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http://dx.doi.org/10.3746/jkfn.2004.33.10.1668

Gelation Properties and Industrial Application of Functional Protein from Fish Muscle-1. Effect of pH on Chemical Bonds during Thermal Denaturation  

Jung, Chun-Hee (경상대학교 해양생물이용학부/해양산업연구소)
Kim, Jin-Soo (경상대학교 해양생물이용학부/해양산업연구소)
Jin, Sang-Keun (국립진주산업대학교 동물소재공학과)
Kim, Il-Suk (국립진주산업대학교 동물소재공학과)
Jung, Kyoo-Jin (남도대학 식품공학과)
Choi, Yeung-Joon (경상대학교 해양생물이용학부/해양산업연구소)
Publication Information
Journal of the Korean Society of Food Science and Nutrition / v.33, no.10, 2004 , pp. 1668-1675 More about this Journal
Abstract
The effect of pH on surface hydrophobicity, sulfhydryl group, infrared spectrum, SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) pattern and enthalpy was investigated in recovered protein from mackerel and frozen blackspotted croaker by alkaline processing. Hydrophobic residue in myofibrillar protein exposed to the surface of protein, and hydrophobic interaction were the highest around 6$0^{\circ}C$. The surface hydrophobicity was different between myofibrillar protein and myofibrillar protein including sarcoplasmic protein (recovered protein). The peak at 1636 c $m^{-l}$ was increased with pH, and the recovered protein was unfolded in alkali pH. Difference of surface and total sulfhydryl group at pH 7.0 and 10 was comparative high, and decrease of surface sulfhydryl group indicated formation of S-S bonds. Mackerel and frozen blackspotted croaker in alkaline pH showed bands of polymerized myosin heavy chain on SDS-PAGE pattern. The transition temperatures of recovered protein were 33.1, 44.3 and 65.5$^{\circ}C$. Gelation of recovered protein from alkali processing was estimated by increase of $\beta$-sheet structure by pH treatment, S-S bonds by oxidation of surface sulfhydryl group in heating, polymerization of myosin heavy chain in order.r.
Keywords
recovered fish protein; alkaline processing; thermal denaturation;
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  • Reference
1 Chang H-S, Feng Y, Hultin HO. 2001. Role of pH in gel formation of washed chicken muscle at low ionic strength. J Food Biochemistry 25: 439-457   DOI   ScienceOn
2 Xiong YL. 1997. Structure-function relationships of muscle proteins. In Food Proteins and Their Applications. Damodaran S, Paraf A, eds. Marcel Dekker, Inc, New York. p 341-392
3 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
4 Kristinsson HG, Hultin HO. 2003. Role of pH and ionic strength on water relationships in washed minced chicken- breast muscle gels. J Food Sci 68: 917-922   DOI   ScienceOn
5 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   DOI   ScienceOn
6 Park JD, Yoon S-S, Jung C-H, Cho MS, Choi YJ. 2003. Effect of sarcoplasmic protein and NaCl on heating gel from fish muscle surimi prepared by acid and alkaline processing. J Korean Soc Food Sci Nutr 32: 567-573   DOI   ScienceOn
7 Bouraoui M, Nakai S, Li-Chan E. 1997. In situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy. Food Research International 30: 65- 72   DOI   ScienceOn
8 Krishnamurthy G, Chang H-S, Hultin HO, Feng Y, Srinivasan S, Kelleher SD. 1996. Solubility of chicken breast muscle proteins in solutions of low ionic strength. J Agric Food Chem 44: 408-415   DOI   ScienceOn
9 Lanier TC. 1987. Muscle protein functional properties and protease content of surimi prepared from fatty, dark-fleshed fish species. In Fatty fish utilization: upgrading from feed to food. Proceedings of a national technical conference in Raleigh. NC, USA. p 247-262
10 Snow GW. 1992. Development of under-utilized species in Atlantic Canada. In Seafood science and technology. Bligh EG, ed. Fishing News Books, Cambridge, MA, USA. p 149-153
11 Beas VE, Wagner JR, Crupkin M, Anon MC. 1990. Thermal denaturation of hake (Merluccius hubbsi) myofibrillar proteins. A differential scanning calorimetric and electrophoretic study. J Food Sci 55: 683-687, 696   DOI
12 Lanier TC. 1992. Measurement of surimi composition and functional properties. In Surimi Technology. Lanier TC, Lee CM, eds. Marcel Dekker Inc, New York. p 123-163
13 Roura S, Saavedra JP, Truco R, Crupkin M. 1992. Conformational change in actomyosin from post-spawned hake stored on ice. J Food Sci 57: 1109-1111   DOI
14 Choi YJ, Park JW. 2002. Acid-aided protein recovery from enzyme-rich Pacific whiting. J Food Sci 67: 2962-2967   DOI   ScienceOn
15 Li-Chan E, Nakai S. 1991. Raman spectroscopic study of thermally and/or dithiothreitol induced gelation of lysozyme. J Agric Food Chem 39: 1238-1245   DOI
16 Ogawa M, Nakamura S, Horimoto Y, An H, Tsuchiya T, Nakai S. 1999. Raman spectroscopic study of changes in fish actomyosin during setting. J Agric Food Chem 47: 3309-3318   DOI   ScienceOn
17 JMP. 2002. Statistics and graphics guide. SAS Institute, Cary, NC, USA
18 Sano T, Ohno T, Otsuka-Fuchino H, Matsumoto JJ, Tsuchiya T. 1994. Carp natural actomyosin: Thermal denaturation mechanism. J Food Sci 59: 1002-1008   DOI   ScienceOn
19 Itoh Y, Yoshinaka R, Ikeda S. 1979. Behavior of the sulfhydryl groups of carp actomyosin by heating. Nippon Suisan Gakkaishi 45: 1019-1022   DOI
20 Niwa E, Mori H, Nakayama T, Hamada I. 1986. Contribution of SS bonding to fish flesh gel. Nippon Suisan Gakkaishi 52: 1103   DOI
21 Kimura I, Sugimoto M, Toyoda K, Seki N, Arai K, Fujita T. 1991. A study on the cross-linking reaction of myosin in Kamaboko 'suwari' gels. Nippon Suisan Gakkaihsi 57: 1389-1396   DOI
22 Margoshes BA. 1990. Correlation of protein sulfhydryls with the strength of heat formed egg white gels. J Food Sci 55: 1753-1756   DOI
23 Chawla SP, Venugopal V, Nair PM. 1996. Gelation of proteins from washed muscle of threadfin bream (Nemipterus japonicus) under mild acidic conditions. J Food Sci 61: 362-366, 371   DOI   ScienceOn
24 Hossain MI, Itoh Y, Morioka K, Obtatake A. 2001. Inhibiting effect of polymerization and degradation of myosin heavy chain during preheating at 30oC and 50oC on the gel- forming ability of walleye pollack surimi. Fisheries Science 67: 718-725   DOI   ScienceOn
25 Akahane T, Chihara S, Niki TP, Sano T, Tsuchiya T, Noguchi SF. 1985. Differential scanning calorimetric studies on thermal bahaviors of myofibrillar proteins. Nippon Suisan Gakkaishi 51: 1841-1846   DOI
26 Iso N, Mizuno H, Ogawa H, Mochizuki Y, Masuda N. 1991. Differential scanning calorimetry on fish meat paste. Nippon Suisan Gakkaishi 57: 337-340   DOI
27 Ellman GL. 1959. Tissue sulfhydryl groups. Arch Biochem Biophys 82: 70-77   DOI   ScienceOn
28 Laemmli UK. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227: 680-685   DOI   ScienceOn