Protein cross-linking with oxidative enzymes and transglutaminase: Effects in meat protein systems

VTT Publications

Volumn , Issue 642, 2007, Pages 3-114

  Lantto, Raija ^a  

^a NONE

Author keywords

Chicken breast; Cross linking; Enzymes; Food; Gel formation; Laccase; Meat; Myofibril; Proteins; Structure; Texture; Thermal behaviour; Transglutaminase; Trichoderma reesei; Tyrosinase; Water holding

Indexed keywords

EID: 35348880320     PISSN: 12350621     EISSN: 14550849     Source Type: Book Series    
DOI: None     Document Type: Article

References (299)

1. Aboumahmoud, R., and Savello, P. (1990) Cross-linking of whey protein by transglutaminase. J. Dairy Sci. 73: 256-263.
2. Akamittath, J.G., and Ball, H.R. (1992) Transglutaminase mediated polymerization of crude actomyosin refined from mechanically deboned poultry meat. J. Muscle Foods 3: 1-14.
3. Aktaş, N., and Kiliç, B. (2005) Effect of microbial transglutaminase on thermal and electrophoretic properties of ground beef. LWT - Food Sci. Technol. 38: 815-819.
4. Alexandre, M.-C., Pipineau, Y., Viroben, G., Chiarello, M., Lelion, A., and Gueguen, J. (1993) Wheat γ gliadin as substrate for bovine plasma factor XIII. J. Agric. Food Chem. 41: 2206-2214.
5. Amako, D.E.N., and Xiong, Y.L. (2001) Effects of carrageenan on thermal stability of proteins from chicken thigh and breast muscles. Food Res. Int. 34: 247-253. (Pubitemid 32235356)
6. Ameille, V., Castello, P., Garcia, R., Rakotozafy, L., Potus, J., and Nicolas, J. (2000) Effects of glucose oxidase or lipase addition on dough consistency and oxygen consumption during mixing of unyeasted flour dough. Sciences des aliments 20: 441-455.
7. An, H., Peters, M.Y., and Seymour, T.A. (1996) Roles of endogenous enzymes in surimi gelation. Trends Food Sci. Technol. 7: 321-327. (Pubitemid 27094074)
8. Ando, H., Adachi, M., Umeda, K., Matsuura, A., Nonaka, M., Uchio, R., Tanaka, H., and Motoki, M. (1989) Purification and characteristics of a novel transglutaminase derived from microorganism. Agric. Biol. Chem. 53: 2613-2617. (Pubitemid 20077525)
9. Anghileri, A., Lantto, R., Kruus, K., Arosio, C., and Freddi, G. (2007) Tyrosinase-catalyzed grafting of sericin peptides onto chitosan and production of protein-polysaccharide bioconjugates. J. Biotechnol. 127: 508-519. (Pubitemid 44827392)
10. Arnfield, S.D., and Murray, E.D. (1981) The influence of processing parameters of food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation. Can. Inst. Food Sci. Technol. J. 14: 289-294.
11. Asghar, A., Samejima, K., and Yasui, T. (1983) Functionality of muscle proteins in gelation mechanisms of structured meat products. CRC Crit. Rev. Food Sci. Nutr. 22: 27-106.
12. Aurbach, G.D., and Jakoby, W.B. (1962) The multiple functions of thiooxidase. J. Biol. Chem. 237: 565-568.
13. Autio, K., Kruus, K., Knaapila, A., Gerber, N., Flander, L., and Buchert, J. (2005) Kinetics of transglutaminase-induced cross-linking of wheat proteins in dough. J. Agric. Food Chem. 53: 1039-1045. (Pubitemid 40270394)
14. Awad, A., Powrie, W.D., and Fennema, O. (1968) Chemical deterioration of frozen bovine muscle at -4°C. J. Food Sci. 33: 227-234.
15. Babiker, E.E. (2000) Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein. Food Chem. 70: 139-145.
16. Bailey, A.J., and Light, N.D. (1989) Connective tissue in meat and meat products. 1st ed. Elsevier Science Publishers, London and New York.
17. Basman, A., Köksel, H., and Ng, P.K.W. (2002a) Effects of transglutaminase on SDS-PAGE patterns of wheat, soy and barley proteins and their blends. J. Food Sci. 67: 2654-2658. (Pubitemid 35212125)
18. Basman, A., Köksel, H., and Ng, P.K.W. (2002b) Effects of increasing levels of transglutaminase on the rheological properties and bread quality characteristics of two wheat flours. Eur. Food Res. Technol. 215: 419-424.
19. Bean, R.C., and Hassid, W.Z. (1956) Carbohydrate oxidase from a red alga Iridophycus flaccidum. J. Biol. Chem. 218: 425-436.
20. Belitz, H.-D., and Grosch, W. (1999) Muscle tissue: composition and function. In: Food Chemistry. 2. Ed. Springer-Verlag, Berlin Heidelberg, Germany. Pp. 532-550.
21. Bertram, H.C., Høll Andersen, R., and Andersen, H.J. (2007) Development in myofibrillar water distribution of two pork qualities during 10-month freezer storage. Meat Sci. 75: 128-133. (Pubitemid 44548202)
22. Billaud, C., Maraschin, C., and Nicolas, J. (2004) Inhibition of polyphenoloxidase from apple by Maillard products prepared from glucose or fructose with Lcysteine under various conditions of pH and temperature. LWT - Food Sci. Technol. 37: 69-78. (Pubitemid 38215410)
23. Boumans, J.W.L., Nagtegaal, R.M.A., Dunnewind, A., Happe, R.P., Bos, M.A., Færgemand, M., and Degn, P. (2006) A method for enzymatic cross-linking of a protein, cross-linked protein thus obtained and use thereof. WO 2006/016809.
24. Broderick, E.P., O'Halloran, D.M., Rotchev, Y.A., Griffin, M., Collighan, R.J., and Pandit, A.S. (2004) Enzymatic stabilization of gelatin-based scaffolds. J. Biomed. Mater Res. Part B: Appl. Biomater. 72B: 37-42. (Pubitemid 40039607)
25. Burton, S.G. (2003) Oxidizing enzymes as biocatalysts. Trends Biotechnol. 21: 543-549.
26. Burzio, L.A., Burzio, V.A., Pardo, J., and Burzio, L.O. (2000) In vitro polymerization of mussel polyphenolic proteins catalyzed by mushroom tyrosinase. Comp. Biochem. Physiol. Part B 126: 383-389. (Pubitemid 30628899)
