Transglutaminases - a review with special reference to microbial transglutaminase and its application in food processing
Published:
Nov 30, 2017
Keywords:
Transglutaminase proteins food processing
Abstract
Some properties and applications of the transglutaminase (TG), with particular focus on TG derived from microorganisms (MTG), are described. TG catalyzes an acyltransfer reaction in which the γ-carboxyamide groups of pep tidebound glutamine residues are the acyl-donors. Most food proteins, such as legume globulins, wheat gluten and gliadin, egg yolk and egg white proteins, meat actins and myosins, gelatin, collagen, milk caseins, a-lactalbumin and /Mactoglobulin, could be crosslinked by TG. TG are present in an extremely broad spectrum of living organisms, such as humans, most advanced animals, birds, amphibians, fish, plants and microorganisms. Commercial TG has been merely obtained from animal tissues for decades. The limited supply and the complicated separation and purification procedure for obtaining tissue TG have resulted in an extremely high price of the enzyme, which hampers a wide application in food processing. MTG, mass-produced at low cost by fermentation, catalyses the cross-linking of most food proteins through the formation of c-(v-glutamyl) lysine bonds, in the same way as wellknown mammalian enzymes. However, MTG is quite unique from other mammalian TG, since it is totally independent of Ca + and has a relatively lower molecular weight. The results of many studies suggest that MTG has many potential applications in food processing. Food treated with MTG appeared to have an improved flavour, appearance and texture. In addition, this enzyme can increase shelf-life and reduce allergenicity of certain foods. Using additional components, such as sodium ceseinate, maltodextrine and starch, MTG can be customized for use in many other foods, even those with lower protein content. In this respect, MTG technology will be an essential tool for producing acceptable protein foods from non-animal proteins in the future.
Article Details
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TZIKAS (Ζ. ΤΖΗΚΑΣ) Z., & AMBROSIADIS (Ι. ΑΜΒΡΟΣΙΑΔΗΣ) I. (2017). Transglutaminases - a review with special reference to microbial transglutaminase and its application in food processing. Journal of the Hellenic Veterinary Medical Society, 56(4), 311–324. https://doi.org/10.12681/jhvms.15091
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- Vol. 56 No. 4 (2005)
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- Review Articles
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References
Aeschlimann D, Paulsson M (1994) Transglutaminases: Protein cross-linking enzymes in tissues and body fluids. Thromb Haemost, 71(4):402-415
Ajinomoto (2004) Food Ingredients Division-Activa™ TG: http://www.ajinomoto-usa.com/old/f2act06.htm
An H, Peters MY, Seymour TA (1996) Roles of endogenous enzymes in surimi gelation. Trends Food Sci Techn, 7:321-327
Ando H, Adachi M, Umeda Κ, Matsuura A, Nonaka M, Uchio R, Tanaka H, Motoki M (1989) Purification and characteristics of a novel transglutaminase derived from microorganims. Agric Biol Chem, 53:2613-2617
Armbrust C, Werlein HD, Watkinson BM (2003) Transglutaminase - Application and properties in fish products. Deutsc Lebensmit- Rundsc, 99(5):181-187
Ashie INA, Lanier TC (1999) High pressure effects on gelation of surimi and turkey breast muscle enhanced by microbial transglutaminase. J Food Sci, 64(4):704-708
Bauer N, Koehler P, Wieser H, Schieberle Ρ (2003α) Studies on effects of microbial transglutaminase on gluten proteins of wheat. I. Biochemical analysis. Cereal Chem, 80(6):781-786
Bauer N, Koehler P, Wieser Η, Schieberle Ρ (2003β) Studies on effects of microbial transglutaminase on gluten proteins of wheat. II. Rheological properties, Cereal Chem, 80(6):787-790
