메뉴 건너뛰기




Volumn 52, Issue 26, 2004, Pages 7931-7937

Structural characteristics of purified β-conglycinin from soybeans stored under four conditions

Author keywords

7S protein; Soybeans; Storage; Structure; conglycinin

Indexed keywords

AMINO ACID; BETA CONGLYCININ; DISULFIDE; GLYCININ; SUGAR; THIOL DERIVATIVE; UNCLASSIFIED DRUG; VITRONECTIN;

EID: 11144238233     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf049430p     Document Type: Article
Times cited : (60)

References (44)
  • 1
    • 0000447918 scopus 로고
    • Scanning electron microscopy of soybean protein bodies
    • Wolf, W. T. Scanning electron microscopy of soybean protein bodies. J. Am. Oil Chem. Soc. 1970, 47, 107-108.
    • (1970) J. Am. Oil Chem. Soc. , vol.47 , pp. 107-108
    • Wolf, W.T.1
  • 2
    • 0017598953 scopus 로고
    • β-conglycinin from soybean proteins: Isolation and immunological and physicochemical properties of the monomeric forms
    • Thanh, V. H.; Shibasaki, K. β-Conglycinin from soybean proteins: isolation and immunological and physicochemical properties of the monomeric forms. Biochim. Biophys. Acta 1977, 490, 370-384.
    • (1977) Biochim. Biophys. Acta , vol.490 , pp. 370-384
    • Thanh, V.H.1    Shibasaki, K.2
  • 3
    • 0030151307 scopus 로고    scopus 로고
    • Purification, characterization, and crystallization of single molecular species of β-conglycinin from soybean seeds
    • Morita, S.; Fukase, M.; Yamaguchi, M.; Fukuda, Y.; Morita, Y. Purification, characterization, and crystallization of single molecular species of β-conglycinin from soybean seeds. Biosci., Biotechnol., Biochem. 1996, 60, 866-873.
    • (1996) Biosci., Biotechnol., Biochem. , vol.60 , pp. 866-873
    • Morita, S.1    Fukase, M.2    Yamaguchi, M.3    Fukuda, Y.4    Morita, Y.5
  • 4
    • 0001390643 scopus 로고
    • Major proteins of soybean seeds: Reversible and irreversible dissociation of β-conglycinin
    • Thanh, V. H.; Shibasaki, K. Major proteins of soybean seeds: reversible and irreversible dissociation of β-conglycinin. J. Agric. Food Chem. 1979, 27, 805-811.
    • (1979) J. Agric. Food Chem. , vol.27 , pp. 805-811
    • Thanh, V.H.1    Shibasaki, K.2
  • 5
    • 0000308581 scopus 로고
    • Effects of heat and ionic strength upon dissociation-association of soybean protein fractions
    • Iwabuchi, S.; Yamanchi, F. Effects of heat and ionic strength upon dissociation-association of soybean protein fractions. J. Food Sci. 1984, 49, 1289-1294.
    • (1984) J. Food Sci. , vol.49 , pp. 1289-1294
    • Iwabuchi, S.1    Yamanchi, F.2
  • 6
    • 0001355455 scopus 로고
    • Effect of heating and cooling on the gelation kinetics of 7S globulin from soybeans
    • Nagano, T.; Mori, H.; Nishinari, K. Effect of heating and cooling on the gelation kinetics of 7S globulin from soybeans. J. Agric. Food Chem. 1994, 42, 1415-1419.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1415-1419
    • Nagano, T.1    Mori, H.2    Nishinari, K.3
  • 7
    • 84981466858 scopus 로고
    • Differences in functional properties of 7S and 11S soybean proteins
    • Saio, K.; Watanabe, T. Differences in functional properties of 7S and 11S soybean proteins. J. Texture Stud. 1978, 9, 135-157.
    • (1978) J. Texture Stud. , vol.9 , pp. 135-157
    • Saio, K.1    Watanabe, T.2
  • 8
    • 85052678887 scopus 로고    scopus 로고
    • Structure-function relationships of soy proteins
    • Damodaran, S., Paraf, A., Eds.; Dekker: New York, 1997
    • Utsumi, S.; Matsumura, Y.; Mori, T. 1997. Structure-function relationships of soy proteins. In Food Proteins and Their Applications; Damodaran, S., Paraf, A., Eds.; Dekker: New York, 1997; pp 257-291.
