, M.S. Cho and Y.I. Choi. 2003a. Surimi processing using acid and alkali solubilization of fish muscle protein. J. Kor. Soc. Food Sci. Nutr., 32, 400-405 https://doi.org/10.3746/jkfn.2003.32.3.400
  15. Park, J.D., S.S. Yoon, C.H. Jung, M.S. Cho and Y.Y. Choi. 2003b. Effect of sarcoplasmic protein and NaCI on heating gel from fish muscle surimi prepared by acid and alkaline processing. J. Kor. Soc. Food Sci. Nutr., 32, 567-573 https://doi.org/10.3746/jkfn.2003.32.4.567
  16. Raymond, M.L. 1980. Studies concerning the determination of lysinoalanine in food proteins. J. Food Sci., 45, 56-59 https://doi.org/10.1111/j.1365-2621.1980.tb03869.x
  17. Savoie, L. and G. Parent. 1983. Susceptibility of protein fractions to lysinoalanine formation. J. Food Sci., 48, 1876-1877 https://doi.org/10.1111/j.1365-2621.1983.tb05108.x
  18. Undeland, I. S.D., Kelleher and H.O. Hultin. 2002. Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process. J. Agric. Food Chem., 50, 7371-7379 https://doi.org/10.1021/jf020199u
  19. Whitaker, J.R. and R.E. Feeney. 1977. Behavior of o-glycosyl and o-phosphoryl proteins in alkaline solution. In Advances in Experimental Medicine and Biology. Vol. 86B. Plenum Press, New York, 1-155
  20. Woodard, J.C. and M.T. Alvarez. 1967. Renal lesions in rat fed diets containing alpha protein. Arch Path., 84, 153-162
  21. Woodard, J.C. and D.D. Short. 1973. Toxicity of alkalitreated soy proteins in rats. J. Nutr., 103, 569-574 https://doi.org/10.1093/jn/103.4.569