Beltran-Lugo AI, Maeda-Martinez AN, Pacheco-Aguilar R, Nolasko-Soria WG, Ocano-Higuera VM (2005) Physical, textural and microstructural properties of restructured adductor muscles of 2 scallop species using 2 cold-binding systems. J Food Sci, 70(2):E78-E84
Bernard BK, Tsubuku S, Shioya S (1998) Acute toxicity and genotoxicity studies of a microbial transglutaminase. Inter J Toxicol, 17: 703-721
Bishop PD, Teller DC, Smith RA (1990) Expression, purification and characterization of human factor XIII in Saccharomyces cerevisiae. Biochem, 29(7):1861-1869
Chanyongvorakul Y, Matsumura Y, Nonaka M, Motoki M, Mori Τ (1995) Physical properties of soybean and broad bean US globulin gels formed by transglutaminase reaction. J Food Sci, 60(3):483-488
Claparols MI, Bassie L, Miro Β, Duca SD, Rodriguez-Montesinos J, Christou P, Serafini-Fracassini D, Capell Τ (2004) Transgenic rice as a vehicle for the production of the industrial enzyme transglutaminase. Transg Research, 13:195-199
Collar C, Bollain C (2004) Impact of microbial transglutaminase on the viscoelastic profile of formulated bread doughs. Europ Food Resear Techn, 218(2):139-146
Collar C, Bollain C, Angioloni A (2005) Significance of microbial transglutaminase on the sensory, mechanical and crumb grain pattern of enzyme supplemented fresh pan breads. J Food Engin, 70(4):479-488
Colmenero FJ, Ayo MJ, Carballo J (2005) Physicochemical properties of low sodium frankfurter with added walnut: effect of transglutaminase combined with caseinate, KCL and dietary fibre as salt replacers. Meat Sci, 69(4):781-788
Date M, Yokoyama Kl, Umezawa Y, Matsui H, Kikuchi Y (2003) Production of native-type Streptoverticillium mobaraense transglutaminase in Corynebacterium glutamicum. Appi Environ Microbiol, 69(5):3011-3014
DeBacker-Royer C, Traore F, Meunier C (1992) Purification and properties of factor XIII from human placenta. Intrer J Biochem, 24:91-97
De Jong GAH, Wijngaards G, Koppelman SJ (2003) Transglutaminase inhibitor from milk. J Food Sci, 68(3):820-825
Del Duca S, Beninati S, Serafini- Fracassini D (1995) Poly amines in chloroplasts: identification of their glutamyl and acetyl derivatives. Biochem J, 305:233-237
Dickinson E, Yamamoto Y (1996) Rheology of milk protein gels and protein-stabilized emulsion gels cross-linked with transglutaminase. J Agric Food Chem, 44:1371-1377
Dimitrakopoulou MA, Ambrosiadis JA, Zetou FK, Bloukas JG (2005) Effect of salt and transglutaminase (TG) level and processing conditions on quality characteristics of phosphatefree, cooked, restructured pork shoulder. Meat Sci, 70:743-749
Eissa AS, Bisram S, Khan SA (2004) Polymerization and gelation of whey protein isolates at low pH using transglutaminase enzyme. J Agric Food Chem, 52(14):4456-4464
Enzyme Nomenclature (1992) Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, (eds) Academic Press, San Diego, California, USA
Fan JF, Saito M, Yanyan Ζ, Szesze Τ, Wang LJ, Tatsumi E, Li LT (2005) Gel-forming ability and radical scavenging activity of soy protein hydrolysate treated with transglutaminase. J Food Sci, 70(1):C87-C92
Farnsworth J, Hendricks G, Gotcheva V, Akuzawa R, Guo M (1992) Effects of enzymatic crosslinking on the consistency and structure of probiotic goat milk yogurt. J Anim Sci, Vol 80, Suppl 1/ J Dairy Sci, Vol 85, Suppl 1
Fink ML, Chung SI, Folk JE (1980) γ-glutamine cyclotransferase: specifity toward e-(Y-Glutamyl)-L-Lysine and related compounds. Proc Natl Acad Sci, 77:4564-4568
Folk JE (1980) Transglutaminases. Annu Rev Biochem, 49:517-531
Gerber U, Jucknischke U, Putzien S, Fuchsbauer H (1994) A rapid and simple method for the purification of transglutaminase from Streptoverticillium mobaraense. Biochem J, 299:825-829
Gerrard JA (2002) Protein-protein crosslinking in food: methods, consequences, applications. Trends Food Sci Techn, 13:391-399
Gilleland MG, Lanier TC, Hamann DD (1997) Covalent bonding in pressure-induced fish protein gels. J Food Sci, 62:713-716