27. Butler, M.J., and Day, A.W. (1998) Fungal melanins: a review. Can. J. Microbiol. 44: 1115-1136.
28. Bönisch, M.P., Lauber, S., and Kulosik, U. (2007) Improvement of enzymatic cross-linking of casein micelles with transglutaminase by glutathione addition. Int. Dairy J. 17: 3-11. (Pubitemid 46070166)
29. Caballero, P.A., Bonet, A., Rosell, C.M., and Gómez, M. (2005) Effect of microbial transglutaminase on the rheological and thermal properties of insect damaged wheat flour. J. Cereal Chem. 42: 93-100. (Pubitemid 40717564)
30. Carballo, J., Ayo, J., and Jiménez Colmenero, F. (2006) Microbial transglutaminase and caseinate as cold set binders: Influence of meat species and chilling storage. LWT - Food Sci. Technol. 39: 692-699. (Pubitemid 43340494)
31. Cariello, L., Ristoratore, F., and Zanetti, L. (1997) A new transglutaminase-like from the ascidian Ciona intestinalis. FEBS Lett. 408: 171-176. (Pubitemid 27226790)
32. Carvajal-Millan, E., Guigliarelli, B., Belle, V., Rouau, X., and Micard, V. (2005) Storage stability of laccase induced arabinoxylan gels. Carbohydr. Polym. 59: 181-188. (Pubitemid 40142419)
33. Chambi, H., and Grosso, C. (2006) Edible films produced with gelatin and casein cross-linked with transglutaminase. Food Res. Int. 39: 458-466. (Pubitemid 43233731)
34. Chau, D.Y.S., Collighan, R.J., Verderio, E.A.M., Addy, V.L., and Griffin, M. (2005) The cellular response to transglutaminase-cross-linked collagen. Biomaterials 26: 6518-6529. (Pubitemid 41021746)
35. Chen, J.S.K., and Mehta, K. (1999) Tissue transglutaminase: an enzyme with a split personality. Int. J. Biochem. Cell. Biol. 31: 817-836. (Pubitemid 29354079)
36. Chen, R.N., Ho, H.-O., and Sheu, M.-T. (2005) Characterisation of collagen matrices crosslinked using microbial transglutaminase. Biomaterials 26: 4229-4235. (Pubitemid 40430849)
37. Chen, Q.-X., Song, K.-K., Qiu, L., Liu, X.-D., Huang, H., and Guo, H.-Y. (2005) Inhibitory effects of mushroom tyrosinase by p-alkoxybenzoic acids. Food Chem. 91: 269-274. (Pubitemid 39601639)
38. Chung, J.E., Kurisawa, M., Uyama, H., and Kobayashi, S. (2003) Enzymatic synthesis and antioxidant property of gelatin-catechin conjugates. Biotechnol. Lett. 25: 1993-1997. (Pubitemid 37502440)
39. Clare, D.A., Horton, H.R., Stabel, T.H., Swaisgood, H.E., and Lecce, J.G. (1984) Tissue distribution of mammalian sulfhydryl oxidase. Arch. Biochem. Biophys. 230: 138-145. (Pubitemid 14131906)
40. Claus, H. (2003) Laccases and their occurrence in prokaryotes. Arch. Microbiol. 179: 145-150.
41. Claus, H., and Filip, Z. (1997) The evidence for a laccase-like enzyme activity in a Bacillus sphaericus strain. Microbiol. Res. 152: 209-216. (Pubitemid 27320464)
42. Claus, H., and Decker, H. (2006) Bacterial tyrosinases. Syst. Appl. Microbiol. 29: 3-14. (Pubitemid 43102498)
43. Cortez, J., Bonner, P.L.R., and Griffin, M. (2004) Application of transglutaminases in the modification of wool textiles. Enz. Microb. Technol. 34: 64-72. (Pubitemid 37510326)
44. Cortez, J., Bonner, P.L.R., and Griffin, M. (2005) Transglutaminase treatment of wool fabrics leads to resistance to detergent damage. J. Biotechnol. 116: 379-386. (Pubitemid 40312682)
45. Cummins, P., and Perry, S.V. (1974) Chemical and immunochemical characteristics of tropomyosins from striated and smooth muscle. Biochem. J. 141: 43-49.
46. Dabbous, M.K. (1966) Inter- and intramolecular cross-linking in tyrosinase-treated tropocollagen. J. Biol. Chem. 241: 5307-5312.
47. Dalfard, A.B., Khajeh, K., Soudi, M.R., Naderi-Manesh, H., Ranjbar, B., and Sajedi, R.H. (2006) Isolation and biochemical characterization of laccase and tyrosinase activities in a novel melanogenic soil bacterium. Enz. Microb. Technol. 39: 1409-1416. (Pubitemid 44402685)
48. Davies, K.J.A. (1987) Protein damage and degradation by oxygen radicals. I. General aspects. J. Biol. Chem. 262: 9895-9901.
49. Davies, K.J.A., and Delsignore, M.E. (1987) Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure. J. Biol. Chem. 262: 9908-9913.
50. De Backer-Royer, C., Traoré, F., and Meunier, J.C. (1992) Polymerization of meat and soybean proteins by human placental calcium-activated factor XIII. J. Agric. Food Chem. 40: 2052-2056.
51. De la Motte, R.S., and Wagner, F.W. (1987) Aspergillus niger sulfhydryl oxidase. Biochem. 26: 7363-7371.
52. De Marco, A., and Roubelakis-Angelakis, K.A. (1997) Laccase activity could contribute to cell-wall reconstitution in regenerating protoplasts. Phytochem. 46: 421-425. (Pubitemid 27414918)
53. 14C-labelled putrescine. Biochem. Biophys Res. Commun. 22: 82-88.
54. Dickinson, E. (1997) Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization. Trends Food Sci. Technol. 8: 334-339.
55. Dimitrakopoulou, M.A., Ambrosiadis, J.A., Zetou, F.K., and Bloukas, J.G. (2005) Effect of salt and transglutaminase (TG) level and processing conditions on quality characteristics of phosphate-free, cooked, restructured pork shoulder. Meat Sci. 70: 743-749. (Pubitemid 40684089)
56. Dondero, M., Figueroa, V., Morales, X., and Curotto, E. (2006) Transglutaminase effects on gelation capacity of thermally induced beef protein gels. Food Chem. 99: 546-554.
57. Dowling, J.H., and Levine, H.B. (1956) Hexose oxidation by an enzyme system of Malleomyces pseudomallei. J. Bacteriol. 72: 555-560.
58. Dunnewind, B., van Vliet, T., and Orsel, R. (2002) Effect of oxidative enzymes on bulk rheological properties of wheat flour doughs. J. Cereal Sci. 36: 357-366. (Pubitemid 35212073)
59. Duran, N., and Sakurai, A. (2003) Applications of oxidative enzymes in wastewater treatment. In: Wastewater treatment using enzymes. Research Signpost, Trivandrum, INDE, INIST-CNRS, Vandoeuvre-lès-Nancy, France. Pp. 41-51.
60. Duran, R., Junqua, M., Schmitter, J.M., Gancet, C., and Goulas, P. (1998) Purification, characterisation, and gene cloning of transglutaminase from Streptoverticillium cinnamoneum CBS 683.68. Biochimie 80: 313-319. (Pubitemid 28291165)
61. Ekstrand, B., and Björck, L. (1986) Oxidation of β-carotene by bovine milk lactoperoxidase-halide-hydrogen peroxide systems. J. Agric. Food Chem. 34: 412-415.
62. Eli-Berchoer, L., Hegyi, G., Patthy, A., Reisler, E., and Muhlrad, A. (2000) Effect of intramolecular cross-linking between glutamine-41 and lysine-50 on actin structure and function. J. Muscle Res. Cell. Motility 21: 405-414.
63. Elzinga, M., Collins, J.E., and Kuehl, W.M. (1973) Complete amino-acid sequence of actin of rabbit skeletal muscle. Proc. Natl. Acad. Sci. U.S.A. 70: 2687-2691.
64. Espin, J.C., Varón, R., Fenoll, L.G., Gilabert, M.A., García-Ruíz, P.A., Tudela, J., and García-Cánovas, F. (2000) Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase. Eur. J. Biochem. 267: 1270-1279. (Pubitemid 30143264)
65. Farouk, M.M., Wieliczko, K.J., and Merts, I. (2004) Ultra-fast freezing and low storage temperatures are not necessary to maintain the functional properties of manufacturing beef. Meat Sci. 66: 171-179.
66. Feeney, R.E., and Whitaker, J.R. (1988) Importance of cross-linking reactions in proteins. Adv. Cereal Sci. Technol. 9: 21-46.
67. Fennema, O.R. (1976) Principles of food science. Part I. In: Food Chemistry. Fennema, O.R. (Ed.). Marcel Dekker Inc., New York. P. 205.
68. Fennema, O.R. (1985) Water and Ice. In: Food Chemistry. Fennema, O.R. (Ed.). Marcel Dekker, Inc., New York. Pp. 23-67.
69. Fesus, L., and Piacentini, M. (2002) Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem. Sci. 77: 534-539. (Pubitemid 35279599)
70. Figueroa-Espinoza, M.-C., and Rouau, X. (1998) Oxidative cross-linking of pentosans by a fungal laccase and horse radish peroxidase. Mechanism of linkage between feruloylated arabinoxylans. Cereal Chem. 75: 259-265.
71. Figueroa-Espinoza, M.-C., Morel, M.H., and Rouau, X. (1998) Effect of lysine, tyrosine, cysteine and glutathione on the oxidative cross-linking of feruloylated arabinoxylans by a fungal laccase. J. Agric. Food Chem. 46: 2583-2589. (Pubitemid 128488339)
72. Findley, C.J., Parkin, K.L., and Stanley, D.W. (1986) Differential scanning calorimetry can determine kinetics of thermal denaturation of beef muscle proteins. J. Food Biochem. 10: 1-15.