    • (1997) Food Proteins and Their Applications , pp. 257-291
    • Utsumi, S.1    Matsumura, Y.2    Mori, T.3
  • 9
    • 0007596825 scopus 로고
    • On the role of disulfide bonds in polymerization of soybean 7S globulin during storage
    • Hoshi, Y.; Yamauchi, F.; Shibasaki, K. On the role of disulfide bonds in polymerization of soybean 7S globulin during storage. Agric. Biol. Chem. 1982, 46, 2803-2807.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 2803-2807
    • Hoshi, Y.1    Yamauchi, F.2    Shibasaki, K.3
  • 10
    • 0040644356 scopus 로고
    • Protein denaturation during model storage studies of soybeans and meals
    • Saio, K.; Kobayakawa, K.; Kito, M. Protein denaturation during model storage studies of soybeans and meals. Cereal Chem. 1982, 59, 408-412.
    • (1982) Cereal Chem. , vol.59 , pp. 408-412
    • Saio, K.1    Kobayakawa, K.2    Kito, M.3
  • 12
    • 2942593798 scopus 로고    scopus 로고
    • Structural characteristics of purified glycinin from soybeans stored under various conditions
    • Hou, H. J.; Chang, K. C. Structural characteristics of purified glycinin from soybeans stored under various conditions. J. Agric. Food Chem. 2004, 52, 3792-3800.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 3792-3800
    • Hou, H.J.1    Chang, K.C.2
  • 13
    • 0036689284 scopus 로고    scopus 로고
    • Interconversions of isoflavones in soybeans as affected by storage
    • Hou, H. J.; Chang, K. C. Interconversions of isoflavones in soybeans as affected by storage. J. Food Sci. 2002, 67, 2083-2089.
    • (2002) J. Food Sci. , vol.67 , pp. 2083-2089
    • Hou, H.J.1    Chang, K.C.2
  • 14
    • 0001124642 scopus 로고
    • Saturated salt solution for static control of relative humidity between 5 °C and 40 °C
    • Rockland, L. B. Saturated salt solution for static control of relative humidity between 5 °C and 40 °C. Anal. Chem. 1960, 32, 1375-1376.
    • (1960) Anal. Chem. , vol.32 , pp. 1375-1376
    • Rockland, L.B.1
  • 16
    • 0001544334 scopus 로고    scopus 로고
    • Partial purification and characterization of the 15S globulin of soybeans, a dimer of glycinin
    • Wolf, W. J.; Nelsen, T. C. Partial purification and characterization of the 15S globulin of soybeans, a dimer of glycinin. J. Agric. Food Chem. 1996, 44, 785-791.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 785-791
    • Wolf, W.J.1    Nelsen, T.C.2
  • 17
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall, A. G.; Bardawill, J.; David, M. M. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 1949, 177, 751-766.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, J.2    David, M.M.3
  • 19
    • 0006544980 scopus 로고
    • Association of Official Analytical Chemists: Washington, DC
    • AOAC. Official Methods of Analysis, 16th ed.; Association of Official Analytical Chemists: Washington, DC, 1995.
    • (1995) Official Methods of Analysis, 16th Ed.
  • 20
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois, M.; Gilles, K. A.; Hamilton, J. K.; Rebers, P. A.; Smith, F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 1959, 28, 350-356.
    • (1959) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 21
    • 84985225780 scopus 로고
    • Analysis of amino acids in soy isolate and navy beans hydrolyzates using precolumn derivatization with phenylisothiocyanate and reverse-phase high performance liquid chromatography
