IJCRR - 7(18), September, 2015
EFFECT OF SETTING ON THE PROPERTIES OF PROTEINS FROM THREADFIN BREAM (NEMIPTERUS JAPONICUS) FISH MINCE
Author: B. U. Supreetha, M. V. Chandra, B. A. Shamasundar
In the present investigation effect of setting on the properties of proteins and gel forming ability from threadfin bream (Nemipterus japonicus) fish mince has been assessed. The term setting refers to obtaining a soft elastic gel upon incubating the fish mince mixed with sodium chloride (NaCl) at less than 40 °C for a known duration. When the set meat is subjected to heat processing at 90 °C for 45 min, yields a gel with higher strength. The setting was carried out at a temperature at 35 °C for different durations. The gel strength of the gel obtained from set meat at 35 °C for 45 min was found to be 643.8 while obtained from unset meat was 264.5 g.cm. The setting of fish mince was accompanied by decrease in protein solubility, free-sulfhydryl content, Ca2+-ATPase
enzyme activity and viscosity.
Keywords: Threadfin bream mince, Setting and gel forming ability
B. U. Supreetha, M. V. Chandra, B. A. Shamasundar. EFFECT OF SETTING ON THE PROPERTIES OF PROTEINS FROM THREADFIN BREAM (NEMIPTERUS JAPONICUS) FISH MINCE International Journal of Current Research and Review. 7(18), September, 19-24
1. Benjakul S., Visessanguan W. and Pecharat, S. 2004. Suwari gel properties as affected by transglutaminase activator and inhibitors. Food Sci. Nutr., 22:27-107.
2. Binsi P. K. and Shamasundar B. A. 2012. Purification and characterisation of transglutaminase from four fish species: Effect of added transglutaminase on the viscoelastic behaviour of fish mince. Food Chem., 132 (4):1922-1929.
3. Ellman, G.L. 1959. Tissues sulfhydryl groups. Arch. Biochem. Biophys., 82: 70-77.
4. Laemmlli U.K., 1970. Cleavage of structural protein during assembly of the head bacteriophage T4. Nature., 227: 680-685.
5. Lanier T.C. 2000. Surimi gelation chemistry. In: J.W. (Ed) surimi and surimi seafood. Marcel Dekker , New York., pp 99-145.
6. Liu R., Zhao S., Xiong S., Xie B. and Liu H. 2007. Studies on fish and pork paste gelation by dynamic rheology and circular dichroism. J. Food Sci., 72: 399-403.
7. Lowry O.H., Rosebrough, N.J., Farr, A.L. and Randall R.J. 1951. Protein measurement with folin phenol reagent. J. Boil. Chem., 193(1): 256-275.
8. Niwa E., Nowsad, A.A and Kanoh, S. Changes in viscoelastic properties of salted fish flesh sol during its low temperature setting. Nippon suisan Gakk., 57 (12): 2333-2336.
9. Noguchi S. and Matsumoto, J. J. 1970. Studies on the control of the denaturation of the fish muscle proteins during the frozen storage. I. Preventive effect of Na–glutamate. Bull. Jap. Soc. Sci. Fish., 36: 1078-1087.
10. Nowsad A.K., K Anoh S and Niwa E.1997. Phscico-chemical protperites of a Suwari gel from Alaska Pollack surimi with iodoacetic acid added. Bull.Fac. Bioresources, Mie Univ.,13: 25- 31.
11. Roussel H. and Cheflel J.C. 1990. Mechanism of gelation of sardine protein influence of thermal processing and various additives on the texture and protein solubility of kamaboko gel. Int. J. Food Sci. Technol., 25: 260-280.
12. Samejima K., Ishioroshi, M., and 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.
13. Tausky H. H. and Shorr E. 1952. A micro colorimetric method for determination of inorganic phosphorous. J. Biol. Chem., 202: 675-685.
14. Xiang, D.S and Holley R.A. 2011. Factors influencing gel formation by myofibrillar proteins in muscle foods. Comprehensive Rev in Food Sci and Food Safety., 10: 33-51.
15. Yin T. and Park J.W . 2014. Effects of nano-scaled fish bone on the gelation properties of Alaska Pollock surimi. Food Chem., 150: 463-468.