Structure-physicochemical function relationships of soybean glycinin at subunit levels assessed by using mutant lines

Journal of Agricultural and Food Chemistry

Volumn 52, Issue 26, 2004, Pages 8197-8201

  Maruyama, Nobuyuki ^a   Prak, Krisna ^a   Motoyama, Shiori ^a   Choi, Seon Kang ^a,b   Yagasaki, Kazuhiro ^c   Ishimoto, Masao ^d   Utsumi, Shigeru ^a  

^a KYOTO UNIVERSITY   (Japan)

^b MARINE BIOTECHNOLOGY INSTITUTE   (Japan)

^c Nagano Ctrl Agric Exp Station   (Japan)

^d NATIONAL AGRICULTURAL RESEARCH CENTER FOR HOKKAIDO REGION   (Japan)

Author keywords

Emulsifying ability; Glycinin; Solubility; Soybean; Surface hydrophobicity; Thermal stability

Indexed keywords

GLYCININ; PROTEIN; PROTEIN SUBUNIT;

ARTICLE; DENATURATION; HYDROPHOBICITY; MUTANT; NONHUMAN; PH; PHYSICAL CHEMISTRY; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SOLUBILITY; SOYBEAN; STRUCTURE ANALYSIS; TEMPERATURE; THERMAL ANALYSIS; THERMOSTABILITY;

GLYCINE MAX;

EID: 11144219949     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf048786y     Document Type: Article

References (36)

