The ε-(γ-Glutamyl)lysine moiety in crosslinked casein is an available source of lysine for rats

Journal of Nutrition

Volumn 126, Issue 10, 1996, Pages 2557-2562

  Seguro, Katsuya ^a   Kumazawa, Yoshiyuki ^a   Kuraishi, Chiya ^a   Sakamoto, Hiroko ^a   Motoki, Masao ^a  

^a AJINOMOTO CO INC   (Japan)

Author keywords

bioavailability; rats; transglutaminase; glutamyltransferase; ( glutamyl)lysine

Indexed keywords

6 (GAMMA GLUTAMYL)LYSINE; CASEIN; GLUTEN; LYSINE; DIPEPTIDE; EPSILON (GAMMA GLUTAMYL) LYSINE; EPSILON-(GAMMA-GLUTAMYL)-LYSINE; GAMMA GLUTAMYLTRANSFERASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

AMINO ACID METABOLISM; ANIMAL EXPERIMENT; ARTICLE; BIOAVAILABILITY; CONTROLLED STUDY; DIET SUPPLEMENTATION; FOOD COMPOSITION; GROWTH RATE; MALE; NONHUMAN; RAT; ANIMAL; CHEMISTRY; EATING; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; METABOLISM; PHYSIOLOGY; PROTEIN INTAKE; WEIGHT GAIN; WISTAR RAT;

ANIMALIA; TRITICUM AESTIVUM;

ANIMALS; BIOLOGICAL AVAILABILITY; CASEINS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DIETARY PROTEINS; DIPEPTIDES; EATING; GAMMA-GLUTAMYLTRANSFERASE; GLUTEN; LYSINE; MALE; RATS; RATS, WISTAR; TRANSGLUTAMINASES; WEIGHT GAIN;

EID: 0029662180     PISSN: 00223166     EISSN: None     Source Type: Journal    
DOI: 10.1093/jn/126.10.2557     Document Type: Article

References (27)