    • Chang, K. C.; Skauge, L. H.; Satterlee, L. D. Analysis of amino acids in soy isolate and navy beans hydrolyzates using precolumn derivatization with phenylisothiocyanate and reverse-phase high performance liquid chromatography. J. Food Sci. 1989, 54, 756-757.
    • (1989) J. Food Sci. , vol.54 , pp. 756-757
    • Chang, K.C.1    Skauge, L.H.2    Satterlee, L.D.3
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analy. Biochem. 1976, 72, 248-254.
    • (1976) Analy. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama, N.; Woody, R. W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 1993, 209, 32-44.
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 25
    • 0037818006 scopus 로고    scopus 로고
    • Yield and quality of soft tofu as affected by soybean physical damage and storage
    • Hou, H. J.; Chang, K. C. Yield and quality of soft tofu as affected by soybean physical damage and storage. J. Agric. Food Chem. 1998, 46, 4798-4805.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 4798-4805
    • Hou, H.J.1    Chang, K.C.2
  • 26
    • 0038528588 scopus 로고    scopus 로고
    • Yield and textural properties of tofu as affected by the changes of phytate content during soybean storage
    • Hou, H. J.; Chang, K. C. Yield and textural properties of tofu as affected by the changes of phytate content during soybean storage. J. Food Sci. 2003, 68, 1185-1191.
    • (2003) J. Food Sci. , vol.68 , pp. 1185-1191
    • Hou, H.J.1    Chang, K.C.2
  • 27
    • 0034775183 scopus 로고    scopus 로고
    • Characterization of β-conglycinin and glycinin soy protein fractions from four selected soybean genotypes
    • Riblett, A. L.; Herald, T. J.; Schmidt, K. A.; Tilley, K. A. Characterization of β-conglycinin and glycinin soy protein fractions from four selected soybean genotypes. J. Agric. Food Chem. 2001, 49, 4983-4989.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4983-4989
    • Riblett, A.L.1    Herald, T.J.2    Schmidt, K.A.3    Tilley, K.A.4
  • 29
    • 0001544334 scopus 로고    scopus 로고
    • Partial purification and characterization of the 15S globulin of soybeans, a dimer of glycinin
    • Wolf, W. J.; Nelsen, T. C. Partial purification and characterization of the 15S globulin of soybeans, a dimer of glycinin. J. Agric. Food Chem. 1996, 44, 785-791.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 785-791
    • Wolf, W.J.1    Nelsen, T.C.2
  • 30
    • 0035994868 scopus 로고    scopus 로고
    • Excipient crystallinity and its protein-structure stabilizing effect during freeze-drying
    • Izutsu, K.; Kojima, S. Excipient crystallinity and its protein-structure stabilizing effect during freeze-drying. J. Pharm. Pharmacol. 2002, 54, 1033-1039.
    • (2002) J. Pharm. Pharmacol. , vol.54 , pp. 1033-1039
    • Izutsu, K.1    Kojima, S.2
  • 31
    • 11144245163 scopus 로고
    • Chromatographic and sedimentation behavior of a purified 7S protein in soybean globulins
    • Koshiyama, I. Chromatographic and sedimentation behavior of a purified 7S protein in soybean globulins. Cereal Chem. 1968, 45, 405-412.
    • (1968) Cereal Chem. , vol.45 , pp. 405-412
    • Koshiyama, I.1
  • 32
    • 33947094131 scopus 로고
    • Major proteins of soybean seeds: Subunit structure of β-conglycinin
    • Thanh, V. H.; Shibasaki, K. Major proteins of soybean seeds: subunit structure of β-conglycinin. J. Agric. Food Chem. 1978, 25, 692-695.
    • (1978) J. Agric. Food Chem. , vol.25 , pp. 692-695
    • Thanh, V.H.1    Shibasaki, K.2
  • 33
    • 0000020517 scopus 로고
    • Internal structure of 7S and 11S globulin molecules in soybean proteins