73. Foegeding, E.A. (1988) Thermally induced changes in muscle proteins. Food Technol. June: 58-64.
74. Folk, J.E. (1970) Transglutaminase (Guinea pig liver). Methods Enzymol. 17A: 889-894.
75. Folk, J.E. (1980) Transglutaminases. Annu. Rev. Biochem. 49: 517-531.
76. Folk, J.E., and Finlayson, J.S. (1977) The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv. Protein Chem. 31: 1-33.
77. Freddi, G., Anghileri, A., Sampaio, S., Buchert, J., Monti, P., and Taddei, P. (2006) Tyrosinase-catalyzed modification of Bombyx mori silk fibroin: grafting of chitosan under heterogenous reaction conditions. J. Biotechnol. 125: 281-294. (Pubitemid 44192552)
78. 2+ -independent microbial transglutaminase from Streptomyces lydicus. Food Hydrocoll. 11: 19-25.
79. Færgemand, M., Otte, J., and Qvist, K.B. (1998a) Crosslinking of whey proteins by enzymatic oxidation. J. Agric. Food Chem. 46: 1326-1333. (Pubitemid 128498765)
80. Færgemand, M., Otte, J., and Qvist, K.B. (1998b). Emulsifying properties of milk proteins crosslinked with microbial transglutaminase. Int. Dairy J. 8: 715-723. (Pubitemid 29032162)
81. Færgemand, M., Murray, B.S., Dickinson, E., and Qvist, K.B. (1999) Crosslinking of adsorbed casein films with transglutaminase. Int. Dairy J. 9: 343-346. (Pubitemid 29395665)
82. Garrison, W.M. (1987) Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem. Rev. 87: 381-398.
83. Gembeh, S.V., Farrell, H.M., Taylor, M.M., Brown, E.M., and Marmer, W.N. (2005) Application of transglutaminase to derivatize proteins: 1. Studies on soluble proteins and preliminary results on wool. J. Sci Food Agric. 85: 418-424. (Pubitemid 40198992)
84. Gerber, J., Muhlenhoff, U., Hofhaus, G., Lill, R., and Lisowsky, T. (2001) Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the ERV1p/Alrp protein family. J. Biol. Chem. 276: 23486-23491.
85. Gerrard, J.A. (2002) Protein-protein cross-linking in food: methods, consequences, applications. Trends Food Sci. Technol. 13: 389-397.
86. Gersman, L.C., Stracher, A., and Dreizen, P. (1969) Subunit structure of myosin. III. A proposed model for rabbit skeletal myosin. J. Biol. Chem. 244: 2726-2736.
87. Gianfrida, L., Xu, F., and Bollag, J.-M. (1999) Laccases: A useful group of oxidoreductive enzymes. Biorem. J. 3: 1-25.
88. Girelli, A.M., Mattei, E., Messina, A., and Tarola, A.M. (2004) Inhibition of polyphenol oxidases activity by various dipeptides. J. Agric. Food Chem. 52: 2741-2745.
89. Griffin, M., Casadio, R., and Bergamini, C.M. (2002) Transglutaminases: Nature's biological glues. Biochem. J. 368: 377-396. (Pubitemid 35454517)
90. Gross, A.J., and Sizer, L.W. (1959) The oxidation of tyramine, tyrosine, and related compounds by peroxidise. J. Biol. Chem. 259: 1611-1614.
91. Guerrero-Beltrán, J.A., Swanson, B.G., and Barbosa-Cánovas, G.V. (2005) Inhibition of polyphenoloxidase in mango puree with 4-hexylresorcinol, cysteine and ascorbic acid. LWT - Food Sci. Technol. 38: 625-630.
92. Ha, C.-R., and Iuchi, I. (2003) Transglutaminase. In: Handbook of food enzymology. Whitaker, J.R., Voragen, A., and Wong, D.W.S. (Eds.). Marcel Dekker Inc., New York. Pp. 637-655.
93. Haarasilta, S., and Pullinen, T. (1992) Novel enzyme combinations. A new tool to improve baking results. Agro-Food-Industry Hi-Tech May/June: 12-13.
94. Halaouli, S., Asther, Mi., Kruus, K., Guo, L., Hamdi, M., Sigoillot, J.-C., Asther, M., and Lomascolo, A. (2005) Characterisation of a new tyrosinase from Pycnoporus species with high potential for food technological applications. J. Appl. Microbiol. 98: 332-343.
95. Hamm, R. (1960) Biochemistry of meat hydration. Adv. Food Res. 10: 355-463.
96. Hamm, R. (1972) Kolloidchemie des Fleisches. Paul Parey, Berlin and Hamburg. 222 p.
97. Hammer, G. (1998) Mikrobielle Transglutaminase und Diphosphat bei feinzerkleinerter Brühwurst. Fleischwirtschaft 78: 1155-1162, 1186.
98. Heldt-Hansen, H.P. (1998) Development of enzymes for food applications. In: Biotechnology in the food chain, new tools and applications. VTT Symposium 177. VTT, Espoo, Finland. Pp. 45-55.
99. Hermansson, A.-M. (1986) Water- and fatholding. In: Functional properties of food macromolecules. Mitchell, J.R., and Ledward, D.A. (Eds.). Elsevier Appl. Sci. Publ., London and New York. Pp. 273-314.
100. Hermansson, A.-M., and Lucisano, M. (1982) Gel characteristics - Waterbinding properties of blood plasma gels and methodological aspects on the waterbinding of gel systems. J. Food Sci. 47: 1955-1964.
101. Hill, H.Z. (1992) The function of melanin or six blind people examine an elephant. BioEssays 14: 49-56.
102. Hillhorst, R., Dunnewind, B., Orsel, R., Stegeman, P., van Vliet, T., Gruppen, H., and Schols, H.A. (1999) Baking performance, rheology, and chemical composition of wheat dough and gluten affected by xylanase and oxidative enzymes. J. Food Sci. 64: 808-813. (Pubitemid 29536846)
103. Hoober, K.L., Joneja, B., White, H.B., and Thorpe, C. (1996) A sulfhydryl oxidase from chicken egg white. J. Biol. Chem. 271: 30510-30516. (Pubitemid 26404059)
104. Hornyak, T.J., Bishop, B.D., and Shafer, J.A. (1989) α-Thrombin- catalyzed activation of human platelet factor XIII: relationship between proteolysis and factor XIII activity. Biochem. 28: 7326-7332.
105. http://faculty.etsu.edu/currie/images/
106. Huff-Lonergan, E., and Lonergan, S.M. (2005) Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Sci. 71: 194-204. (Pubitemid 40972870)
107. Huxley, H.E. (1963) Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J. Mol. Biol. 7: 281-308.
108. Icekson, I., and Apelbaum, A. (1987) Evidence for transglutaminase activity in plant tissue. Plant. Physiol. 84: 972-974.
109. Ichinose, A., Bottenus, R.E., and Davie, E.W. (1990) Structure of transglutaminases. J. Biol. Chem. 265: 13411-13414.
110. Ikura, K., Kometani, T., Sasaki, R., and Chiba, H. (1980) Crosslinking of soybean 7S and 11S protein by transglutaminase. Agric. Biol. Chem. 44: 2979-2984.
111. Ikura, K., Sasaki, R., and Motoki, M. (1992) Use of transglutaminase in qualityimprovement and processing of food proteins. Comments Agric. Food Chem. 2: 389-407.
112. Ito, S., Kato, T., Shinpo, K., and Fujita, K. (1984) Oxidation of tyrosine residues in proteins by tyrosinase. Biochem. J. 222: 407-411.
113. İyidoǧan, N.F., and Bayindirli, A. (2004) Effect of L-cysteine, kojic acid and 4-hexylresorcinol combination on inhibition of enzymatic browning in Amasya apple juice. J. Food Eng. 62: 299-304.