Gomez-Guillen MC, Monterò Ρ, Solas MT, Perez-Mateos M (2005) Effect of chitosan and microbial transglutaminase on the gel forming ability of horse mackerel {Trachurus spp.) muscle under high pressure. Food Resear Inter, 38(1):103-110
Griffin M, Casadio R, Bergamini CM (2002) Transglutaminases: Nature's biological glues. Biochem J, 368:377-396
Gujral HS, Roseli CM (2004) Functionality of rice flour modified with a microbial transglutaminase. J Cereal Sci, 39(2):225-230
Hammer GF (1998) Microbial transglutaminase and diphosphate in finely comminuted cooked sausage. Fleischwirt, 78(11) : 1155-1162
Han XQ, Pfeifer JK, Lincourt RH, Schuerman JM (2003) Process for making a cheese product using transglutaminase. US Patent and Trademark Office: http://appft.uspto.gov/netacgi/nph-Parser? Sectl
Hozova B, Kukurova I, Dodok L (2003) Application of transglutaminase and fermizyme for sensory quality improvement of pastry. Nahrung-Food, 47(3):171-175
Icekson I, Apelbaum A (1987) Evidence for transglutaminase activity in plant tissue. Plant Physiol, 84:972-974
Ichihara Y, Wakameda A, Motoki M (1990) Fish meat pasteproducts containing transglutaminase and their manufacture. Jpn Kokai Tokkyo Koho JP, 02186961
Ichinose A, Hendrickson LE, Fujikawa Κ, Davie EW (1986) Amino acid sequence of the subunit of human factor XIII. Biochem, 25:6900-6906
Ikeda M, Nakagawa S (2003) The Corynebacterium glutamicum genome: features and impacts on biotechnological processes. Appi Microbiol Biotechnol, 62:99-109
Ikura K, Nasu T, Yokota H, Tsuchiya Y, Sasaki R, Chiba Η Κ (1988) Amino acid sequence of guinea pig liver transglutaminase from its cDNA sequence. Biochem, 27:2898-2905
Jarmoluk A, Pietrasik Ζ (2003) Response surface methodology studyon the effects of blood plasma, microbial transglutaminase and κ-carrageenan on pork batter gel properties. J Food Eng, 60:327-334
Jiang ST, Leu SZ, Tsai GJ (1998) Cross-linking of mackerel surimi actomyosin by microbial transglutaminase and ultraviolet irradiation. J Agric Food Chem, 46:5278-5282
Jiang ST, Hsieh JF, Ho ML, Chung YC (2000) Microbial transglutaminase affects gel properties of golden threadfinbream and pollack surimi. J Food Sci, 65(4):694-699
Kanaji T, Ozaki H, Takao T, Kawajiri H, Ide H, Motoki M, Shimonishi Y (1993) Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112. J Biol
Chem, 268(16):11565-11572
Kang H, Cho Y (1996) Purification and properties of transglutaminase from soybean {Glycine max) leaves. Biochem Biophys Res Commun, 223:288-292
Kashiwagi T, Yokoyama K, Ishikawa K, Ono K, Ejima D, Matui H (2002) Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense. J Biol Chem, 277(46) :44252-44260
Kato A, WadaT, Kobayashi K, Seguro K, Motoki M (1991) Ovomucin-food protein conjugates prepared through the transglutaminase reaction. Agric Biol Chem, 55:1027-1031
Kikuchi Y, Date M, Yokoyama Kl, Umezawa Y, Matsui H (2003) Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterìum glutamicum: processing of the pro-domain by a co-secreted subtilisin-like from Streptomyces albogrìseolus. Appi Environ Microbiol, 69(l):358-366
Kilic Β (2003) Effect of microbial transglutaminase and sodium caseinate on quality of chicken doner kebab. Meat Sci, 63:417-421
Kolle DS, Savell JW (2003) Using Activa™ TG-RM to bind beef muscles after removal of excessive seam fat between the m.longissimus thoracis and m. spinalis dorsi and heavy connective tissue from within the m. infraspinatus. Meat Sci, 64:27-33
Kolodziejska I, Kaczorowski K, Piotrowska B, Sadowska M (2004) Modification of the properties of gelatin from skins of Baltic cod (Gadus morhua) with transglutaminase. Food Chem, 86:203-209
Krämer R (1994) Secretion of amino acids by bacteria: physiology and mechanism. FEMS Microbiol Rev, 12:75-94
Kumazawa Y, Seguro K, Takamura M, Motoki M (1993) Formation of 8-(Y-Glutamyl)lysine cross-link in cured horse mackerel meat induced by drying. J Food Sci, 58(5):1062-1064
