Effect of NaCl on gelation characteristics of acid- and alkali-treated pacific whiting fish protein isolates

Journal of Food Biochemistry

Volumn 31, Issue 4, 2007, Pages 427-455

  Thawornchinsombut, Supawan ^a   Park, Jae W ^a  

^a OREGON STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 34547450132     PISSN: 01458884     EISSN: 17454514     Source Type: Journal    
DOI: 10.1111/j.1745-4514.2007.00121.x     Document Type: Article

References (90)

1. AKAHANE, T. 1982. Freeze denaturation of fish muscle proteins. PhD Thesis, Sophia University, Tokyo, Japan.
2. AKAHANE, T., CHIHARA, S., YOSHIDA, Y., TSUCHIYA, T., NOGUCHI, S., OOKAMI, H. MATSUMOTO, J.J. 1984. Roles of constituent proteins in gel properties of cooked meat gels. Bull. Jpn. Soc. Sci. Fish. 50, 1029 1033.
3. ALIZADEH-PASDAR, N. LI-CHAN, E.C.Y. 2000. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescence probes. J. Agric. Food Chem. 48, 328 334.
4. ALUKO, R.E. YADA, R.Y. 1997. Some physicochemical and functional properties of cowpea (Vigna unguiculata) isoelectric protein isolate as a function of pH and salt concentration. Int. J. Food Sci. Nutr. 48 (1 31 39.
5. AN, H., WEERASINGHE, V., SEYMOUR, T.A. MORRISSEY, M.T. 1994. Cathepsin degradation of Pacific whiting surimi proteins. J. Food Sci. 59, 1013 1017, 1033.
6. BADII, F. HOWELL, N.K. 2002. A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) fillets during frozen storage. J. Sci. Food Agric. 82, 87 97.
7. BADII, F. HOWELL, N.K. 2003. Elucidation of the effect of formaldehyde and lipids on frozen stored cod collagen by FT-Raman spectroscopy and differential scanning calorimetry. J. Agric. Food Chem. 51, 1440 1446.
8. BAGSHAW, C.R. 1982. Muscle contraction, p. 38, Chapman & Hall, London, U.K.
9. BEAS, V.E., WAGNER, J.R., CRUPKIN, M. ANON, M.C. 1990. Thermal denaturation of hake (Merluccius hubbsi) myofibrillar proteins. A differential scanning calorimetric and electrophoretic study. J. Food Sci. 55, 683 687, 696.
10. BENJAKUL, S., VISESSANGUAN, W., ISHIZAKI, S. TANAKA, M. 2001. Differences in gelation characteristics of natural actomyosin from two species of Bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus. J. Food Sci. 66, 1311 1318.
11. BRADFORD, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248 254.
12. CARECHE, M., DEL MAZO, M.L., TORREJON, P. TEJADA, M. 1998. Importance of frozen storage temperature in the type of aggregration of myofibrillar proteins in cod (Gadus morhua). J. Agric. Food Chem. 46, 1539 1546.
13. CHANG, H.M., TSAI, C.F. LI, C.F. 1999. Changes of amino acid composition and lysinoalanine formation in alkali-pickled duck egg. J. Agric. Food Chem. 47, 1495 1500.
14. CHOI, Y.I. PARK, J.W. 2002. Acid-aided protein recovery from enzyme-rich Pacific whiting. J. Food Sci. 67, 2962 2967.
15. CORTES-RUIZ, J.A., PACHECO-AGUILAR, R., GARCIA-SANCHEZ, G. LUGO-SANCHEZ, M.E. 2001. Functional characterization of a protein concentrate from bristley sardine made under acidic conditions. J. Aquat. Food Prod. Technol. 10 (4 5 23.
16. DAMODARAN, S. 1996. Amino acids, peptides, and proteins. In Food Chemistry, 3rd Ed O.R. Fennema, ed.) pp. 321 429, Marcel Dekker, Inc., New York, NY.