114. Janolino, V.G., and Swaisgood, H.E. (1975) Isolation and characterization of sulfhydryl oxidase from bovine milk. J. Biol. Chem. 250: 2532-2538.
115. Janolino, V.G., and Swaisgood, H.E. (1992) A comparison of sulfhydryl oxidases from bovine milk and from Aspergillus niger. Milchwissenschaft 47: 143-146.
116. Jaros, D., Partschefeld, C., Henle, T., and Rohm, H. (2006) Transglutaminase in dairy products: chemistry, physics and applications. J. Texture Studies 37: 113-155.
117. Jiménez Colmenero, F., Ayo, M.J., and 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: 781-788. (Pubitemid 40119934)
118. Joseph, D., Lanier, T.C., and Hamann, D.D. (1994) Temperature and pH affect transglutaminase-catalyzed "setting" of crude fish actomyosin. J. Food Sci. 59: 1018-1036.
119. Kahn, D.R., and Cohen, I. (1981) Factor XIIIa - catalyzed coupling of structural proteins. Biochim. Biophys. Acta 668: 490-494. (Pubitemid 11086372)
120. Kato, T., Ito, S., and Fujita, K. (1986) Tyrosinase-catalyzed binding of 3,4-dihydroxyphenylalanine with proteins through the sulfhydryl group. Biochim. Biophys. Acta 881: 415-421. (Pubitemid 16033458)
121. Kim, Y.J., and Uyama, H. (2005) Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future. Cell. Mol. Life Sci. 62: 1707-1723.
122. Kim, S.-H., Carpenter, J.A., Lanier, T.C., and Wicker, L. (1993) Polymerization of beef actomyosin induced by transglutaminase. J. Food Sci. 58: 473-474, 491.
123. Kobayashi, E., Hashiguchi, K., Yikozeki, K., and Yamanaka, S. (1998) Molecular cloning of the transglutaminase gene from Bacillus subtilis and its expression in Escherichia coli. Biosci. Biotech. Biochem. 62: 1109-1114. (Pubitemid 128474979)
124. Kona, R.P., Qureshi, N., and Pai, J.S. (2001) Production of glucose oxidase using Aspergillus niger and corn steep liquor. Bioresource Technol. 78: 123-126. (Pubitemid 32215526)
125. Kramer, K.J., Kanost, M.R., Hopkins, T.L., Jiang, H., Zhu, Y., Xu, R., Kerwin, J.L., and Turecek, F. (2001) Oxidative conjugation of catechols with proteins in insect skeletal systems. Tetrahedron 57: 385-392. (Pubitemid 32112627)
126. Krieg, R., and Halbhuber, K.-J. (2003) Recent advances in catalytic peroxidase histochemistry. Cellular Mol. Biol. 49: 547-563.
127. Krylov, S., and Dunford, H.B. (1996) Reaction of horse radish peroxidase with indole-3-acetic acid. In: Plant peroxidases: Biochemistry and physiology. Obinger, C., Burner, U., Ebermann, R., Penel, C., and Greppin, H. (Eds.). Univ. of Geneva, Geneva, Switzerland. Pp. 59-69.
128. Kubo, I., Kinst-Hori, I., Kubo, Y., Yamagiwa, Y., Kamikawa, T., and Haraguchi, H. (2000) Molecular design of antibrowning agents. J. Agric. Food Chem. 48: 1393-1399. (Pubitemid 30243716)
129. Kubo, I., Chen, Q.-X., and Nihei, K. (2003) Molecular design of antibrowning agents: antioxidative tyrosinase inhibitors. Food Chem. 81: 241-247. (Pubitemid 36411728)
130. Kuraishi, C. (2000) Application of transglutaminase for food processing. Hydrocoll. 2: 281-285.
131. Kuraishi, C., Sakamoto, J., Yamazaki, K., Susa, Y., Kuhara, C., and Soeda, T. (1997) Production of restructured meat using microbial transglutaminase without salt or cooking. J. Food Sci. 62: 488-490, 515.
132. Kuraishi, C., Yamazaki, K., and Susa, Y. (2001) Transglutaminase: Its utilization in the food industry. Food Rev. Int. 17: 221-246.
133. Kurth, L. (1983) Crosslinking of myosin and casein by the enzyme transglutaminase. Food Technology in Australia 35: 420-423.
134. Kurth, K., and Rogers, P.J. (1984) Transglutaminase catalyzed cross-linking of myosin to soya protein, casein and gluten. J. Food Sci. 49: 573-576.
135. Kusakabe, H., Kuninaka, A., and Yoshino, H. (1982) Purification and properties of a new enzyme, glutathione oxidase from Penicillium sp. K-6-5. Agric. Biol. Chem. 46: 2057-2067.
136. Kuuva, T., Lantto, R., Reinikainen, T., Buchert, J., and Autio, K. (2003) Rheological properties of laccase-induced sugar beet pectin gels. Food Hydrocoll. 17: 679-684.
137. Kwon, B.S., Haq, A.K., Pomerantz, S.H., and Halaban, R. (1987) Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proc. Nat. Acad. Sci. 84: 7473-7477. (Pubitemid 18035714)
138. Kütemeyer, C., Froeck, M., Werlein, H.-D., and Watkinson, B.M. (2005) The influence of salts and temperature on enzymatic activity of microbial transglutaminase. Food Control 16: 735-737. (Pubitemid 40331424)
139. Köksel, H., Sivri, D., Ng, P.K.W., and Steffe, J.F. (2001) Effects of transglutaminase enzyme on fundamental rheological properties of sound and bug-damaged wheat flour doughs. Cereal Chem. 78: 26-30. (Pubitemid 32095760)
140. Labat, E., Morel, M.H., and Rouau, X. (2000) Effect of laccase and ferulic acid on wheat flour dough during mixing. Cereal Chem. 77: 823-828.
141. Lantto, R., Schönberg, C., Heine, E., and Buchert, J. (2004) Effects of laccasemediator combinations on wool. Textile Res. J. 74: 713-717.
142. Lantto, R., Heine, E., Freddi, G., Lappalainen, A., Miettinen-Oinonen, A., Niku- Paavola, M.-L., and Buchert, J. (2005) Enzymatic modification of wool with tyrosinase and peroxidase. J. Textile Inst. 96: 109-116. (Pubitemid 40899912)
143. Lantto, R., Plathin, P., Niemistö, M., Buchert, J., and Autio, K. (2006) Effects of transglutaminase, tyrosinase and freeze-dried apple pomace powder on gel forming and structure of pork meat. LWT - Food Sci. Technol. 39: 1117-1124.
144. Larré, C., Denery-Papini, S., Popineau, Y., Deshayes, G., Desserme, C., and Lefebvre, J. (2000) Biochemical analysis and rheological properties of gluten modified by transglutaminase. Cereal Chem. 77: 32-38. (Pubitemid 30053670)
145. Lawrie, R.A. (1998) Lawrie's meat science. 6. edition. Woodhead Publishing Ltd., Cambridge, England.
146. Lee, H.-S. (2002) Tyrosinase inhibitors of Pulsatilla cernua root-derived materials. J. Agric. Food Chem. 50: 1400-1403.
147. Lee, H.G., Lanier, T.C., Hamann, D.D., and Kopp, J.A. (1997) Transglutaminase effects on low temperature gelation of fish protein gels. J. Food Sci. 62: 20-24. (Pubitemid 27295285)
148. Lee, M.-K., Kim, Y.-M., Kim, N.-Y., Kim, G.-N., Kim, S.-H., Bang, K.-S., and Park, I. (2002) Prevention of browning in potato with a heat-treated onion extract. Biosci. Biotechnol. Biochem. 66: 856-858. (Pubitemid 39251350)
149. Leonowicz, A., and Grzywnowicz, K. (1981) Quantitative estimation of laccase forms in some white-rot fungi using syringaldazine as a substrate. Enz. Microb. Technol. 3: 55-58. (Pubitemid 11458044)
150. Lerch, K. (1981) Copper monooxygenases: tyrosinase and dopamine β-monooxygenase. In: Metal ions in biological systems. Siegel, H. (Ed.). Marcel Decker Inc., New York. Pp. 143-186.
