Prevención de la desnaturalización proteica en actomiosina de jurel (Trachurus murphyi) durante su almacenamiento en congelación/Prevention of protein denaturation of jack mackerel actomyosin (Trachurus murphyi) during frozen storage
Restricted accessResearch articleFirst published online April, 1996
Prevención de la desnaturalización proteica en actomiosina de jurel (Trachurus murphyi) durante su almacenamiento en congelación/Prevention of protein denaturation of jack mackerel actomyosin (Trachurus murphyi) during frozen storage
Protein denaturation during frozen storage at -18 "C for 16 weeks was studied in jack mackerel (Trachurus murphyi) actomyosin. The cryoprotective effect of different additives was evaluated at a level of 8°/, (w/w): sucrose/sorbitol (1:1), maltodextrin 25 DE, milk whey and sodium lactate. The results were compared with a control sample without additives. The decrease in protein solubility and calcium ATPase activity confirmed that protein denaturation occurred both during the freezing process and during frozen storage. Higher losses were observed after one week at -18 °C. Sucrose/sorbitol and maltodextrin 25 DE were the best cryoprotectants. DSC thermograms showed two endothermic transitions with Tmax at 46.8 °C and 68.9 °C assigned to myosin and actin respectively. The best cryoprotective effect was achieved with sucrose/sorbitol and maltodextrin 25 DE. These additives showed Tmax and ΔH values for myosin and actin significantly higher than the control.
Akahane T., Chihara S., Niki P., Sano T., Tsuchiya T., Noguchi F. (1985) Differential scanning calorimetric studies on thermal behaviors of myofibrillar protein. Bull J Soc Sci Fish51: 1841-1846.
2.
Araya M. (1994) Estudio de la desnaturalización por congelación de las proteinas de jurel (Trachurus murphyi) y merluza (Merluccius gayi gayi). Tesis Facultad de Recursos Naturales. Escuela de Alimentos UCV, Valparaíso, Chile.
3.
Beas VE, Wagner JR, Cuprkin M., Anon MC ( 1990) Thermal denaturation of hake (Merluccius hubbsi) myofibrillar proteins. A differential scanning calorimetric and electrophoretic study. J Food Sci55: 683-687.
4.
Dondero M., Santibañez M., Tarky W., Curotto E., Canto M. (1989) Desnaturalización proteica en merluza (Merluccius gayi gayi) almacenada congelada. Rev Agroquím Tecnol Aliment29: 230-238.
5.
Dondero M., Yanez G., Curotto E., Canto M. (1991) Efecto de crioprotectores en surimi de jurel (Trachurus murphyi) durante el almacenamiento congelado. Rev Agroquim Tecnol Aliment31: 539-549.
6.
Dondero M., Carvajal P., Cifuentes A. (1994a). Efecto crioprotector del suero lácteo en surimi de jurel (Trachurus murphyi). Rev Esp Cienc Tecnol Aliment34: 285-300.
7.
Dondero M., Gandolfo M., Cifuentes A. (1994b) Efecto crioprotector de maltodextrina 25 DE, suero y mezcla de aditivos en surimi de jurel (Trachurus murphyi). Rev Esp Cienc Tecnol Aliment34: 389-408.
8.
Dyer W., French M., Snox J. ( 1950) Protein in fish muscle. I Extraction of protein fraction in fresh fish. J Fish Res Bd Canada7: 585-591.
9.
Fiske C., Subbarow Y. (1925) The colorimetric determination of phosphorus. J Biol Chem66: 375-400.
10.
Holmquist J., Buck E., Hultin H. (1984) Properties of Kamaboko made from red hake (Urophyssis chus) fillets, mince or surimi. J Food Sci49: 192-196.
11.
Howell B., Matthew A., Donnelly R. (1992) Thermal stability of fish myofibrils. A differential scanning calorimetric study. Int J Food Technol27: 283-295.
12.
Iguchi S., Tsuchiya T., Matsumoto J. (1981) Studies on the freeze denaturation of squid actomyosin . Bull Jap Soc Sci Fish47: 1499-1505.
13.
MacDonald GA, Lanier T. (1994) Actomyosin stabilization to freeze-thaw and heat denaturation by lactate salts. J Food Sci59: 101-105.
14.
Matsumoto J. (1980) Chemical deterioration of muscle protein during frozen storage. En: Advances in Chemistry Series 123 (Whitaker J, Jujimata M, eds.), pp. 95-124. Washington DC: American Chemical Society.
15.
Noguchi D. (1974) Studies on the control of denaturation of fish muscle protein during frozen storage. PhD Thesis, Sophia Univ. Tokio, Japón.
16.
Osnishi M., Tsuchiya T., Matsumoto J. (1978) Kinetic study on the denaturation mechanism of carp actomyosin during frozen storage. Bull Jap Soc Sci Fish44: 27-37.
17.
Park J., Lanier T., Keeton J., Hamman D. (1987) Use of cryo-protectants to stabilize functional properties of prerigor salted beef during frozen storage. J Food Sci52: 537-543.
18.
Poulter G., Ledward S., Godberg S., Hall G., Rawland B. (1985) Heat stability of fish muscle proteins. J Food Technol20: 203-217.
19.
Shenouda S. (1980) Theories of protein denaturation during frozen storage of fish flesh. Adv Food Res26: 275-307.
20.
Stabursvik R., Martens H. (1980) Thermal denaturation of proteins in post-rigor muscle tissue as studied by differential scanning calorimetry. J Sci Food Agric31: 1034-1042.
21.
Sych J., Lacroix C., Adambounou L., Castaigne F. (1990a) Cryoprotective effects of lactilol, palatinit and polidextrose on cod surimi proteins during frozen storage. J Food Sci55: 356-363.
22.
Sych J., Lacroix C., Adambounou L., Castaigne F. (1990b) Cryoprotective effects of some materials on cod surimi proteins during frozen storage. J Food Sci55: 123-126.
23.
Tsuchiya T., Nomomura Y., Matsumoto J. (1975) Prevention of freeze denaturation of carp actomyosin by sodium glutamate. J Biochem77: 853-862.
24.
Wagner J., Añon M. ( 1985) Effect of freezing on the denaturation of myofibrillar proteins. J Food Technol.20: 735-744.
25.
Wagner JR, Añon MC ( 1986) Effect of frozen storage on protein denaturation in bovine muscle. I. Myofibrillar ATPase activity and differential scanning calorimetric studies. J Food Technol21: 9-18.
26.
Wright D., Leach B., Wilding P. (1977) Differential scanning calorimetric studies of muscle and its constituents proteins. J Sci Food Agric28: 557-564.