Kumazawa Y, Sakamoto H, Kawajiri H, Seguro K, Motoki M (1996) Determination ε-(γ-Glutamyl) lysine in several fish eggs and muscle proteins. Fish Sci, 62:331-332
Kuraishi C, Sakamoto J, Soeda Τ (1996) The usefulness of transglutaminase for food processing. In: Biotechnology for improved foods and flavors, Takeoka GR, Teranishi R, Williams PJ, Kobayashi A (eds), ACS symposium series 637,:29-38
Kuraishi C, Sakamoto J, Yamazaki Κ, Susa Y, Kuhara C, Soeda Τ (1997) Production of restructured meat using microbial transglutaminase without salt or cooking. J Food Sci, 62(3):488-490
Kuraishi C et al. (2001) Transglutaminase: its utilization in the food industry. Food Rev Inter, 17:221-246
KDtemeyer C, Froeck M, Werlein HD, Watkinson BM (2005) The influence of salts and temperarure on enzymatic activity of microbial transglutaminase. Food Cont, 16(8):735-737
Kwan SW, Easa AM (2003) Comparing physical properties of retortresistant glucono-delta-lactone tofu treated with commercial transglutaminase enzyme or low levels of glucose. Lebensmit- Wissensc Techn- Food Sci Techn, 36(6):643-646
Lauber S, Krause I, Klostermeyer H, Henle Τ (2003) Microbial transglutaminase crosslinks beta-casein and beta-lactoglobulin to eterologus oligomers under high pressure. Europ Food Res Techn, 216(1):15-17
Lee HG, Lanier TC, Hamann DD, Knopp JA (1997) Transglutaminase effects on low temperature gelation of fish protein sols. J Food Sci, 62 (l):20-24
Lee EY, Park J (2003) Microbial transglutaminase induced crosslinking of a selected comminuted muscle system – Processing conditions for physical properties of restructured meat. Food Sci Biotechn, 12(4):365-370
Liebl W (1991) The genus Corynebactenum-nonmQdical. In: The prokaryotes. Balows A, Trüper HG, Dworkin M, Harder W, Schleifer KH (eds), Springer, New York Berlin Heidelberg: 1157-1171
Lu SY, Zhou ND, Tian YP, Li HZ, Chen J (2003) Purification and properties of transglutaminase from Streptoverticillium mobaraense. J Food Biochem, 27(2): 109-125
Malumbres M, Gil JA, Martin JF (1993) Codon preference in Corynebacteria. Gene, 134:15-24
Margosiak SA, Dharma A, Bruce-Carver MR, Gonzales AP, Louie D, Kuehn GD (1990) Identification of the large subunit of ribrolose 1,5-biophosphate carboxylase/osygenase as a substrate for transglutaminase in Medicago sativa L. (alfalfa). Plant Physiol, 92:88-96
Masson Ρ (1992) Pressure denaturation of proteins. In: High Pressure and Biotechnology. John Libbey Eurotext, London, UK, 224:84-89
Meister A, Tate SS, Griffith OW (1981) γ-Glutamyl Transpeptidase. In: Method Enzymol. Vol 77, Academic Press, New York,:237-253
Menendez O, Schwarzenbolz U, Rohm H, Henle Τ (2004) Casein gelation under simultaneus action of transglutaminase and glucono-delta-lactone. Nahrung-Food, 48(3): 165-168
Monterò Ρ, López-Caballero ME, Pérez-Mateos M, Solas MT, Gómez-Guillién MC (2005) Transglutaminase activity in pressure-induced gelation assisted by prior setting. Food Chem,
(4):751-758
Motoki M, Okiyama A, Nonaka M, Tanaka H, Uchio R, Matsura A, Ando H, Umeda Κ (1989) Novel transglutaminase manufacture for preparation of protein gelling compounds. Jpn Kokai Tokkyo Koho JP, 0127471
Motoki M, Seguro Κ (1998) Transglutaminase and its use for food processing. Trends Food Sci Techn, 9:204-210
Mounsey JS, 0£Kennedy BT, Kelly PM (2005) Influence of transglutaminase treatment on properties of micellar casein and products made therefrom. Lait, 85(4-5):405-418
Muguruma M, Tsuruoka K, Fujino H, Kawahara S, Yamauchi K, Matsumura S, Soeda Τ (1999) Gel strength enhancement of sausages by treating with microbial transglutaminase. In: Proceedings of 45th international congress of meat science and technology. Yokohama, Japan: 138-139
Muguruma M, Tsuruoka K, Katayama K, Erwanto Y, Kawahara S, Yamauchi Κ (2003) Soybean and milk proteins modified by transglutaminase improves chicken sausage texture even at reduced levels of phosphate. Meat Sci, 63:191-197