151. Lerch, K. (1983) Neurospora tyrosinase. Structural, spectroscopic and catalytic properties. Mol. Cell. Biochem. 52: 125-138.
152. Lersch, P., Weitemeyer, C., and Wollenweber, U. (2003) Compositions for skin lightening and toning in down pigment disorders, comprising creatinine and/or creatinine derivatives as active substances. US 2003/0180237.
153. Lesiów, T., and Xiong, Y.L. (2001a) Gelation properties of poultry myofibrillar proteins and comminuted poultry meat. Effect of protein concentration, pH and muscle type - A review. Fleischwirtschaft Int. 4: 39-44.
154. Lesiów, T., and Xiong, Y.L. (2001b) Mechanism of rheological changes in poultry myofibrillar proteins during gelation. Avian and Poultry Biology Rev. 12: 137-149. (Pubitemid 33676316)
155. Lewis, D.M. (1992) Wool printing. In: Wool dyeing. Lewis, D.M. (Ed.). Soc. of Dyers and Colorists, Bradford, England. Pp. 332-360.
156. Lim, C.H., and Yoo, J.Y. (2000) Synthesis of ortho-directed polyaniline using horseradish peroxidise. Process Biochem. 36: 233-241.
157. Lim, L.-T., Mine, Y., and Tung, M.A. (1998) Transglutaminase cross-linked egg white protein films: tensile properties and oxygen permeability. J. Agric. Food Chem. 46: 4022-4029. (Pubitemid 128488486)
158. Liu, N., Zhang, T., Wang, Y.J., Huang, Y.P., Ou, J.H., and Shen, P. (2004) A heat-inducible tyrosinase with distinct properties from Bacillus thuringiensis. Lett. Appl. Microbiol. 39: 407-412. (Pubitemid 39421146)
159. Locker, R.H. (1987) The non-sliding filaments of the sarcomere. Meat Sci. 20: 217-236.
160. Lorenzen, P.C., Neve, H., Mautner, A., and Schlimme, E. (2002) Effect of enzymatic cross-linking of milk proteins on functional properties of set-style yogurt. Int. Dairy Technol. 55: 152-157. (Pubitemid 34966655)
161. Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193: 265-275.
162. Macfarlane, J.J., Schmidt, G.R., and Turner, R.H. (1977) Binding of meat pieces: a comparison of myosin, actomyosin, and sarcoplasmic proteins as binding agents. J. Food Sci. 42: 1603-1604.
163. Malencik, D.A., and Anderson, S.R. (1996) Dityrosine formation in calmodulin: Cross-linking and polymerization catalyzed by Arthromyces peroxidase. Biochem. 35: 4375-4386. (Pubitemid 26113497)
164. Martinaud, A., Mercier, Y., Marinova, P., Tassy, C., Gatellier, P., and Renerre, M. (1997) Comparison of oxidative processes on myofibrillar proteins from beef during maturation and by different model oxidation systems. J. Agric. Food Chem. 45: 2481-2487. (Pubitemid 127476965)
165. Martins, L.O., Soares, C.M., Pereira, M.M., Teixeira, M., Costa, T., Jones, G.H., and Henriques, A.O. (2002) Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat. J. Biol. Chem. 277: 18849-18859. (Pubitemid 34952444)
166. Matheis, G., and Whitaker, J.R. (1984a) Modification of a protein by polyphenol oxidase and peroxidase and their products. J. Food Biochem. 8: 137-162.
167. Matheis, G., and Whitaker, J.R. (1984b) Peroxidase-catalyzed cross-linking of proteins. J. Protein Chem. 3: 35-48.
168. Matheis, G., and Whitaker, J.R. (1987) A review: Enzymatic cross-linking of proteins applicable to foods. J. Food Biochem. 11: 309-327.
169. Mathiasen, T.E. (1995) Laccase and beer storage. WO9521240.
170. Matoba, Y., Kumagai, T., Yamamoto, A., Yoshitsu, H., and Sugiyama, M. (2006) Crystallographic evidence the dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 281: 8981-8990. (Pubitemid 43848005)
171. Matsumura, Y., Lee, D.S., and Mori, T. (2000) Molecular weight distributions of α-lactalbumin polymers formed by mammalian and microbial transglutaminases. Food Hydrocoll. 14: 49-59.
172. Mattinen, M.-L., Kruus, K., Buchert, J., Nielsen, J.H., Andersen, H.J., and Steffensen, C.L. (2005) Laccase-catalyzed polymerization of tyrosine-containing peptides. FEBS J. 272: 3640-3650. (Pubitemid 41021176)
173. Mattinen, M.-L., Hellman, M., Permi, P., Autio, K., Kalkkinen, N., and Buchert, J. (2006) Effect of protein structure on laccase-catalyzed protein oligomerization. J. Agric. Food Chem. 54: 8883-8890. (Pubitemid 44797540)
174. Mayer, A.M., and Harel, E. (1979) Polyphenol oxidases in plants. Phytochem. 18: 193-215.
175. Mayer, A.M., and Staples, R.C. (2002) Laccase: new functions for an old enzyme. Phytochem. 60: 551-565. (Pubitemid 34832184)
176. Michon, T., Wand, W., Ferrasson, E., and Guéguen, J. (1999) Wheat prolamine crosslinking through dityrosine formation catalysed by peroxidases: Improvement in the modification of a poorly accessible substrate by "indirect"catalysis. Biotechnol. Bioeng. 63: 499-458.
177. Miller, K.A., and Hoseney, R.C. (1999) Effect of oxidation on the dynamic rheological properties of wheat flour-water doughs. Cereal Chem. 76: 100-104. (Pubitemid 29059135)
178. Millman, B.M., and Nickel, B.G. (1980) Electrostatic forces in muscle and cylindrical gel systems. Biophys. J. 32: 49-63.
179. Minussi, R.C., Pastore, G.M., and Durán, N. (2002) Potential applications of laccase in food industry. Trends Food Sci. Technol. 13: 205-216. (Pubitemid 35380997)
180. Montejano, J.G., Hamann, D.D., and Lanier, T.C. (1984) Thermally induced gelation of selected comminuted muscle systems - rheological changes during processing, final strengths and microstructure. J. Food Sci. 49: 1496-1505.
181. Motoki, M., and Seguro, K. (1998) Transglutaminase and its use for food processing. Trends Food Sci. Technol. 9: 204-210. (Pubitemid 28434053)
182. Mugumura, M., Tsuruoka, K., Fujino, H., Kawahara, S., Yamauchi, K., Matsumura, S., and Soeda, T. (1999) Gel strength enhancement of sausages by treating with microbial transglutaminase. Proc. 45th Int. Congr. Meat Sci. Technol. 1999. Vol. 1. Yokohama, Japan. Pp. 138-139.
183. Myllärinen, P., Buchert, J., and Autio, K. Effect of transglutaminase on rheological properties and microstructure of chemically acidified sodium caseinate gels. Int. Dairy J. (in press).
184. Nelson, G., and Jones, C.A. (1998) Adhesives. WO 99/52988.
185. Nerya, O., Vaya, J., Musa, R., Izrael, S., Ben-Arie, R., and Tamir, S. (2003) Glabrene and isoliquiritigenin as tyrosinase inhibitors from licorice roots. J. Agric. Food Chem. 51: 1201-1207.
186. Nicolas, J.J., Richard-Forget, F.C., Goupy, P.M., Amiot, M., and Aubert, S.Y. (1994) Enzymatic browning reactions in apple and apple products. Crit. Rev. Food Sci. Nutr. 34: 109-157.
187. Nielsen, P.M. (1995) Reactions and potential industrial applications of transglutaminase. Review of literature and patents. Food Biotechnol. 9: 119-156.
188. Nielsen, G.S., Petersen, B.R., and Møller, A.J. (1995) Impact of salt, phosphate and temperature on the effect of a transglutaminase (F XIIIa) on the texture of restructured meat. Meat Sci. 41: 293-299.
189. Nio, N., Motoki, M., and Takinami, K. (1985) Gelation of casein and soybean globulins by transglutaminase. Agric. Biol. Chem. 49: 2283-2286.
