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Research Article
 

Effect of pH-Shifting on Setting and Disintegrating Behaviors of Walleye Pollack Surimi



Fatema Hoque Shikha , Mohammed Ismail Hossain , Katsuji Morioka , Satoshi Kubota and Yoshiaki Itoh
 
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ABSTRACT

In order to study the effect of pH-shifting of meat on setting (suwari) at 30°C and disintegrating (modori) of fish meat at 60°C, the walleye pollack surimi whose pH was lowered to pH 6.0 and was readjusted to original pH were examined for different preheating time. At 30°C, acidified sample did not increase in gel strength with the prolongation of preheating time. Reneutralized sample (pH 7.2) increased in gel strength with the increase in preheating time, but the gel strength was weaker than that of the original sample. At 60°C, gel strength decreased with the lapse of preheating time irrespective of pH value. Acidified sample was much weak compared with the original sample and reneutralized sample was only a little stronger than the acidified sample. These results seem that the suwari was inhibited and modori was promoted, once the surimi was acidified. Then, the effect of pH-shifting to the activity of transglutaminase (TGase) and proteases in surimi, which are known to be related to the suwari and modori, respectively, were examined. Both of transglutaminase and protease activities in reneutralized surimi were the same level as that of the original surimi. These results confirmed that pH-shifting do not denature transglutaminase or protease, irreversively. Therefore, the decrease in gel strength by pH-shifting might be due to the denaturation of myosin itself which is known as the major protein in gel forming ability.

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  How to cite this article:

Fatema Hoque Shikha , Mohammed Ismail Hossain , Katsuji Morioka , Satoshi Kubota and Yoshiaki Itoh , 2005. Effect of pH-Shifting on Setting and Disintegrating Behaviors of Walleye Pollack Surimi. Pakistan Journal of Biological Sciences, 8: 1290-1297.

DOI: 10.3923/pjbs.2005.1290.1297

URL: https://scialert.net/abstract/?doi=pjbs.2005.1290.1297

REFERENCES
1:  Alvarez, C., I. Couso and M. Tejada, 1995. Sardine surimi gels as affected by salt concentration, blending, heat treatment and moisture. J. Food Sci., 60: 622-626.

2:  Shimizu, Y., 1990. Biochemical and Functional Properties of Material Fish. In: Engineered Seafood Including Surimi, Martin, R.E. and R.L. Collette (Eds.). Noyes Data Corporation, Park Ridge, New Jercy, pp: 143-161.

3:  Funatsu, Y. and K. Arai, 1991. The pH-dependence of changes in gel forming ability and myosin heavy chain of salt-ground meat from walleye pollack. Nippon Suisan Gakkaishi, 57: 1973-1980.

4:  Seki, N., H. Uno, N.H. Lee, I. Kimura, K. Toyota, T. Fujita and K. Arai, 1990. Transglutaminase activity in Alaska pollack muscle and surimi and its reaction with myosin B. Nippon Suisan Gakkaishi, 56: 125-132.

5:  Kimura, I., M. Sugimoto, K. Toyoda, N. Seki, K. Arai and T. Fujita, 1991. A study on the cross-linking reaction of myosin in kamaboko [email protected] gels. Nippon Suisan Gakkaishi, 57: 1389-1396.

6:  Wan, J., I. Kimura, M. Satake and N. Seki, 1994. Effect of calcium ion concentration on the gelling properties and transglutaminase activity of walleye pollack surimi paste. Fish. Sci., 60: 107-113.

7:  Takeda, H. and N. Seki, 1996. Enzyme-catalyzed cross-linking and degradation of myosin heavy chain in walleye pollack surimi paste during setting. Fish. Sci., 62: 462-467.

8:  Seki, N., H. Nozawa and S. Ni, 1998. Effect of transglutaminase on the gelation of heat-denatured surimi. Fish. Sci., 64: 959-963.
Direct Link  |  

9:  Makinodan, Y., H. Toyohara and S. Ikeda, 1984. Comparison of muscle proteinase activity among fish species. Comp. Biochem. Physiol., 79: 129-134.
PubMed  |  Direct Link  |  

10:  Barrett, A.J. and J.K. McDonald, 1980. Mammalian Proteinases: A Glossary and Bibliography. Academic Press, London, UK.

11:  Siebert, G., 1958. Protein-spliting enzyme activity of fish flesh. Experimentia, 14: 65-66.