Neilsen PM (1995) Reactions and potential industrial applications of transglutaminase. Review of literature and patends. Food Biotechnol, 9:119-156
Nielsen GS, Petersen BR, Moller AJ (1995) Impact of salt, phosphate and temperature on the effect of a transglutaminase (F XHIa) on the texture of restructured meat. Meat Sci, 41(3):293-299
Nieuwenhuizen WF, Decker HL, Groneveld T, de Koster CG, de Jong GAH (2004) Transglutaminase-mediated modification of glutamine and lysine residues in native bovine beta-lactoglobulin. Biotechn Bioeng, 85(3):248-258
Nomura Y, Toki S, Ishii Y, Shirai Κ (2001) Effect of transglutaminase on reconstruction and physicochemical properties of collagen gel from shark type I collagen. Biomacromol, 2:105-110
Nonaka M, Tanaka H, Okiyama A, Motoki M, Ando Η, Umeda Κ, Matsura A (1989) Polymerization of several proteins by Ca2+- independent transglutaminase derived from microorganism. Agric Biol Chem, 53:2619-2623
Nonaka M, Sakamoto H, Kawajiri H, Soeda T, Motoki M (1992) Sodium caseinate and skim milk gels formed by incubation with microbial transglutaminase. J Food Sci, 57:1214-1218
Nonaka M, Matsuura Y, Motoki M (1996) Incorporation of Lysine peptides into as l-casein by Ca2+-independent microbial transglutaminase. Biosci Biotech Bioch, 60:131-133
Nonaka M, Ito R, Sawa A, Motoki M, Nio Ν (1997) Modification of several proteins by using Ca2+-independent microbial transglutaminase with high pressure treatment. Food Hydrocol, 11(3)351-353
Nozawa H, Mamegoshi S, Seki Ν (1997) Partial purification and characterization of six transglutaminases from ordinary muscles of various fishes and marine invertebrates. Comp Biochem Physiol, 118B(2):313-317
Nozawa H, Seki Ν (2001) Purification of transglutaminase from scallop striated adductor muscle and NaCl-induced inactivation. Fish Sci, 67(3):493-499
Oh JH, Wang B, Field PD, Aglan HA (2003) Characteristics of edible films made from dairy proteins and zein hydrolysate cross-linked with transglutaminase. Inter J Food Sci Techn, 39(3):287-294
Ohtsuka T, Umezawa Y, Nio N, Kubota Κ (2001) Comparison of deamidation activity of transglutaminases. J Food Sci, 66(l):25-29
O' Sullivan MM, Kelly AL, Fox PF (2002) Effect of transglutaminase on the heat stability of milk: a possible mechanism. J Dairy Sci, 85:1-7
Pedersen MH, Hanses TK, Sten E, Seguro Κ, Ohtsuka Τ, Morita A, Bindslev-Jensen C, Poulsen LK (2004) Evaluation of the potential allergenicity of the enzyme microbial transglutaminase using the 2001 FAO/WHO Decision Tree. Molec Nutr Food Resear, 48(6):434-440
Pérez-Mateos M, Gomez-Guillin MC, Hurtado JL, Solas M, Monterò Ρ (2002) Rosemary extract and omega-3 effect on gelification treatment of mince mackerel. Food Chem, 79:1-8
Pérez-Mateos M, Amato PM, Lanier TC (2004) Gelling properties of Atlantic croaker surimi processed by acid or alkaline solubilization. J Food Sci, 69(4):C328-C333
Pietrasik Z, Li-Chan ECY (2002) Response surface methodology study on the effects of salt, microbial transglutaminase and heating temperature on pork batter gel properties. Food Res
Inter, 35:387-396
Pietrasik Ζ (2003) Binding and textural properties of beef gels processed with κ-carrageenan, egg albumin and microbial transglutaminase. Meat Sci, 63:317-324
Pietrasik Z, Jarmoluk A (2003) Effect of sodium caseinate and κ-carrageenan on binding and textural properties of pork gels enhanced by microbial transglutaminase addition. Food Res Inter, 36:285-294
Puszkin EG, Raghuraman V (1985) Catalytic properties of a calmodulin-regulated transglutaminase from human platelet and chicken gizzard. J Biol Chem, 260:16012-16020
Ramirez JA, Rondirguez-Sosa R, Morales OG, Vazquez M (2000) Surimi gels from striped mullet (Mugil cephalus) employing microbial transglutaminase. Food Chem, 70:443-449
Ramirez JA, Uresti R, Téllez S, Vazquez M (2002) Using salt and microbial transglutaminase as binding agents in restructured fish products resembling hams. J Food Sci, 67(5): 1778-1784