1. Ando, H., Adachi, M., Umeda, K., Matsuura, A., Nonaka, M., Uchio, R., Tanaka, H. & Motoki, M. (1989) Purification and characteristics of a novel transglutaminase derived from microorganisms. Agric. Biol. Chem. 53: 2613-3617.
2. Asquith, R. S., Otterburn, M. S. & Sinclair, W. J. (1974) Isopeptide crosslinks-their occurrence and importance in protein structure. Angew. Chem. Int. Edit. 13: 514-520.
3. Fink, M. L., Chung, S. I. & Folk, J. E. (1980) γ-Glutamylamine cyclotransferase: specificity toward ε-(L-γ-glutamyl)-L-lysine and related compounds. Proc. Nad. Acad. Sci. U.S.A. 77: 4564-4568.
4. Finot, P.-A., Mottu, F., Bujard, E. & Mauron, J. (1978) N-Substituted lysines as sources of lysine in nutrition. In: Nutritional Improvement of Food and Feeds Proteins (Friedman, M., ed.), pp. 549-570. Plenum, London, UK.
5. Folk, J. E. (1983) Mechanism and basis for specificity of transglutaminase-catalyzed ε-(γ-glutamyl)lysine bond formation. Adv. Enzymol. Relat. Areas Mol. Biol. 54: 1-56.
6. Folk, J. E. & Chung, S. I. (1973) Molecular and catalytic properties of transglutaminase. Adv. Enzymol. 38: 109-191.
7. Folk, J. E. & Finlayson, J. S. (1977) The ε-(7-glutamyl)lysine cross-link and the catalytic role of transglutaminase. Adv. Protein Chem. 31: 1-133.
8. Friedman, M. & Finot, P.-A. (1990) Nutritional improvement of bread with lysine and γ-glutamyllysine. J. Agric. Food Chem. 38: 2011-2020.
9. Hurrell, R. F., Carpenter, K. J., Sinclair, W. J., Otterburn, M. S. & Asquith, R. S. (1976) Mechanisms of heat damage in proteins. Br. J. Nutr. 35: 383-395.
10. Kato, A., Wada, T., Kobayashi, K., Seguro, K. & Motoki, M. (1991) Ovomucin-food protein conjugates prepared through the transglutaminase reaction. Agric. Biol. Chem. 55: 1027-1031.
11. Kumazawa, Y., Seguro, K., Takamura, M. & Motoki, M. (1993) Formation of ε(γ-glutamyl)lysine cross-link in cured Horse mackerel meat induced by drying process. J. Food Sci. 58: 1062-1064, 1083.
12. ε-(γ-glutamyl)lysine crosslink: method of analysis, occurrence in extracellular and cellular proteins. Methods Enzymol. 107: 241-257.
13. Mauron, J. (1970) Le comportement chimique des proteines lors de la preparation des aliments et ses incidences biologiques. J. Int. Vitaminol. 40: 209-227.
14. s1-Casein film prepared using transglutaminase. Agric. Biol. Chem. 51: 992-996.
15. National Research Council (1978) Nutrient Requirements of the Laboratory Rat. In: Nutrient Requirements of Domestic Animals: Nutrient Requirement of Laboratory Animals. No. 10, (3rd ed.), National Academy of Sciences, Washington, DC.
16. Nonaka, M., Sakamoto, H., Toiguchi, S., 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.
17. Nonaka, M., Toiguchi, S., Sakamoto, H., Kawajiri, H., Soeda, T. & Motoki, M. (1994) Changes caused by microbial transglutaminase on physical properties of thermally induced soy protein gels. Food Hydrocolloids 8: 1- 8.
18. Otterburn, M., Healy M. & Sinclair, W. (1977) The formation, isolation and importance of isopeptides in heated proteins. In: Protein Crosslinking, Nutritional and Medical Consequences. Adv. Exp. Med. Biol. 86B: 239-262.
19. Raczynski, G., Snochowski, M. &. Buraczewski, S. (1975) Metabolism of ε-(γ-L-glutamyl)-L-lysine in the rat. Br. J. Nutr. 34: 291-296.
20. Sakamoto, H., Kumazawa, Y., Kawajiri, H. &. Motoki, M. (1995) ε-(γ-Glutamyl)lysine crosslink distribution in foods as determined by improved method. J. Food Sci. 60: 416-419.
21. Sakamoto, H., Kumazawa, Y. & Motoki, M. (1994) Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. J. Food Sci. 59: 866-871.
22. Seguro, K., Kumazawa, Y., Ohtsuka, T., Ide, H., Nio, N., Motoki, M. & Kubota, K. (1995) ε-(γ-Glutamyl)lysine: hydrolysis by γ-glutamyltransferase of different origins, when free or protein bound. J. Agric. Food Chem. 43: 1977-1981.
23. Sugawara, K. & Soejima, M., (1986) Kjeldahl method. In: Quantitation of Proteins, 2nd ed., (Uritani, Y., Shimura, K., Nakamura, M. & Funatsu, M., eds.), pp. 25-73. Gakkai Shuppan Center, Tokyo, Japan.
24. Yoshida, M, (1971) Bioassay of protein. In. Animal Nutritional Evaluation (Morimoto, H., ed.), pp. 264-265.Yoken-dou, Tokyo, Japan.
25. Yoshida, M, (1989) Comparison of averages. In: Design of Experiments for Animal Husbandry, pp. 84-104. Yoken-dou, Tokyo, Japan.
26. Waibel, P. E. & Carpenter, K. J. (1972) Mechanisms of heat damage in proteins. Br. J. Nutr. 27: 509-515.
27. Washizu, K., Ando, K., Koikeda, S., Hirose, S., Matsuura, A., Takagi, H., Motoki, M. & Takeuchi, K. (1994) Molecular cloning of the gene for microbial transglutaminase from Streptoverticillium and its expression in Streptomyces lividans. Biosci. Biotech. Biochem. 58: 82-87.