12:  Anonymous, 1998. Official Methods of Analysis. 4th Revision, 16th Edn., Association of Official Analytical Chemists, Washington, DC., pp: 9-10.

13:  Shimizu, Y., R. Machida and S. Takenami, 1981. Species variations in the gel-forming characteristics of fish meat paste. Nippon Suisan Gakkaishi, 47: 95-104.

14:  Weber, K. and M. Osborn, 1969. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem., 244: 4406-4412.
PubMed  |  Direct Link  |  

15:  Kanoh, S., A.K.M. Nowsad, T. Suzumura and E. Niwa, 1993. Setting of actomyosin paste containing few amount of transglutaminase. Nippon Suisan Gakkaishi, 59: 2043-2046.
Direct Link  |  

16:  Tsukamasa, Y., Y. Miyake and M. Ando and Y. Makinodan, 2002. Total activity of transglutaminase at various temperatures in several fish meats. Fish. Sci., 68: 929-933.
Direct Link  |  

17:  Alvarez, C. and M. Tejada, 1997. Influence of texture of suwari gels on kamaboko gels made from sardine (Sardina pilchardus) surimi. J. Sci. Food Agric., 75: 472-480.
Direct Link  |  

18:  Ishizaki, S., K. Endo, W.L. Lin, M. Tanaka, T. Taguchi and K. Amano, 1994. Thermal gel formation of air-blown dish muscle actomyosin. Nippon Shokuhin Kogyo Gakkaishi, 41: 355-357.

19:  Toyohara, H. and Y. Shimizu, 1988. Relation between modori phenomenon and myosin heavy chain breakdown in threadfin-bream gel. Agric. Biol. Chem., 52: 255-257.
Direct Link  |  

20:  Boye, S.W. and T.C. Lanier, 1988. Effect of heat stable alkaline protease activity of Atlantic menhaden (Brevoorti tyrannus) on surimi gel. J. Food Sci., 53: 1340-1342.

21:  Greene, D.H. and J.K. Babbitt, 1990. Control of muscle softening and protease-parasite interactions in arrowtooth flounder Atheresthes stomias. J. Food Sci., 55: 579-580.
Direct Link  |  

22:  Toyohara, H., T. Sakata, K. Yamashita, M. Kinoshita and Y. Shimizu, 1990. Degradation of oval-filefish meat caused by myofibrillar proteinase(s). J. Food Sci., 55: 364-368.
Direct Link  |  

23:  Kim, S.H., J.A. Carpenter, T.C. Lanier and L. Wicker, 1993. Polymerization of beef actomyosin induced by transglutaminase. J. Food. Sci., 58: 473-476.
CrossRef  |  

24:  Kamath, G.G., T.C. Lanier, E.A. Foegeding and D.D. Hamann, 1992. Non-disulfide covalent cross-linking of myosin heavy chain in setting of Alaska pollack and Atlantic croaker surimi. J. Food Biochem., 16: 151-172.
Direct Link  |  

25:  Tsukamasa, Y. and Y. Shimizu, 1990. Setting property of sardine and pacific mackerel meat. Nippon Suisan Gakkaishi, 56: 1105-1112.

26:  Nishimoto, S., A. Hashimoto, N. Seki, I. Kimura, K. Toyoda, T. Fujita and K. Arai, 1987. Influencing factors on changes in myosin heavy chain and jelly strength of salted meat paste from Alaska polack during setting. Nippon Suisan Gakkaishi, 53: 2011-2020.

27:  Nowsad, A.K.M., S. Kanoh and E. Niwa, 1995. Contribution on transglutaminase on the setting of various actomyosin paste. Fish. Sci., 61: 79-81.

28:  Seguro, K., Y. Kumazawa, T. Ohtsuka, S. Toiguchi and M. Motoki, 1995. Microbial transglutaminase and ε-(γ-glutamyl) lysine cross-link effects of elastic properties of kamaboko gels. J. Food Sci., 60: 305-311.
Direct Link  |  

29:  Jiang, S.T., M.L. Ho, S.H. Jiang and H.C. Chen, 1998. Purified NADPH-sulphate reductase from Saccharomyces cerevisiae effects on quality of ozonated mackerel surimi. J. Food Sci., 63: 777-781.
Direct Link  |  

30:  Lanier, T.C., 2000. Surimi Gelation Chemistry. In: Surimi and Surimi Seafood, Park, J.W. and M. Dekker (Eds.). Basel, New York, pp: 237-265.

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