1. Kito, M.; Moriyama, T.; Kimura, Y.; Kambara, H. Changes in plasma lipid levels in young healthy volunteers by adding an extruder cooked soy protein to conventional meals. Biosci., Biotechnol., Biochem. 1993, 57, 354-355.
2. Utsumi, S. Plant food protein engineering. In Advances in Food and Nutrition Research; Kinsella, J. E., Ed.; Academic Press: SanDiego, CA, 1992; pp 89-208.
3. Utsumi, S.; Matsumura, Y.; Mori, T. Structure-function relationships of soy proteins. In Food Proteins and Their Applications; Damodaran, S., Paraf, A., Eds.; Dekker: New York, 1997; pp 257-291.
4. Maruyama, N.; Sato, R.; Wada, Y.; Matsumura, Y.; Goto, H.; Okuda, E.; Nakagawa, S.; Utsumi, S. Structure-physicochemical function relationships of soybean β-conglycinin constituent subunits. J. Agric. Food Chem. 1999, 47, 5278-5284.
5. Maruyama, N.; Mohamad Ramlan, M. S.; Takahashi, K.; Yagasaki, K.; Goto, H.; Hontani, N.; Nakagawa, S.; Utsumi, S. The effect of the N-linked glycans on structural features and physicochemical functions of soybean β-conglycinin homotrimers. J. Am. Oil Chem. Soc. 2002, 79, 139-144.
6. Maruyama, N.; Mohamad Ramlan, M. S.; Takahashi, K.; Yagasaki, K.; Goto, H.; Hontani, N.; Nakagawa, S.; Utsumi, S. Structure-physicochemical function relationships of soybean β-conglycinin heterotrimers. J. Agric. Food Chem. 2002, 50, 4323-4326.
7. Mohamad Ramlan, M. S.; Maruyama, N.; Takahashi, K.; Yagasaki, K.; Higasa, T.; Matsumura, Y.; Utsumi, S. Biosci., Biotechnol., Biochem. 2004, 68, 1091-1096.
8. Mori, T.; Utsumi, S.; Nakamura, T. Formation of pseudoglycinins and their gel hardness. J. Agric. Food Chem. 1982, 30, 828-831.
9. Nakamura, T.; Utsumi, S.; Kitamura, K.; Harada, K.; Mori, T. Cultivar differences in gelling characteristics of soybean (Glycine max) glycinin. J. Agric. Food Chem. 1984, 32, 647-651.
10. Nakamura, T.; Utsumi, S.; Mori, T. Formation of pseudoglycinins from intermediary subunits of glycinin and their gel properties and network structure. Agric. Biol. Chem. 1985, 49, 2733-2740.
11. Lee, D.-S.; Matsumoto, S.; Hayashi, Y.; Matsumura, Y.; Mori, T. Differences in physical and structural properties of heat-induced gels from glycinins among soybean cultivars. Food Sci. Technol. Res. 2002, 8, 360-366.
12. Zhang, G.-Y.; Hayashi, Y.; Matsumoto, S.; Matsumura, Y.; Mori, T. Molecular species of glycinin in some soybean cultivars. Phytochemistry 2002, 60, 675-681.
13. Teraishi, M.; Takahashi, M.; Hajika, M.; Matsunaga, R.; Uematsu, Y.; Ishimoto, M. Suppression of soybean β-conglycinin genes by dominant gene, Scg-1. Theor. Appl. Genet. 2001, 103, 1266-1272.
14. Takahashi, M.; Uematsu, Y.; Kashiwaba, K.; Yagasaki, K.; Hajika, M.; Matsunaga, R.; Komatsu, K.; Ishimoto, M. Accumulation of high levels of free amino acids in soybean seeds through integration of mutations conferring seed protein deficiency. Planta 2003, 217, 577-586.
15. Nagano, T.; Hirotsuka, M.; Mori, H.; Kohyama, K.; Nishinari, K. Dynamic viscoelastic study on the gelation of 7S globulin from soybean. J. Agric. Food Chem. 1992, 40, 941-944.
16. Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
17. Maruyama, N.; Katsube, T.; Wada, Y.; Oh, M. H.; Barba de la Rosa, A. P.; Okuda, E.; Nakagawa, S.; Utsumi, S. The roles of the N-linked glycans and extension regions of soybean β-conglycinin in folding, assembly and structural features. Eur. J. Biochem. 1998, 258, 854-862.
18. Clark, A. H.; Lea-Tuffnell, C. D. Gelation of globular proteins. In Functional Properties of Food Macromolecules; Mitchell, J. R., Ledword, D. A., Eds.; Elsevier Applied Science: London, 1986; pp 203-272.
19. Takaiwa, F.; Katsube, T.; Kitagawa, S.; Higasa, T.; Kito, M.; Utsumi, S. High level accumulation of soybean glycinin in vacuole-derived protein bodies in the endosperm tissue of transgenic tobacco seed. Plant Sci. 1995, 111, 39-49.
20. Katsube, T.; Kurisaka, N.; Ogawa, M.; Maruyama, N.; Ohtsuka, R.; Utsumi, S.; Takaiwa, F. Accumulation of soybean glycinin and its assembly with the glutelins in rice. Plant Physiol. 1999, 120, 1063-1073.
21. Choi, S. K.; Adachi, M.; Yoshikawa, M.; Maruyama, N.; Utsumi, S. Soybean glycinin A1aB1b subunit has a molecular chaperone-like function to assist the folding of the other subunit having low folding ability. Biosci., Biotechnol., Biochem. 2004, 68, 1991-1994.
22. Utsumi, S.; Nakamura, T.; Harada, H.; Mori, T. Occurrence of dissociable and undissociabel soybean glycinin. Agric. Biol. Chem. 1987, 51, 2139-2144.
23. Tezuka, M.; Yagasaki, K.; Ono, T. Changes in charactors of soybean glycinin groups I, IIa, and IIb caused by heating. J. Agric. Food Chem. 2004, 52, 1693-1699.
24. Nakai, S. Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. J. Agric. Food Chem. 1983, 31, 676-683.
25. Nakai, S.; Li-Chan, E. Hydrophobicity-functionality relationship of food proteins. Hydrophobic Interactions in Food Systems; CRC Press: Boca Raton, FL, 1988; pp 23-41.
26. Kato, A.; Nakai, S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta 1980, 624, 13-20.
27. Hayakawa, S.; Nakai, S. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J. Food Sci. 1985, 50, 486-491.
28. Kinsella, J. E. Functional properties of soy proteins. J. Am. Oil Chem. Soc. 1979, 56, 242-258.
29. Mori, T.; Maruyama, N.; Nishizawa, K.; Higasa, T.; Yagasaki, K.; Ishimoto, M.; Utsumi, S. The composition of newly synthesized proteins in the endoplamic reticulum determines the transport pathways of soybean seed storage proteins. Plant J. 2004, 40, 238-249.
30. Maruyama, N.; Adachi, M.; Takahashi, K.; Yagasaki, K.; Kohno, M.; Takenaka, Y.; Okuda, E.; Nakagawa, S.; Mikami, B.; Utsumi, S. Crystal structures of recombinant and native soybean β-conglycinin β homotrimers. Eur. J. Biochem. 2001, 268, 3595-3604.
31. Maruyama, Y.; Maruyama, N.; Mikami, B.; Utsumi, S. Structure of the core region of the soybean β-conglycinin α′ subunit. Acta Crystallogr. 2004, D60, 289-297.
32. Adachi, M.; Takenaka, Y.; Gidamis, A. B.; Mikami, B.; Utsumi, S. Crystal structure of soybean proglycinin A1aB1b homotrimer. J. Mol. Biol. 2001, 305, 291-305.
33. Adachi, M.; Kanamori, J.; Masuda, T.; Yagasaki, K.; Kitamura, K.; Mikami, B.; Utsumi, S. Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 7395-7400.
34. Damodaran, S. Protein-stabilized forms and emulsions. In Food Proteins and Their Applications; Damodaran, S., Paraf, A., Eds.; Marcel Dekker: New York, 1997; pp 57-110.
35. Kato, A.; Yutani, K. Correlation of surface properties with conformational stabilities of wild-type and six mutant tryptophan syntase α-subunits substituted at the same position. Protein Eng. 1988, 2, 153-156.
36. Argos, P.; Narayana, S. V. L.; Nielsen, N. C. Structural similarity between legumin and vicilin storage proteins from legumes. EMBO J. 1985, 4, 1111-1117.