    • Fukushima, D. Internal structure of 7S and 11S globulin molecules in soybean proteins. Cereal Chem. 1968, 45, 203-224.
    • (1968) Cereal Chem. , vol.45 , pp. 203-224
    • Fukushima, D.1
  • 34
    • 0007661830 scopus 로고
    • Chemical and physical properties of a 7S protein in soybean globulins
    • Koshiyama, I. Chemical and physical properties of a 7S protein in soybean globulins. Cereal Chem. 1968, 45, 394-405.
    • (1968) Cereal Chem. , vol.45 , pp. 394-405
    • Koshiyama, I.1
  • 35
    • 0001661381 scopus 로고
    • Structures of plant storage proteins and their functions
    • Fukushima, D. Structures of plant storage proteins and their functions. Food Rev. Int. 1991, 7, 353-382.
    • (1991) Food Rev. Int. , vol.7 , pp. 353-382
    • Fukushima, D.1
  • 37
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C., Jr. Protein secondary structure and circular dichroism: a practical guide. Proteins: Struc., Funct., Genet. 1990, 7, 205-214.
    • (1990) Proteins: Struc., Funct., Genet. , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 38
    • 0001439385 scopus 로고
    • Comparison of conformations of 7S and 11S soybean globulins by optical rotatory dispersion and circular dichroism studies
    • Koshiyama, I.; Fukushima, D. Comparison of conformations of 7S and 11S soybean globulins by optical rotatory dispersion and circular dichroism studies. Cereal Chem. 1973, 50, 114-121.
    • (1973) Cereal Chem. , vol.50 , pp. 114-121
    • Koshiyama, I.1    Fukushima, D.2
  • 39
    • 0011299125 scopus 로고
    • Conformational transition of alkali-denatured soybean 7S and 11S globulins by ethanol
    • Ishino, K.; Kudo, S. Conformational transition of alkali-denatured soybean 7S and 11S globulins by ethanol. Agric. Biol. Chem. 1980, 44, 537-543.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 537-543
    • Ishino, K.1    Kudo, S.2
  • 40
    • 1642590674 scopus 로고
    • Structural similarity between legumin and vicilin storage proteins from legumes
    • 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.
    • (1985) EMBO J. , vol.4 , pp. 1111-1117
    • Argos, P.1    Narayana, S.V.L.2    Nielsen, N.C.3
  • 41
    • 33751499115 scopus 로고
    • Thermal gelation of globular proteins: Influence of protein conformation on gel strength
    • Wang, C. H.; Damodaran, S. Thermal gelation of globular proteins: influence of protein conformation on gel strength. J. Agric. Food Chem. 1991, 39, 433-438.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 433-438
    • Wang, C.H.1    Damodaran, S.2
  • 42
    • 2942578584 scopus 로고    scopus 로고
    • Recent progress on biotechnology of soybean proteins and soybean protein food products
    • Kourin Publishing: Tsukuba, Tokyo, Japan
    • Fukushima, D. Recent progress on biotechnology of soybean proteins and soybean protein food products. In Proceedings of the Third International Soybean Processing and Utilization Conference; Kourin Publishing: Tsukuba, Tokyo, Japan, 2000; pp 11-16.
    • (2000) Proceedings of the Third International Soybean Processing and Utilization Conference , pp. 11-16
    • Fukushima, D.1
  • 43
    • 84954875344 scopus 로고
    • Effects of partial denaturation on surface properties of ovalbumin and lysozyme
    • Kato, A.; Tsutsui, N.; Matsudomi, N.; Kobayashi, K.; Nakai, S. Effects of partial denaturation on surface properties of ovalbumin and lysozyme. Agric. Biol Chem. 1981, 45, 2788-2760.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 2788-2760
    • Kato, A.1    Tsutsui, N.2    Matsudomi, N.3    Kobayashi, K.4    Nakai, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.