Ramirez-Suarez JC, Xiong YL (2003) Effect of transglutaminaseinduced cross-linking on gelation of myofibrillar/soy protein mixtures. Meat Sci, 65(2):899-907
Ramirez-Suarez JC, Addo Κ, Xiong YL (2005) Gelation of mixed myofibrillar/wheat gluten proteins treated with microbial transglutaminase. Food Resear Inter, 38(10): 1143-1149
Roseli CM, Wang J, Aja S, Bean S, Lookhart G (2003) Wheat flour proteins as affected by transglutaminase and glucose oxidase. Cereal Chem, 80(l):52-55
Ruiz-Carrascal J, Regenstein J (2002) Emulsion stability and water uptake ability of chicken breast muscle proteins as affected by microbial transglutaminase. J Food Sci, 67(2):734-739
Sakamoto H, Kumazawa Y, Kawajiri H, Motoki Μ (1995α) ε-(γ-Glutamyl)lysine crosslink distribution in foods as determined by improved method. J Food Sci, 60(2):416-419
Sakamoto H, Kumazawa Y, Toiguchi S, Seguro K, Soeda T, Motoki M (1995β) Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture. J Food Sci, 60(2):300-304
Sakamoto H, Yamazaki K, Kaga C, Yamamoto Y, Ito R, Kurosawa Y (1996) Strength enhancement by addition of microbial transglutaminase during Chinese noodle processing. Nip Shokuh Kagaku Kaishi, 43:598-602
Sato K, Tsukamasa Y, Imai C, Ohtsuki K, Shimizu Y, Kawabata M (1992) Improved method for identification and determination of e-(Y-Glutamyl)lysine crosslink in protein using proteolytic digestion and derivatization with phenyl isothiocyanate followed by high-performance liquid chromatography separation. J Agric Food Chem, 40:806-810
Seguro K, Kumazawa Y, Ohtsuka T, Toiguchi S, Motoki M (1995) Microbial transglutaminase and e-(Y-Glutamyl)lysine crosslink effects on elastic properties of Kamaboko gels. J Food Sci, 60(2):305-311
Seguro K, Nio N, Motoki Μ (1996α) Some characteristics of a microbial protein cross-linking enzyme: Transglutaminase. In: Macromolecular interactions in food technology (ACS Symposium series 650). American Chemical Society:271-280
Seguro K, Kumazawa Y, Kuraishi C, Sakamoto H, Motoki Μ (1996β) The 8-(Y-Glutamyl)lysine moiety in cross-linked casein is an available source of lysine for rats. Nutrition, 126:2557-2562
Seki N, Uno Η, Lee NH, Kimura I, Toyoba K, Fujita T, Arai Κ (1990) Transglutaminase activity in Alaska Pollack muscle and surimi, and its reaction with myosin b.Nip Suis Gakkai, 56:125-132
Seo H, Shin WS, Yoon S, Lee S (2003) Effect of microbial transglutaminase on physical and textural properties of noodles made with Korean wheat flour (Geurumil). Food Sci Biotechn, 12(l):l-8
Serafini-Fracassini D, Del Duca S, D£Orazi D (1988) First evidence for polyamine conjugation mediated by an enzymic activity in plants. Plant Physiol, 87:757-761
Serafini-Fracassini D, Del Duca S, Torrigiani Ρ (1989) Polyamine conjugation during the cell cycle of Helianthus tuberosis: Nonenzymatic and trnsglutaminase-like binding activity. Plant Physiol Biochem, 27:659-668
Serrano A, Cofrades S, Colmenero FJ (2004) Transglutaminase as binding agent in fresh restructured beef steak with added walnuts. Food Chem, 85:423-429
Sharma R, Zakora M, Qvist KB (2002) Susceptibility of an industrial alfa-lactalbumin concentrate to cross-linking by microbial transglutaminase. Inter Dairy J, 12(12):1005-1012
Shimba N, Shinohara M, Yokoyama KI, Kashiwagi T, Ishikawa K, Ejima D, Suzuki ΕΙ (2002a) Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site. FEBS Let, 517:175-179
Shimba N, Yokoyama KI, Suzuki EI (2002ß) NMR-based screening method for transglutaminases: rapid analysis of their substrate specificities and reaction rates. J Agric Food Chem, 50:1330-1334
Shoji T, Saeki H, Wakameda A, Nonaka M (1994) Influence of ammonium salt on the formation of pressure-induced gel from Walleye Pollack surimi. Nip Suis Gakkan, 60(1):101-109
Signorini M, Beninati S, Bergamini CM (1991) Identification of transglutaminase activity in the leaves of silver beet {Beta vulgarìs L.). J Plant Physiol, 137:547-552
