Surimi jelinin fiziksel özellikleri etkileyen faktörler

Surimi ticari olarak JeI oluşturma özelliğine sahip kıyılmış balık etinin rafine edilmiş halidir. Kas proteinlerinin {elleşmesi, bu ürünlerde istenen su ve doku stabilizasyonunu sağlar. Balık protein jelinin fiziksel özellikleri bazı faktörlerle etkilenir. Bunlar çiğ balığın özellikleri, yıkama ve arıtma, parçalama, ısı setting ve depolamadır. Bu derlemede, surimi tipi ürünlerde stabilizasyonu ve JeI formasyonunu etkileyen faktörler değerlendirilmiştir.

Factors affecting physical properties of surimi gel

Surimi products are minced and rafined fish meat which have gelling ability. Gelation of muscle proteins contributes to desirable texture and stabilization of water in muscle protein protein products. There are some factors which affect the pysical properties of fish protein gel. Theese factors are; condition of raw fish, washing and refining, comminuting and heat application and storage. In this review, factors affecting gel formation and stabilization in surimi type products were evaluated.

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  • ALVAREZ, C, COUSO, I and TEJADA, M. 1995. Sardine surimi gels as affected by salt concentration, blending, heat treatment and moisture, J. Food Sci. 60: 3, 622-626.
  • ALVAREZ, C, CÖUSO, I and TEJADA, M. 1999. Thermal gel degradation (modorn) in sardine surimi gels. J. Food Sci. 64:4,633-637.
  • CONNELL, J.J. 1961. The relative stability of the skeletal muscle myosin of some Animals. Biochem. J. 80:503-509.
  • GAO, J.C., PIGOTT, M.G. and RENIE, B. 1999. Gel forming additive effects on properties of thermally induced minced fish gel. J. Food Sci. 64: 3, 414-417.
  • JIANG, S.T; LEE, J.J and CHEN, HC. 1996. Proteolysis of actomyosin by cathepsins B, L, L-like and Xfrom mackarel(Scomber austrasicus). J. Agric. Food Chem. 44: 768-773.
  • JIANG, S.T; LEE, B.L; TSAO, C.Y. and LEE, J.J. 1997. Mackarel cathepsins B and L effects on thermal degradation of"surirni. J. Food Sci. 62: 2, 310-315.
  • KANG, I. S and LANIER, T.C. 1999. Bovine plazma protein functions in surimi gelation compared with cysteine protease inhibitors. J. Food Sci. 64: 5, 842-846.
  • KIMURA, I., MASAAKI, S., TOYODA, K., SEKİ, N., ARAI, K and FUJITA, T. 1991. A study on the cross-l Linking reaction of myosin in kamaboko "suwari" gels. Nip. Suis. Gak. 57:7, 1389-1396.
  • LANIER, T.C, LIN, T.S., HAMANN, D.D and THOMAS, F.B. 1981. Effects of alkaline protease in minced fish on texture of heat-processed Gels. J. Food Sci. 46:1643-1645
  • LEE, CM., 1984 Surimi process technology. Food Technol. 38:11, 69-80
  • LEE, CM- 1992. Factors affecting physical properties of fish protein gel, p. 43-68 In George R R Flick, JR; Roy E. Martin (Eds), Advances in Seafood Biochemistry, Composition and Quality, Technomic publishng Co, Lancaster, Basel.
  • LEE, H.G. and LANIER, T.C, 1995. The role of covalent linking in the texturizing of muscle protein sols. J. Muscle Foods 6:125-138.
  • LEE, H.G; LANIER, T.C; HAMANN, D.D and KNOPP. A. 1997. Transglutaminase Effects on low temperature gelation offish protein sols. J. Food Sci. 62:1, 20-24.
  • MARTIN, R. 1992. Surimi products, p. 377-391. In GEORGE R Flick, JR; ROY E. MARTIN (Eds), Advances in Seafood Biochemistry, Composition and Quality, Technomic publishing Co, Lancaster, Basel.
  • NIWA, E. 1992. Chemistry of surimi gelation p. 389-427. In T.C. Lanier and CM. Leed (Eds.), Surimi Technology, p. Marcel Dekker, New York.
  • PARK, W.J., KORHOREN, R.W. and LANIER, T.C. 1990 Effects of rigor mortis on gel-forming properties of surimi and unwashed mince prepared from tilapia. J. Food Sci. 55: 2, 353, 360.
  • PARK, J.W; LIN, T.M; YONNGSAWATDIGUL, J. 1997. New developments in manufacturing of surimi and surimi seafood.Food Rev. Int. 577-610.
  • PARSONS, N and KNIGTH, P. 1990, ORIGIN of variable extraction of myosin from myofibrils treated with salt and pyrophosphate. J.Sci. Food Agric. 51-71.
  • REPPOND, K.D., BABITT, J.K., BERNTSEN, S and TSURUTA, M. 1995. Gel properties of surimi from pacific herring. J.Food Sci. 69:4, 707,714.
  • ROUSSEL, H and CHEFTEL, C J. 1990. Mechanizms of gelation of sardine proteins: influence of thermal processing and various addtives on the texture and protein solubility of kamoboko gels. Int. J. Food Sci. Technol. 25: 260-280.
  • SAKAMOTO, H., KUMAZAWA, Y., TOIGUCHI S., SEGURO, K., SODEA, T and MOTOKI, M. 1995. Gel strength enhancement by addition of microbial transgulataminase during onshore surimi manufacture. J. Food Sci. 60:2,300-304.
  • SAKEI, H; WAKAMEDA, A., ICHIARA, Y and SASAMOTO, Y. 1989. Effect of CaCI2 on the elution of cross linking factor in Alaska Pollack. Nip. Suis. Gak. 55:1867-1869.
  • SEKİ, N., UNO, H., LEE, N-H; KIMURA, I., TOYODA, K., FUJITA, T and ARAI, K. 1990. Transglutaminase activity in Allaska pollock muscle and surimi and its reaction with myosin B. Nip Suis Gak. 56:125-132.
  • SHIMIZU, Y., MACHIDA, R and TAKENAMI, S. 1981. Spices variation in gel forming characteristics of fish meat paste. Nip.Suis. Gak. 47:95-104.
  • SHIMIZU, Y and KAGURI, A. 1986. Influence of death condition and freshness on the gel forming characteristics of fish meat paste. Nippon Suis. Gakkaishi vol. 52:1837-1841
  • SWAFFORD, T.C, BABBIT, J., REPPOND, K. and HARDY, A. 1985 SURIMI Process yield improvements and quality contribution by centrifuging. Proc. Intl. Symp. Eng. Seafood Incl. Surimi. National Fisheries Institute. P: 483.
  • THIEBAUD, M., DUMAY, E and CHEFTEL, J.C. 1996. Influence of process variables on the characteristics of a high moisture fish soy protein mix texturized by extrusion cooking Lebensm. Wiss U.- Technol., 29: 526-535.
  • TOYODA, K., KİMURA, I., FUJİTA, T., NOGUCHI, S.F., LEE, C. M. 1992. The surimi manufacturing process. In: LANIER,C.T. and LEE, M.C (eds.) Surimi Technology. Marcel Decker Inc. New York.
  • VISESSANGUAN, W., OGAWA, M., NAKAI, S and AN, H. 2000 Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin. J. Agric Food Chem. 48:1016-1023.
  • YANG, H and PARK, W.J. 1998. Effects of starch properties and thermal processing conditions on surimi-starch gels.Lebensm.-Technol, 31: 344-353.