190. Nonaka, M., Tanaka, H., Okiyama, A., Motoki, M., Ando, H., Umeda, K., and Matsuura, A. (1989) Polymerization of several proteins by Ca2+ -independent transglutaminases derived from microorganisms. Agric. Biol. Chem. 53: 2619-2623. (Pubitemid 20077526)
191. Norsker, M., Jensen, M., and Adler-Nissen, J. (2000) Enzymatic gelation of sugar beet pectin in food products. Food Hydrocoll. 14: 237-243.
192. Nosanchuk, J.D., and Casadevall, A. 2003. The contribution of melanin to microbial pathogenesis. Cell. Microbiol. 5: 203-223. (Pubitemid 36511568)
193. Obinger, C., Burner, U., Voetsch, B., Hofstetter, W., and Ebermann, R. (1996) Reaction of peroxidases with thiols: hydrogen peroxide generation and the influence of thiols In: Plant peroxidases: Biochemistry and physiology. Obinger, C., Burner, U., Ebermann, R., Penel, C., and Greppin, H. (Eds.). Univ. of Geneva, Geneva, Switzerland. Pp. 106-112.
194. O'Connell, J.E., and de Kruif, C.G. (2003) β-casein micelles: cross-linking with transglutaminase. Colloids and Surfaces A: Physicochem. Eng. Aspects 216: 75-81.
195. Offer, G., and Trinick, J. (1983) On the mechanism of waterholding in meat: The swelling and shrinkage of myofibrils. Meat Sci. 8: 245-281.
196. Offer, G., and Knight, P. (1988a) The structural basis of water-holding capacity in meat. Part 1. General principles and water uptake in meat processing. In: Developments in meat science. Vol. 4. Lawrie, R. (Ed.). Elsevier Applied Science, London, U.K. Pp. 63-171.
197. Offer, G., and Knight, P. (1988b) The structural basis of water-holding capacity in meat. Part 2: Drip losses. In: Developments in meat science. Vol. 4. Lawrie, R. (Ed.). Elsevier Applied Science, London, U.K. Pp. 173-243.
198. Ofstad, R., Kidman, S., Myklebust, R., and Hermansson, A.-M. (1993) Liquid holding capacity and structural changes during heating of fish muscle: cod (Gadus morhua L.) and salmon (Salmo salar). Food Structure 12: 163-174.
199. Ostrowski, M.C., and Kistler, W.S. (1980) Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion. Biochem. 19: 2639-2645.
200. Ouali, A. (1992) Proteolytic and physiochemical mechanisms involved in meat texture development. Biochimie 74: 251-265.
201. Ouali, A., Herrera-Mendez, C.H., Coulis, G., Samira, B., Boudjellal, A., Aubry, L., and Sentandreu, M.A. (2006) Revisiting the conversion of muscle into meat and the underlying mechanisms. Meat Sci. 74: 44-58. (Pubitemid 43975231)
202. Ozer, B., Kirmaci, H.A., Oztekim, S., Hayaloglu, A., and Atamer, M. (2007) Incorporation of microbial transglutaminase into non-fat yogurt production. Int. Dairy J. 17: 199-207. (Pubitemid 44708748)
203. Pasternack, R., Dorsch, S., Otterbach, J.T., Robenek, I.R., Wolf, S., and Fucshbauer, H.L. (1998) Bacterial pro-transglutaminase from Streptoverticellum mobaraense: purification, characterization and sequence of zymogen. Eur. J. Biochem. 257: 570-576. (Pubitemid 28512124)
204. Pearlstone, J.R., Carpenter, J.P., and Smillie, L.B. (1976) Amino-acid sequence of tropomyosin - binding component of rabbit skeletal muscle troponin. Proc. Natl. Acad. Sci. U.S.A. 73: 1902-1906.
205. Pierpoint, W.S. (1969) O-quinones formed in plant extracts. Biochem. J. 112: 619-629.
206. Pietrasik, Z., and Li-Chan, E.C.Y. (2002) Binding and textural properties of beef gels as affected by protein, κ-carrageenan and microbial transglutaminase addition. Food Res. Int. 35: 91-98. (Pubitemid 34775866)
207. Pomerantz, S.H., and Ances, I.G. (1975) Tyrosinase activity in human skin. J. Clin. Investigation 55: 1127-1131.
208. Poulsen, C., and Bak Høstrup, P. (1998) Purification and characterization of a hexose oxidase with excellent strengthening effects in bread. Cereal Chem. 75: 51-57. (Pubitemid 28131984)
209. Puolanne, E., and Turkki, P. (1985) The effect of freeze storage on the water binding capacity of the raw materials of cooked sausage. Proc. Eur. Meeting of Meat Res. Workers, No. 31: 583-586.
210. Ramirez, J., Uresti, R., Téllez, S., and Vásquez, M. (2002) Using salt and microbial transglutaminase as binding agents in restructured fish products resembling hams. J. Food Sci. 67: 1778-1784. (Pubitemid 34817092)
211. Ramirez-Suarez, J.C., Xiong, Y.L., and Wang, B. (2001) Transglutaminase crosslinking of bovine cardiac myofibrillar proteins and its effect on protein gelation. J. Muscle Food 12: 85-96.
212. Ramirez-Suarez, J.C., and Xiong, Y.L. (2002a) Transglutaminase cross-linking of whey/myofibrillar proteins and the effect on protein gelation. J. Food Sci. 67: 2885-2891. (Pubitemid 35376165)
213. Ramirez-Suarez, J.C., and Xiong, Y.L. (2002b) Rheological properties of mixed muscle/nonmuscle protein emulsions treated with transglutaminase at two ionic strengths. Int. J. Food Sci. Technol. 38: 777-785. (Pubitemid 37218323)
214. Ramirez-Suarez, J.C., and Xiong, Y.L. (2003) Effect of transglutaminaseinduced cross-linking on gelation of myofibrillar/soy protein mixtures. Meat Sci. 65: 899-907. (Pubitemid 36747732)
215. Ramirez-Suarez, J.C., Addo, K., and Xiong, Y.L. (2005) Gelation of mixed myofibrillar/wheat gluten proteins treated with microbial transglutaminase. Food Res. Int. 38: 1143-1149. (Pubitemid 41097554)
216. Ramsohoye, P.V., and Kozlov, I.A. (1991) Isoprotein composition and crosslinking of thaumatins using mushroom tyrosinase and dimethyl suberimidate. Int. J. Food Sci. Technol. 26: 271-282.
217. Rasiah, I.A., Sutton, K.H., Low, F.L., Lin, H.-M., and Gerrard, J.A. (2005) Cross-linking of wheat dough by glucose oxidase and the resulting effects on bread and croissants. Food Chem. 89: 325-332. (Pubitemid 39195102)
218. Rescigno, A., Sollai, F., Pisu, B., Rinaldi, A., and Sanjust, E. (2002) Tyrosinase inhibition: General and applied aspects. J. Enz. Inhibition and Med. Chem. 17: 207-218. (Pubitemid 35175257)
219. Rittstieg, K., Suurnäkki, A., Suortti, T., Kruus, K., Guebitz, G., and Buchert, J. (2002) Investigations on the laccase-catalyzed polymerization of lignin model compounds using size-exclusion HPLC. Enzyme Microb. Technol. 31: 403-410. (Pubitemid 34874820)
220. Robb, D.A. (1984) Tyrosinase. In: Copper proteins and copper enzymes. Vol. 2. Lontie, R. (Ed.). CRC Press Inc., Boca Raton FL. Pp. 207-240.
221. Rolle, R.S., Guizani, N., Chen, J.S., Marshall, M.R., Yang, J.S., and Wei, C.I. (1991) Purification and characterization of phenol oxidase isoforms form Taiwanese black tiger shrimp (Penaeus monodon). J. Food Biochem. 15: 17-32.