Soares LHD, Assmann F, Ayub MAZ (2003) Purification and properties of a transglutaminase produced by a Bacillus circulans strain isolated from the Amazon environment. Biotechn Appi Biochem, 37:295-299
Soares LHD, Assmann F, Ayub MAZ (2003) Production of transglutaminase from Bacillus circulans on solid-state and submerged cultivations. Biotechn Lett, 25(23): 2029-2033
Soeda T, Sakamoto H, Nonaka M (1992) Manufacture of plant protein powders with emulsifiers and transglutaminase. Jpn Kokai Tokkyo Koho, JP 0479842
Soeda T, Kaneko T, Hokazono A, Tujimoto K, Nurakami Η (2005α) Effects of microbial transglutaminase on melting point and gel properly of gelatins. J Japan Soc Food Sci Techn, 52(6) :251-256
Soeda T, Hokazono A, Ozawa T, Fujiwara Η (2005β) Characteristics and mechanism of binding of foods by microbial transglutaminase. J Japan Soc Food Sci Techn, 52(5):207-211
Suklim K, Flick GJ, Marcy JE, Eigei WN, Haugh CG, Granata LA (2004) Effect of cold-set binders: Alginates and microbial transglutaminase on the physical properties of restructured scallops. J Text Stud, 35(6):634-642
Takagaki Y, Narukawa K, Yamazaki T, Motoki M (1990) Solid fats containing transglutaminase for food and their manufacture. Jpn Kokai Tokkyo Koho, JP 02128648
Takagaki Y, Narukawa K, Uchio R (1991) Coating of vegetables and fruits with transglutaminase and proteins for preservation. Jpn Kokai Tokkyo Koho, JP 03272639
Takehana S, Washizu K, Ando Κ (1994) Chemical synthesis of the gene for microbial transglutaminase from Streptoverticillium and its expression in Escherichia coli. Biosci Biotech Bioch, 58(l):88-92
Téllez-Luis S J, Uresti RM, Ramirez JA, Vazquez M (2002) Low-salt restructured fish products using microbial transglutaminase as binding agent. J Sci Food Agric, 82:953-959
Téllez-Luis S J, Gonzalez-Cab riales JJ, Ramirez JA, Vazquez M (2004α) Production of transglutaminase by Streptoverticillium ladakanum NRRL-3191 grown on media made from hydrolysates of sorghum straw. Food Technol Biotechnol, 42(l):l-4
Téllez-Luis S J, Ramirez JA, Vazquez Μ (2004ß) Production of transglutaminase by Streptoverticillium ladakanum NRRL-3191 using glycerol as carbon source. Food Technol Biotechnol, 42(2):75-81
Truong VD, Clare DA, Catignani GL, Swaisgood HE (2004) Crosslinking and rheological changes of whey proteins treated with microbial transglutaminase. J Agric Food Chem, 52(5): 1170-1176
Tsai GJ, Lin SM, Jiang ST (1996) Transglutaminase from Streptoverticillium ladakanum and application to minced fish product. J Food Sci, 61:1234-1238
Tsao CY, Kao YC, Hsieh JF, Jiang ST (2002) Use of soy protein and microbial transglutaminase as a binder in low-sodium restructured meats. J Food Sci, 67(9):3502-3506
Tseng TF, Liu DC, Chen MT (2000) Evaluation of transglutaminase on the quality of low-salt chicken meat-balls. Meat Sci, 55:427-431
Tsukamasa Y, Sato K, Shimizu Y, Imai C, Sugiyama M, Minegishi Y, Kawabata M (1993) e-(Y-Glutamyl)lysine crosslink formation in sardine myofibril sol during setting at 25° G J Food Sci, 58:785-787
Tsukamasa Y, Miyake Y, Ando M, Makinodan Y (2002) Total activity of transglutaminase at various temperatures in several fish meats. Fish Sci, 68:929-933
Uresti RM, Ramirez JA, Lopez-Arias N, Vazquez M (2003) Negative effect of combining microbial transglutaminase with low methoxyl pectins on the mechanical properties and colour attributes offish gels. Food Chem, 80:551-556
Uresti RM, Τ (1993) ε-(γ-Glutamyl)lysine crosslink formation in sardine myofibril sol during setting at 25° C. J Food Sci, 58:785-787
Tsukamasa Y, Miyake Y, Ando M, Makinodan Y (2002) Total activity of transglutaminase at various temperatures in several fish meats. Fish Sci, 68:929-933
Uresti RM, Ramirez JA, Lopez-Arias N, Vazquez M (2003) Negative effect of combining microbial transglutaminase with low methoxyl pectins on the mechanical properties and colour attributes offish gels. Food Chem, 80:551-556
