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2001 | 08 | 2 |
Tytuł artykułu

Transglutaminaza i jej wykorzystanie w przemysle zywnosciowym

Treść / Zawartość
Warianty tytułu
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.
Wydawca
-
Rocznik
Tom
08
Numer
2
Opis fizyczny
s.5-16,bibliogr.
Twórcy
autor
  • Katedra Technologii Żywności, Akademia Rolnicza w Szczecinie, 71-459 Szczecin, ul. Papieża Pawia VI 3, bl. B
autor
  • 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.
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  • [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.
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  • [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.
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  • [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.
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  • [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.
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  • [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.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-article-908e23bc-8669-42c5-884d-048e9ab2716a
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