222. Ruusunen, M., and Puolanne, E. (2005) Reducing sodium intake from meat products. Meat Sci. 70: 531-541.
223. Sakamoto, H., Kumazawa, Y., and Motoki, M. (1994) Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. J. Food Sci. 59: 866-871. (Pubitemid 2143879)
224. Sampaio, S., Taddei, P., Monti, P., Buchert, J., and Freddi, G. (2005) Enzymatic grafting of chitosan onto Bombyx mori silk fibroin: kinetic and IR vibrational studies. J. Biotechnol. 116: 21-33. (Pubitemid 40126164)
225. Sánchez-Ferrer, Á., Rodríguez-López, J.N., García-Cánovas, F., and García-Carmona, F. (1995) Tyrosinase: a comprehensive review of its mechanism. Biochim. Biophys. Acta 1247: 1-11.
226. Sarkar, N.K., Clarke, D.D., and Waelsch, H. (1957) An enzymatically catalyzed incorporation of amines into proteins. Biochim. Biophys. Acta 25: 451-452.
227. Schorsch, C., Carrie, H., Clark, A.H., and Norton, I.T. (2000a) Cross-linking casein micelles by a microbial transglutaminase: conditions for formation of transglutaminase-induced gels. Int. Dairy J. 10: 519-528.
228. Schorsch, C., Carrie, H., Clark, A.H., and Norton, I.T. (2000b) Cross-linking casein micelles by a microbial transglutaminase: influence of cross-links in acid-induced gelation. Int. Dairy J. 10: 529-539.
229. Seguro, K., Kumazawa, Y., Ohtsuka, T., Toiguchi, S., and Motoki, M. (1995) Microbial transglutaminase and ε-(γ-glutamyl)lysine crosslink effects on elastic properties of kamaboko gels. J. Food Sci. 60: 305-311.
230. Selinheimo, E., Kruus, K., Buchert, J., Hopia, A., and Autio, K. (2005) Effects of laccase, xylanase and their combination on the rheological properties of wheat doughs. J. Cereal Sci. 43: 152-159.
231. Selinheimo, E., Saloheimo, M., Ahola, E., Westerholm-Parvinen, A., Kalkkinen, N., Buchert, J., and Kruus, K. (2006) Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei. FEBS J. 273: 4322-4335. (Pubitemid 44326511)
232. Sentandreu, M.A., Coulis, G., and Ouali, A. (2002) Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends Food Sci. Technol. 13: 400-421.
233. Seo, S.-Y., Sharma, V.K., and Sharma, N. (2003) Mushroom tyrosinase: Recent prospects. J. Agric. Food Chem. 51: 2837-2853.
234. Serafini-Fracassini, D., Del Duca, S., and Beninati, S. (1995) Plant transglutaminases. Phytochem. 40: 355-365.
235. Shi, Y., Chen, Q.-X., Wang, Q., Song, K.-K., and Qiu, L. (2005) Inhibitory effects of cinnamic acid and its derivatives on the diphenolase activity of mushroom (Agaricus bisporus) tyrosinase. Food Chem. 92: 707-712. (Pubitemid 40544815)
236. Singer, M.A., Hortsch, M., Goodman, C.S., and Bentley, D. (1992) Annulin, a protein expressed at limb segment boundaries in the grasshopper embryo, is homologous to protein cross-linking transglutaminases. Dev. Biol. 154: 143-159.
237. Singh, H. (1991) Modification of food proteins by covalent crosslinking. Trends in Food Sci. Technol. 2: 196-200.
238. Siu, N.-C., Ma, C.-Y., Mock, W.-Y., and Mine, Y. (2002) Functional properties of oat globulin modified by a calcium-independent microbial transglutaminase. J. Agric. Food Chem. 50: 2666-2672. (Pubitemid 34437385)
239. Sliwkowski, M.X., Swaisgood, H.E., Clare, D.A., and Horton, H.R. (1984) Kinetic mechanism and specificity of bovine milk sulfhydryl oxidase. Biochem. J. 220: 51-55.
240. Smiddy, M.A., Martin, J.E.G.H., Kelly, A.L., de Kruif, C.G., and Huppertz, T. (2006) Stability of casein micelles cross-linked by transglutaminase. J. Dairy Sci. 89: 1906-1914. (Pubitemid 44365777)
241. Smith, A.T., and Veitch, N.C. (1998) Substrate binding and catalysis in heme peroxidises. Curr. Opinion Chem. Biol. 2: 269-278. (Pubitemid 128428135)
242. Sodini, I., Remeuf, F., Haddad, S., and Corrieu, G. (2004) The relative effect of milk base, starter, and process on yogurt texture: a review. Crit. Rev. Food and Nutrition 44: 113-137. (Pubitemid 38552287)
243. Solomon, E.I., Sundaran, U.M., and Machonkin, T.E. (1996) Multicopper oxidases and oxygenases. Chem. Rev. 96: 2563-2605. (Pubitemid 126641113)
244. Stabursvik, E., and Martens, H. (1980) Thermal denaturation of proteins in post rigor muscle tissue as studied by differential scanning calorimetry. J. Sci. Food Agric. 31: 1034-1042.
245. Stahmann, M.A., Spencer, A.K., and Honold, G.R. (1977) Cross linking of proteins in vitro by peroxidase. Biopolymers 16: 1307-1318. (Pubitemid 8111336)
246. Starr, R., and Offer, G. (1971) Polypeptide chains of intermediate molecular weight in myosin preparations. FEBS Lett. 15: 40-44.
247. Suderman, R.J., Dittmer, N.T., Kanost, M.R., and Kramer, K.J. (2006) Model reactions for insect cuticle sclerotization: Crosslinking of recombinant proteins upon their laccase-catalyzed oxidative conjugation with catechols. Insect Biochem. Mol. Biol. 36: 353-365.
248. Sugumaran, M. (1991) Molecular mechanisms for mammalian melanogenesis. Comparison with insect sclerotization. FEBS Lett. 293: 233-239.
249. Sullivan, J.D., and Ikawa, M. (1973) Purification and characterization of hexose oxidase from the red alga Chondrus crispus. Biochim. Biophys. Acta 309: 11-22.
250. Suzuki, S., Izawa, Y., Kobayashi, K., Eto, Y., Yamanaka, Y., Kubota, K., and Yokozeki, K. (2000) Purification and characterization of novel transglutaminase from Bacillus subtilis spores. Biosci. Biotechnol. Biochem. 64: 2344-2351.
251. Swaisgood, H.E. (1977) Process of removing the cooked flavor from milk. US 4053644.
252. Takasaki, S., and Kawakishi, S. (1997) Formation of protein-bound 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine as new cross-linkers in gluten. J. Agric. Food Chem. 45: 3472-3475. (Pubitemid 127485882)
253. Takasaki, S., Kawakishi, S., Murata, M., and Homma, S. (2001) Polymerisation of gliadin mediated by mushroom tyrosinase. Lebensm.-Wiss. u.-Technol. 34: 507-512. (Pubitemid 34415927)
254. Thalmann, C.R., and Lötzbeyer, T. (2002) Enzymatic cross-linking of proteins with tyrosinase. Eur. Food Res. Technol. 214: 276-281.
255. Thorpe, C., Hoober, K.L., Raje, S., Glynn, N.M., Burnside, J., Turi, G.K., and Coppock, D.L. (2002) Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Archives Biochem. Biophys. 405: 1-12. (Pubitemid 35026160)
256. Thurston, C.F. (1994) The structure and function of fungal laccases. Microbiology 140: 19-26.
257. Tilley, K.A., Benjamin, R.E., Bagorogoza, K.E., Moses Oket-Kotber, B., Praskash, O., and Kwen, H. (2001) Tyrosine cross-links: Molecular basis of gluten structure and function. J. Agric. Food Chem. 49: 2627-2632. (Pubitemid 32843301)
258. Tornberg, E. (2005) Effects of heat on meat proteins - implications on structure and quality of meat products. Meat Sci. 70: 493-508.
259. Trespalacios, P., and Pla, R. (2007) Simultaneous application of transglutaminase and high pressure to improve functional properties of chicken meat gels. Food Chem. 100: 264-272.