Uresti RM, Téllez-Luis SJ, Ramirez JA, Vazquez Μ (2004α) Use of dairy proteins and microbial transglutaminase to obtain low-salt fish products from filleting waste from silver carp {Hypophthalmichthys molitrix). Food Chem, 86:257-262
Uresti RM, Velazquez G, Ramirez JA, Vazquez M, Torres JA (2004ß) Effect of high-pressure treatments on mechanical and functional properties of restructured products from arrowtooth flounder (Atheresthes stomias). J Sci Food Agric, 84(13): 1741-1749
Uresti RM, Velazquez G, Vazquez M, Ramirez JA, Torres JA (2005) Restructured products from arrowtooth flounder {Atheresthes stomias) using high-pressure treatments. Europ Food Resear Techn, 220(2): 113-119
Uresti RM, Velazquez G, Vazquez M, Ramirez JA, Torres JA (2006) Effects of combining microbial transglutaminase and high pressure processing treatments on the mechanical properties of heat-induced gels prepared from arrowtooth flounder {Atheresthes stomias). Food Chem, 94(2):202-209
Wakameda A, Ichihara Y, Toiguchi S, Motoki M (1990) Manufacture of fish meat paste with transglutaminase as phosphate substitute. Jpn Kokai Tokkyo Koho, JP 02100653
Washizu K, Ando Κ, Koikeda S (1994) Molecular cloning of the gene for microbial transglutaminase from Streptoverticillium and its expression in Streptomyces lividans. Biosci Biotechn Biochem, 58(l):82-87
Watanabe M (1994) Controlled enzymatic treatment of wheat proteins for production of hypoallergenic flour. Biosci Biotech Bioch, 58:388-390
Wijngaards G, Paardekooper EJC (1988) In: Trends in modern meat technology. 2nd ed, Ed. by Krol B, van Roon PS, Houben JH, Pudoc, Wageningen: 125
Wilson SA (1992) Modifying meat proteins via enzymatic crosslinking. In: Proceedings of the 27th meat industry research conference. Hamilton, Meal Industry Research Institutes of New Zealand, Mirinz:247-277
Yamazaki K, Naruto Y, Tanno H, Soeda Τ (2004) Effects of microbial transglutaminase on textural improvement of Chinese noodles. J Japan Soc Food Sci Techn-Nip Shokuh Kagaku KogakuKaishi,51(l):13-17
Yan G, Du G, Li Y, Chen J, Zhong J (2005) Enhancement of microbial transglutaminase production by Streptoverticillium mobaraense: application of a two-stage agitation speed controlstrategy. Process Biochem, 40(2):963-968
Yasueda H, Kumazawa Y, Motoki M (1994) Purification and characterization of a tissue-type transglutaminase from Red Sea bream {Pagrus major). Biosci Biotech Biochem, 58:2041-2045
Yasueda H, Kumazawa Y, Motoki M (1995) Tissue-type transglutaminase from Red Sea bream {Pagrus major) Sequence analysis of the cDNA and functional expression in Escherichia coli. European J Biol, 232:411-419
Yongsawatdigul J, Piyadhammaviboon Ρ (2005) Effect of microbial transglutaminase on autolysis and gelation of lizardfish surimi. J Sci Food Agric, 85(9):1453-1460
Yokoyama K, Ohtsuka T, Kuraishi C, Ono K, Kita Y, Arakawa Τ, Ejima D (2003) Gelation of food protein induced by recombinant microbial transglutaminase. J Food Sci, 68(1):48-51
Yokoyama K, Nio N, Kikuchi Y (2004) Properties and application of microbial transglutaminase. Appi Microbiol Biotechnol, 64:447-454
Zhang J, Masui Y (1997) Role of amphibian egg transglutaminase in the development of secondary cytostatic factor in vitro. Mol ReprodDev, 47:302-311
Zhu Y, Rinzema A, Tramper J, Bol J (1995) Microbial transglutaminase-a review of its production and application in food processing. Appi Microbiol Biotechn, 44:277-282
Zhu Y, Rinzema A, Tramper J, Bol J (1996) Medium design based on stoichiometric analysis of microbial transglutaminase production by Streptoverticillium mobaraense. Biotech Bioeng, 50:291-298
Zhu Y, Rinzema A, Bonarius HP J, Tramper J, Bol J (1998) Microbial transglutaminase production by Streptoverticillium mobaraense: Analysis of amino acid metabolism using mass balances. Enz Micro Techn, 23:216-226