17. DEL MAZO, M.L., TORREJON, P., CARECHE, M. TEJADA, M. 1999. Characteristics of the salt-soluble fraction of hake (Merluccius merluccius) fillets stored at -20 and -30 °C. J. Agric. Food Chem. 47, 1372 1377.
18. EGELANSDAL, B., FRETHEIM, K. HARBITZ, O. 1986a. Dynamic rheological measurements on heat-induced myosin gels: An evaluation of the method's suitability for the filamentous gels. J. Sci. Food Agric. 37, 944 954.
19. EGELANSDAL, B., FRETHEIM, K. SAMEJIMA, K. 1986b. Dynamic rheological measurements on heat-induced myosin gels: Effect of ionic strength, protein concentration and addition of adenosine triphosphate or pyrophosphate. J. Sci. Food Agric. 37, 915 926.
20. ESTURK, O. 2003. Characterization of rheological properties and thermal stability of fish myofibrillar proteins. PhD Thesis, Oregon State University, Corvallis, OR.
21. FERNANDEZ-MARTIN, F., PEREZ-MATEOS, M. MONTERO, P. 1998. Effect of pressure/heat combinations on blue whiting (micromesistius Micromesistius poutassou) washed mince: Thermal and mechanical properties. J. Agric. Food Chem. 46, 3257 3264.
22. FINK, A.L., CALCIANO, L.J., GOTO, Y., KUROTSU, T. PALLEROS, D.R. 1994. Classification of acid denaturation of proteins: Intermediates and unfolded states. 33, 12504 12511.
23. FOLK, J.E. 1980. Transglutaminases. Annu. Rev. Biochem. 49, 517 531.
24. FRIEDMAN, M. MASTERS, P.M. 1982. Kinetics of racemization of amino acid residues in casein. J. Food Sci. 47, 760 764.
25. FUJIMAKI, M., HARAGUCHI, T., ABE, K., HOMMA, S. ARAI, S. 1980. Specific conditions that maximize formation of lysinoalanine in wheat gluten and fish protein concentrate. Agric. Biol. Chem. 44, 1911 1916.
26. GODFREY, J.E. HARRINGTON, W.F. 1970a. Self-association in the myosin system at high ionic strength. I. Sensitivity of the interaction to pH and ionic environment. Biochemistry 9, 886 893.
27. GODFREY, J.E. HARRINGTON, W.F. 1970b. Self-association in the myosin system at high ionic strength. II. Evidence for the presence of monomer ↔ dimer equilibrium. Biochemistry 9, 894 908.
28. HAARD, N.F. 1992. Biochemical reactions in fish muscle during frozen storage. In Seafood Science and Technology E.G. Bligh, ed.) pp. 176 209, Fishing News Books, Cornwall, U.K.
29. HAMADA, M., ISHIZAKI, S. NAGAI, T. 1994. Variation of SH content and kamaboko-gel forming ability of shark muscle protein by electrolysis. J. Shimonoseki University of Fisheries 42, 131 135.
30. HAMM, R. 1970. Symposium: Phosphates in Food Processing, p. 65, AVI Publishing Co., Westport, CT.
31. HASKARD, C.A. LI-CHAN, E.C.Y. 1998. Hydrophobicity of bovine serum albumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANS-) fluorescent probes. J. Agric. Food Chem. 46, 2671 2677.
32. HASTINGS, R.J., RODGER, G.W., PARK, R., MATTHEWS, A.D. ANDERSON, E.M. 1985. Differential scanning calorimetry of fish muscle: The effect of processing and species variation. J. Food Sci. 50, 503 506, 510.
33. HERRERA, J.J., PASTORIZA, L. SAMPEDRO, G. 2001. A DSC study on the effects of various maltodextrins and sucrose on protein changes in frozen-stored minced blue whiting muscle. J. Sci. Food Agric. 81, 377 384.
