Transglutaminaza i jej wykorzystanie w przemysle zywnosciowym

• Autorzy: Kolakowski E , Sikorski Z E
• Języki publikacji: PL

Abstrakty

PL

Omówiono występowanie i właściwości transglutaminazy (EC 2.3.2.13) z uwzględnieniem wpływu różnych czynników katalizujących lub inhibitujących reakcję sieciowania białek. Przedstawiono główne kierunki zastosowania transglutaminazy w przemyśle żywnościowym i wartość biologiczną białek modyfikowanych przy jej udziale.

EN

A description of incidence and properties of transglutaminase (EC 2.3.2.13) {TGase} is given with including of different catalytic or inhibitory factors effecting of protein crosslinking phenomenon The main appl.cat.ons of TGase in food industry and biological value of proteins modified by this enzyme are presented.

Słowa kluczowe

PL

wlasciwosci biochemiczne; wlasciwosci chemiczne; wartosc biologiczna; przemysl spozywczy; modyfikacja bialek; zywnosc; cechy sensoryczne; wykorzystanie; transglutaminazy

EN

biochemical property; chemical property; biological value; food industry; protein modification; food; sensory characteristics; utilization; transglutaminase

• Wydawca: -
• Czasopismo: Żywność Nauka Technologia Jakość
• Rocznik: 2001
• Tom: 08
• Numer: 2
• Opis fizyczny: s.5-16,bibliogr.

Twórcy

autor

Kolakowski E

• Katedra Technologii Żywności, Akademia Rolnicza w Szczecinie, 71-459 Szczecin, ul. Papieża Pawia VI 3, bl. B

autor

Sikorski Z E

• Katedra Technologii Utrwalania Żywności, Politechnika Gdańska, 80-952 Gdańsk, ul. G. Narutowicza 11/12