260. Tsai, G.-J., Lin, S.-M., and Jiang, S.-T. (1996) Transglutaminase from Streptoverticillium ladakanum and application to minced fish product. J. Food Sci. 61: 1234-1238. (Pubitemid 27025551)
261. Tseng, T.-F., Liu, D.-C., and Chen, M.-T. (2000) Evaluation of transglutaminase on the quality of low-salt chicken meat-balls. Meat Sci. 55: 427-431.
262. Tseng, T.-F., Chen, M.-T., and Liu, D.-C. (2002) Purification of transglutaminase and its effects on myosin heavy chain and actin of spent hens. Meat Sci. 60: 267-270. (Pubitemid 36537488)
263. Tsuchiya, R., Petersen, B.R., and Christensen, S. (2000) Reduction of malodour. US6074631.
264. Tzeng, S.S., Yin, L.-J., Chen, G.-H., and Jiang, S.-T. (2005) Molecular cloning of microbial transglutaminase from Streptoverticillium ladakanum BCRC 12422. J. Fish. Soc. Taiwan 32: 53-67.
265. Uresti, R.M., Téllez-Luis, S.J., Ramírez, J.A., and Vázques, M. (2004) Use of dairy proteins and microbial transglutaminase to obtain low-salt fish products from filleting waste from silver carp (Hypophthalmichthys molitrix). Food Chem. 86: 257-263.
266. Vamos-Vigyazo, L. (1981) Polyphenol oxidase and peroxidase in fruits and vegetables. Crit. Rev. Food Sci. Nutr. 15: 49-127.
267. van Dijken, J.P., and Veenhuis, M. (1980) Cytochemical localization of glucose oxidase in peroxisomes of Aspergillus niger. Eur. J. Appl. Microbiol. Biotechnol. 9: 275-283.
268. van Oort, M. (1996) Oxidases in baking. Int. Food Ingredients. No. 4: 42-45.
269. Vansteenskiste, E., Babot, C., Rouau, X., and Micard, V. (2004) Oxidative gelation of feruloylated arabinoxylan as affected by protein. Influence on protein enzymatic hydrolysis. Food Hydrocoll. 18: 557-564.
270. Veitch, N.C. (2004) Horseradish peroxidase: a modern view of a classic enzyme. Phytochem. 65: 249-259.
271. Vermulapalli, V., Miller, K.A., and Hoseney, R.C. (1998) Glucose oxidase in bread making systems. Cereal Chem. 75: 439-442. (Pubitemid 28348733)
272. Vroeman, A.J. (2003) Glucose oxidase. In: Handbook of food enzymology. Whitaker, J.R., Voragen, A.G.J., and Wong, D.W.S. (Eds.). Marcel Dekker Inc., New York. Pp. 425-432.
273. Wagner, M., and Nicell, J.A. (2002) Impact of dissolved wastewater constituents on peroxidise-catalyzed treatment of phenol. J. Chem. Technol. Biotechnol. 77: 419-428. (Pubitemid 34256492)
274. Walls, E.W. (1960) The microanatomy of muscle. In: The structure and function of muscle. Vol. 1. Bourne, G.H. (Ed.). Academic Press, New York and London. Pp. 21-61.
275. Wang, K., and Wright, J. (1988) Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line. J. Cell Biol. 107: 2199-2212. (Pubitemid 19015099)
276. Wardman, P. (2002) Indole-3-acetic acid and horseradish peroxidase: A new prodrug/enzyme combination for targeted cancer therapy. Curr. Pharmaceutical Design 8: 1363-1374.
277. Weraarchakul-Boonmark, N., Jeong, J., Murthy, S.N.P., Engel, J.D., and Lorand, L. (1992) Cloning and expression of chicken erythrocyte transglutaminase. Proc. Natl. Acad. Sci. USA 89: 9804-9808.
278. Whitaker, J.R., Voragen, A.G.J., and Wong, D.W.S. (2003) Handbook of food enzymology. Marcel Dekker Inc., New York.
279. Wijngaards, G., and Paardekoopper, E.J.C. (1988) Preparation of a composite meat product by means of enzymatically formed protein gels. In: Trends in modern meat technology. Vol. 2. Krols, B., van Room, P.S., and Houben, J.H. (Eds.). Pudoc, Wageningen, the Netherlands. Pp. 125-129.
280. Wijngaards, G., Zhu, Y., Maagd, J.M., and Bol, J. (1997) Transglutaminase as a potential tool in developing new protein ingredients and foods. Med. Fac. Landbouw Univ. Gent 62: 1381-1383.
281. Williamson, P.R. (1994) Biochemical and molecular characterization of the diphenol oxidase of Cryptococcus neoformans: identification as a laccase. J. Bacteriol. 176: 656-664.
282. Worratao, A., and Yongsawatdigul, J. (2003) Cross-linking of actomyosin by crude tilapia (Oreochromis niloticus) transglutaminase. J. Food Biochem. 27: 35-51. (Pubitemid 36564438)
283. Wright, D.J., Leach, I.B., and Wilding, P. (1977) Differential scanning calorimetric studies of muscle and its constituent proteins. J. Sci. Food Agric. 28: 557-564.
284. Wu, L.-C., Chen, Y.-C., Ho, J.A., and Yang, C.-S. (2003) Inhibitory effect of red koji extracts on mushroom tyrosinase. J. Agric. Food Chem. 51: 4240-4246.
285. Xiong, Y.L., Brekke, C.J., and Leung, H.K. (1987) Thermal denaturation of muscle proteins from different species and muscle types as studied by differential scanning calorimetry. Can. Inst. Food Sci. Technol. J. 20: 357-362.
286. Xiong, Y.L., and Brekke, C.J. (1989) Changes in protein solubility and gelation properties of chicken myofibrils during storage. J. Food Sci. 54: 1141-1146.
287. Xiong, Y.L., and Decker, E.A. (1995) Alterations of muscle protein functionality by oxidative and antioxidative processes. J. Muscle Foods 6: 139-160.
288. Xu, F. (1996) Oxidation of phenols, anilines, and benzenethiols by fungal laccases: correlation between activity and redox potentials as well as halide inhibition. Biochem. 35: 7608-7614.
289. Xu, F. (1997) Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases. J. Biol. Chem. 272: 924-928.
290. Yamaguchi, S. (2000) Method for cross-linking protein by using enzyme. US 6121013.
291. Yamazaki, K., and Nishimura, Y. (2002) Method for producing noodles. US 6403127.
292. Yaropolov, A.I., Skorobogatko, O.V., Vartanov, S.S., and Varfolomeyev, S.D. (1994) Laccase. Properties, catalytic mechanism and applicability. Appl. Biochem. Biotechnol. 49: 257-280.
293. Yasui, T., Ishioroshi, M., and Samejima, K. (1980) Heat induced gelation of myosin in the presence of actin. J. Food Sci. 44: 61-78.
294. Yoruk, R., and Marshall, M.R. (2003) Physicochemical properties and function of plant polyphenol oxidase: A review. J. Food Biochem. 27: 361-422. (Pubitemid 38034245)
295. Yuang, Z.Y., and Jiang, T.J. (2003) Horse radish peroxidase. In: Handbook of food enzymology. Whitaker, J.R., Voragen, A., and Wong, D.W.S. (Eds.). Marcel Dekker Inc., New York. Pp. 403-411.
296. Zawistowski, J., Biliaderis, C.G., and Eskin, N.A.M. (1991) Polyphenol oxidase. In: Oxidative enzymes in foods. Robinson, D.S., and Eskin, N.A.M. (Eds.). Elsevier Science Publishers, London. Pp. 217-273.
297. Zetelaki, K., and Vas, K. (1968) The role of aeration and agitation in the production of glucose oxidase in submerged culture. Biotechnol. Bioeng. 10: 45-59.
298. Zhao, J., and Kwan, H.S. (1999) Characterisation, molecular cloning and differential expression analysis of laccase genes from the edible mushroom Lentinula edodes. Appl. Environ. Microbiol. 65: 4908-4913.
299. Zhu, Y., Bol, J., Rinzema, A., Tramper, J., and Wijngaards, G. (1999) Transglutaminase as a potential tool in developing novel protein foods. Agro-Food Hi-Tech January/February: 8-10.