34. HOWELL, B.K., MATTHEWS, A.D. DONNELLY, A.P. 1991. Thermal stability of fish myofibrils: A differential scanning calorimetric study. Int. J. Food Sci. Technol. 26, 283 295.
35. HSU, C.K., KOLBE, E.R., WANG, D.Q. MACDONALD, G.A. 1993. Comparison of physical, thermal and chemical methods to measure protein denaturation in frozen Pacific whiting (Merluccius productus). J. Aquat. Food Prod. Technol. 2 (2 31 49.
36. HULTIN, H.O. KELLEHER, S.D. 1999. Process for Isolating a Protein Composition from a Muscle Source and Protein Composition. U.S. Patent 6,005,073.
37. ISHIOROSHI, M., SAMEJIMA, K. YASUI, T. 1982. Further studies on the roles of the head and tail regions of the myosin molecule in heat-induced gelation. J. Food Sci. 47, 114 120, 124.
38. KIM, Y.S. 2002. Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditions. MS Thesis, Oregon State University, Corvallis, OR.
39. KIM, Y.S., PARK, J.W. CHOI, Y.J. 2003. New approaches for the effective recovery of fish proteins and their physicochemical characteristics. Fish. Sci. 69, 1231 1239.
40. KIM, Y.S., YONGSAWATDIGUL, J., PARK, J.W. THAWORNCHINSOMBUT, S. 2005. Characteristics of sarcoplasmic proteins and their interaction with myofibrillar proteins. J. Food Biochem. 29, 517 532.
41. KINSELLA, J.E., RECTOR, D.J. PHILLIPS, L.G. 1994. Physicochemical properties of proteins: Texturization via gelation, glass and film formation. In Protein Structure-Function Relationships in Food Y. Yada, R.L. Jackman, J.L. Smith, eds.) p. 14, Blackie Academic & Professional, London, U.K.
42. KRISTINSSON, H.G. HULTIN, H.O. 2003a. Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding. J. Agric. Food Chem. 51, 7187 7196.
43. KRISTINSSON, H.G. HULTIN, H.O. 2003b. Effect of low and high pH treatment on the functional properties of cod muscle proteins. J. Food Sci. 68, 917 922.
44. KRISTINSSON, H.G. HULTIN, H.O. 2003c. Role of pH and ionic strength on water relationships in washed minced chicken-breast muscle gels. J. Agric. Food Chem. 51, 5103 5110.
45. KRISTINSSON, H.G. HULTIN, H.O. 2004. Changes in trout hemoglobin conformations and solubility after exposure to acid and alkali pH. J. Agric. Food Chem. 52, 3633 3643.
46. LAEMMLI, U.K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680 685.
47. LAKEMOND, C.M., DE JONGH, H.H., HESSING, M., GRUPPEN, H. VORAGEN, A.G. 2000. Soy glycinin: Influence of pH and ionic strengtht on solubility and molecular structure at ambient temperatures. J. Agric. Food Chem. 48, 1985 1990.
48. LEBLANC, E.L. LEBLANC, R.J. 1992. Determination of hydrophobicity and reactive groups in proteins of cod (Gadus morhua) muscle during frozen storage. Food Chem. 43 (1 3 11.
49. LOWRY, O.H., ROSEBROUGH, N.J., FARR, A.L. RANDALL, R.J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265 275.
50. MAGA, J.A. 1984. Reviews: Lysinoalanine in foods. J. Agric. Food Chem. 32, 955 964.
51. MATSUMOTO, J.J. 1980. Chemical deterioration of muscle proteins during frozen storage. In Chemical Deterioration of Proteins J.R. Whitaker M. Fujimoto, eds ACS Symposium Series 123, American Chemical Society, Washington D.C.
52. MCGUFFEY, M.K. FOEGEDING, E.A. 2001. Electrostatic effects on physical properties of particulate whey protein isolate gels. J. Texture Studies 32, 285 305.
53. MONAHAN, F.J., GERMAN, J.B. KINSELLA, J.E. 1995. Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins. J. Agric. Food Chem. 43, 46 52.