Bibliografia

• [1] Araki H., Seki N.: Comparison of reactivity of transglutaminase to various fish actomyosins. Bull. Japan. Soc. Sci. Fish., 59, 1993, 711.
• [2] Ashie I.N.A., Lanier T.C.: High pressure effects on gelation of surimi and turkey breast muscle enhanced by microbial transglutaminase. J. Food Sci., 64, 1999, 704.
• [3] Ashie I.N.A., Lanier T.C.: Transglutaminases in seafood processing. In: Seafood Enzymes. Utilization and Influence on Postharvest Seafood Quality. N. F. Haard and B. K. Simpson, eds, Marcel Dekker, New York and Basel, 2000, pp. 147.
• [4] Babiker E.F.E., Matsudomi N., Kato A.: Masking of antigen structure o f soybean protein by conjugation with polysaccharide and cross-linkage with microbial transglutaminase. Nahrung, 42, 1998, 158.
• [5] Casadio R., Polverini E., Mariani P., Spinozzi F., Carsughi F., Fontana A., Polverino de Laureto P., Matteucci G., Bergamini C.M.: The structural basis for the regulation of tissue transglutaminase. Eur. J. Biochem., 262, 1999, 672.
• [6] Colas B., Caer D., Fournier E.: Transglutaminase-catalysed glycosylation of vegetable proteins. Effect on solubility o f pea legumin and wheat gliadins. J. Agric. Food Chem. 41, 1993, 1811.
• [7] Fink M.L., Chung S.I., Folk J.E.: γ-Glutamylamine cyclotransferase: specificity toward ε-(L-γ-glutamyl)-L-lysine and related compounds. Proc. Natl. Acad. Sci. U.S.A., 77, 1980, 4564.
• [8] Gerrard J.A., Newberry M.P., Ross M., Wilson A.J., Fayle S.E., Kavale S.: Pastry lift and croissant volume as affected by microbial transglutaminase. J. Food Sci., 65, 2000, 312.
• [9] Ichihara Y., Wakameda A., Motoki M.: Fish meat paste products containing transglutaminase and their manufacture. Jpn. Kokai Tokkyo Koho, J.P. 02186961, 1990.
• [10] Imm J.Y., Lian P., Lee C.M.: Gelation and water binding properties o f transglutaminase-treated skim milk powder. J. Food Sci., 65, 2000, 200.
• [11] Jabłonowska I.: Wpływ czynników technologicznych na teksturowanie rozdrobnionego mięsa z leszcza metodą kierunkowego zamrażania. Praca doktorska. Akademia Rolnicza w Szczecinie, 2000.
• [12] Jiang S.T., Hsieh J.E., Ho M.I., Chung Y.C.: Combination effects o f microbial transglutaminase, reducing agent, and protease inhibitor on the quality of hairtail surimi. J. Food Sci., 65, 2000, 241.
• [13] Kamath M.: Investigation o f physicochemical basis for the unique „setting” phenomenon of Alaska pollock and Atlantic croaker surimi. Ph.D. Thesis. North Carolina State University. Raleigh, 1990, p. 113.
• [14] Kang I.J., Matsumura Y., Ikura K., Motoki M., Sakamoto H., Mori T.: Gelation and gel properties of soybean glycinin in a transglutaminase-catalyzed system. J. Agric. Food Chem., 42, 1994, 159.
• [15] Kishi H., Nozawa H., Seki N.: Reactivity of muscle transglutaminase on carp myofibryls and myosin B. Bull. Japan. Soc. Sci. Fish., 57, 1991, 1203.
• [16] Kołakowski E., Wianecki M., Bortnowska G., Bednarczyk B.: Use of proteolytic enzymes to improve freeze texturization of minced fish. W: Book o f Abstracts. 19th Intern. Congress of Refrigeration, The Hague, The Netherlands, August 20-25, 1995, 56.
• [17] Kołakowski E., Wianecki M., Bortnowska G., Jarosz R.: Trypsin treatment to improve freeze texturization of minced bream. J. Food Sci., 62, 1997, 737.
• [18] Kumazawa Y., Nakanishi K., Yasueda H., Motoki M.: Purification and characterization of transglutaminase from Walleye Pollack liver. Fisheries Sci., 62, 1996, 959.
• [19] Kurth L., Rogers P.J.: Transglutaminase catalyzed cross-linking of myosin to soya protein, casein and gluten. J. Food Sci., 49, 1984, 573.
• [20] Lauber S., Henle T., Klostermeyer H.: Relationship between the crosslinking of caseins by transglutaminase and the gel strength of yoghurt. Eur. Food Res. Technol., 210, 2000, 305.
• [21] Nio N., Motoki M., Takinami K.: Gelation of casein and soybean globulins by transglutaminase. Agric. Biol. Chem., 49, 1985, 2283.
• [22] Niwa E., Suzumura T., Nowsad AKM A. Kanoh S.: Setting of actomyosin paste containing few amount of transglutaminase. Bull. Japan. Soc. Sci. Fish., 59, 1993, 2043.
• [23] Nonaka M., Sakamoto H., Toiguchi S., Kawajiri H., Soeda T., Motoki M.: Sodium caseinate and skim milk gels formed by incubation with microbial transglutaminase. J. Food Sci., 57, 1992, 1214, 1241.
• [24] Nowsad A. AKM., Kanoh S., Niwa E.: Effects of amine salts on the elasticity of suwari gel from Alaska pollock. Bull. Japan. Soc. Sci. Fish., 59, 1993, 1017.
• [25] Nowsad A. AKM, Kanoh S., Niwa E.: Setting of transglutaminase-free actomyosin paste prepared from Alaska pollock surimi. Fisheries Sci., 60, 1994, 295.
• [26] Nowsad A. AKM., Katoh E., Kanoh S., Niwa E., 1996. Contribution of transglutaminase to the setting of fish pastes at various temperatures. Fisheries Sci., 62, 94.
• [27] Nury S., Meunier J.C., Mouranche A.: The kinetics of the thermal deactivation of transglutaminase from guinea-pig liver. Eur. J. Biochem., 180, 1989, 161.
• [28] Raczyński G., Snochowski M., Buraczewski S.: Metabolism of ε-(γ-L-glutamyl)-L-lysine in the rats. Br. J .N u tr .,34 ,1975,291.
• [29] Saeki H., Shoji T., Hirata F., Nonaka M., Arai K.: Effect of CaCl2 on gel forming ability and crosslinking reaction of myosin heavy chain in salt-ground meat of shipjack tuna, carp, and walleye pollock. Bull. Japan. Soc. Sci. Fish., 58,1992,2137.
• [30] Sakamoto H., Kumazawa Y., Motoki M.: Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. J. Food Sci., 59, 1994, 866.
• [31] Sarkar N.K., Clarke D.D., Waelsch H.: Enzymatically catalyzed incorporation of amines into proteins. Biochem. Biophys. Acta, 25, 1957, 451.
• [32] Tani T., Iwamoto K., Motoki M., Toiguchi S.: Manufacture of shark fin imitation food. Jpn. Kokai Tokkyo Koho, J.P. 02171160, 1990.
• [33] Tanimoto S.Y., Kinsella J.E.: Enzymatic modification of proteins: effects of transglutaminase crosslinking on some physical properties of β-lactoglobulin. J. Agric. Food Chem., 36, 1988, 281.
• [34] Traoré F., Meunier J.-C.: Cross-linking activity of placental F XIIIa on whey proteins and caseins. J. Agric. Food Chem., 40, 1992, 399.
• [35] Tsai G.-J., Lin S.-M., Jiang S.-T.: Transglutaminase from Streptoverticillium ladakanum and application to minced fish product. J. Food Sci., 61, 1996, 1234.
• [36] Tsukamasa Y., Shimizu Y.: Factors affecting the transglutaminase-associated setting phenomenon in fish meat sol. Bull. Japan. Soc. Sci. Fish., 57, 1991, 535.
• [37] Tsukamasa Y., Sato K., Shimizu Y., Imai Ch., Sugiyama M., Minegishi Y., Kawabata M.: ε-(γ- Glutamyl)lysine crosslink formation in sardine myofibril sol during setting at 25°C. J. Food Sci., 58, 1993, 785.
• [38] Wakameda A., Ichihara Y., Motoki M.: Transglutaminase-containing krill meat paste and its manufacture. Jpn. Kokai Tokkyo Koho, J.P. 02100654, 1990.
• [39] Wan J., Kimura I., Satake M., Seki N.: Effect of calcium ion concentration on the gelling properties and transglutaminase activity of walleye pollock surimi paste. Fisheries Sci., 60, 1994, 107.
• [40] Wan J., Miura J., Seki N.: Effect of monovalent cations on cross-linking of myosin heavy chain in suwari gel from walleye pollack. Bull. Japan. Soc. Sci. Fish., 58, 1992, 583.
• [41] Yildirim M., Hettiarachchy N.S.: Biopolymers produced by cross-linking soybean 1 IS globulin with whey proteins using transglutaminase. J. Food Sci., 62, 1997, 270.