54. MORRISSEY, M.T., WU, J.W., LIN, D. AN, H. 1993. Protease inhibitor effects on torsion measurements and autolysis of Pacific whiting surimi. J. Food Sci. 58, 1050 1054.
55. MYERS, C. 1988. Functional attributes of protein isolates. In Characterization of Protein F. Franks, ed.) pp. 491 549, Hamana Press, Totowa, NJ.
56. NAKAGAWA, T. 1978. Rheology, 2nd Ed., The Iwanami Shoten, Co., Tokyo, Japan.
57. OCKERMAN, H.W. 1980. Chemistry of Meat Tissue, pp. IX 3 4, The Ohio State University, Columbus, OH.
58. OGAWA, M., EHARA, T., TAMIYA, T. TSUCHIYA, T. 1993. Thermal stability of fish myosin. Comp. Biochem. Physiol. B: Comp. Biochem. 106, 517 521.
59. OWUSU-ANSAH, Y. HULTIN, H.O. 1987. Effect of in situ formaldehyde production on solubility and cross-linking of proteins of minced red hake muscle during frozen storage. J. Food Biochem. 11, 17 34.
60. PARK, J.W., LIN, T.M. YONGSAWATDIGUL, J. 1997. New development in manufacturing of surimi and surimi seafood. Food Rev. Int. 13, 577 610.
61. PEARSON, A.M. YOUNG, R.B. 1989. Muscle and Meat Biochemistry, p. 444, Academic Press, Inc., San Diego, CA.
62. PETERS, M., SEYMOUR, T., MORRISSEY, M.T. AN, H. 1995. Transglutaminase activity and Pacific whiting surimi processing. Presented at the IFT annual meeting. Abstract #54D-6. Anaheim CA.
63. PTITSYN, O.B. 1995. Molten globule and protein folding. Adv. Protein Chem. 47, 83 229.
64. REGENSTEIN, J.E., JAUREGUI, C.A. BAKER, R.C. 1983. The effect of pH, polyphosphates and different salts on water retention properties of ground trout muscle. J. Food Biochem. 8, 123 131.
65. RIDDLES, P.W., BLAKELEY, B.L. ZERNER, B. 1979. Ellman's reagent: 5,5′(-dithiobis(2-nitrobenzoic acid)-a reexamination. Anal. Biochem. 94 (1 75 81.
66. SAMEJIMA, K., ISHIOROSHI, M. YASUI, T. 1981. Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. J. Food Sci. 46, 1412 1418.
67. SANO, T., NOGUCHI, S.F., TSUCHIYA, T. MATSUMUTO, J.J. 1988. Dynamic viscoelasticity behavior of natural actomyosin and myosin during thermal gelation. J. Food Sci. 52, 924 928.
68. SANO, T., NOGUCHI, S.F., MATSUMUTO, J.J. TSUCHIYA, T. 1990a. Effect of ionic strength on dynamic viscoelasticity behavior of myosin during thermal gelation. J. Food Sci. 55, 51 54, 70.
69. SANO, T., NOGUCHI, S.F., MATSUMUTO, J.J. TSUCHIYA, T. 1990b. Thermal gelation characteristics of myosin subfragments. J. Food Sci. 55, 55 58, 70.
70. SANO, T., OHNO, T., OTSUKA-FUCHINO, H., MATSUMOTO, J.J. TSUCHIYA, T. 1994. Carp natural actomyosin: Thermal denaturation mechanism. J. Food Sci. 59, 1002 1008.
71. SHARP, A. OFFER, G. 1992. The mechanism of formation of gels from myosin molecules. J. Sci. Food Agric. 58, 63 73.
72. SHIKU, Y., HAMAGUCHI, P.Y., WENG, W.Y. TANAKA, M. 2005. Film-forming mechanism of biodegradable films prepared from fish myofibrillar proteins. J. Japan Soc. Food Sci. Technol. 52, 325 329.
73. SOEDA, T., SAKAI, T. TOIGUCHI, S. 1996. Studies of functionalities of microbial transglutaminase for food processing. III. Effects of microbial transglutaminase on the texture of surimi gels prepared from various kinds of fishes. Nippon Shokuhin Kagaku Kaishi. 43, 787 795.
74. STANLEY, D.W., STONE, A.P. HULTIN, H.O. 1994. Solubility of beef and chicken myofibrillar proteins in low ionic strength media. J. Agric. Food Chem. 42, 863 867.
75. SULTANBAWA, Y. LI-CHAN, E.C.Y. 2001. Structural changes in actomyosin and surimi from ling cod (Ophiodon elongates) during frozen storage in the absence and presence of cryoprotectants. J. Agric. Food Chem. 49, 4716 4725.
76. SUZUKI, T. 1981. Fish and Krill Protein: Processing Technology, pp. 31 34, Applied Science Publishers, London, U.K.
77. TAGUCHI, T., ISHIZAKA, H., TANAKA, M., NAGASHIMA, Y. AMANO, K. 1987. Protein-protein interaction of fish myosin fragments. J. Food Sci. 52, 1103 1104.
78. TANFORD, C. 1968. Protein denaturation. In Advances in Protein Chemistry, Vol 23 (C.B. Anfinsen, Jr., M.L. Anson, J.T. Edsall F.M. Richards, eds.) pp. 121 282, Academic Press, New York, NY.
79. TANFORD, C. 1980. The Hydrophobic Effect: Formation of Micelles and Biological Membranes, 2nd Ed., p. 233, John Wiley & Sons, Inc., New York, NY.
80. TEJADA, M., CARECHE, M., TORREJON, P., DEL MAZO, M.L.D., SOLAS, M.T., GARCIA, M.L. BARBA, C. 1996. Protein extracts and aggregates forming in minced cod (Gadus morhua) during frozen storage. J. Agric. Food Chem. 44, 3308 3314.
81. THAWORNCHINSOMBUT, S. PARK, J.W. 2004. Role of pH in solubility and conformational changes of Pacific whiting muscle proteins. J. Food Biochem. 28, 135 154.
82. THAWORNCHINSOMBUT, S. PARK, J.W. 2005. Role of ionic strength in biochemical properties of soluble fish proteins isolated from cryoprotected Pacific whiting mince. J. Food Biochem. 29, 132 151.
83. THAWORNCHINSOMBUT, S. PARK, J.W. 2006. Frozen stability of fish protein isolate under various storage conditions. J. Food Sci. 71, C227 C232.
84. THAWORNCHINSOMBUT, S., PARK, J.W., MENG, G. LI-CHAN, E.C.Y. 2006. Raman spectroscopy determines structural changes associated with gelation properties of fish proteins recovered at alkaline pH. J. Agric. Food Chem. 54, 2178 2187.
85. UNDERLAND, I., KELLERHER, S.D. HULTIN, H.O. 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.
86. VISESSANGUAN, W., OGAWA, M., NAKAI, S. AN, H. 2000. Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin. J. Agric. Food Chem. 48, 1016 1023.
87. WATANABE, K. KLOSTEMEYER, H. 1976. Heat-induced changes in sulfhydryl and disulfide levels of β-lactoglobulin A and formation of polymers. J. Dairy Res. 43, 411 418.
88. WEEDS, A.G. POPE, B. 1977. Studies on the chymotryptic digestion of myosin. Effect of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111, 129 157.
89. WU, M.C., AKAHANE, T., LANIER, L.C. HAMANN, D.D. 1985. Thermal transition of actomyosin and surimi prepared from Atlantic croaker as studied by differential scanning calorimetry. Food Chem. 50, 10 13.
90. YONGSAWATDIGUL, J. PARK, J.W. 2004. Effects of alkaline and acid solubilization on gelation characteristics of Rockfish muscle proteins. J. Food Sci. 69, 499 505.