메뉴 건너뛰기




Volumn 23, Issue 3, 2009, Pages 996-1006

Macromolecular complexes of the main storage protein of Vicia faba seeds with sulfated polysaccharide

Author keywords

Circular dichroism; Conformation; Interaction; Kappa carrageenan; Legumin; Methylene blue; Protein aggregation; SEC MALS; Thermal stability

Indexed keywords

AROMATIC COMPOUNDS; DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; IONIC STRENGTH; LIGHT SCATTERING; MOLECULES; PROTEINS; SIZE EXCLUSION CHROMATOGRAPHY; SPECTROPHOTOMETRY; STABILITY;

EID: 54049101464     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2008.07.012     Document Type: Article
Times cited : (9)

References (49)
  • 1
    • 0038471187 scopus 로고    scopus 로고
    • Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer
    • Adachi M., Kanamori J., Masuda T., Yagasaki K., Kitamura K., Mikami B., et al. Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer. PNAS 100 12 (2003) 7395-7400
    • (2003) PNAS , vol.100 , Issue.12 , pp. 7395-7400
    • Adachi, M.1    Kanamori, J.2    Masuda, T.3    Yagasaki, K.4    Kitamura, K.5    Mikami, B.6
  • 2
    • 33947624264 scopus 로고    scopus 로고
    • Aqueous phase-separated biopolymer mixture compatibilized by physical interactions of the constituents
    • Antonov Y.A., and Friedrich C. Aqueous phase-separated biopolymer mixture compatibilized by physical interactions of the constituents. Polymer Bulletin 58 5-6 (2007) 969-978
    • (2007) Polymer Bulletin , vol.58 , Issue.5-6 , pp. 969-978
    • Antonov, Y.A.1    Friedrich, C.2
  • 3
    • 0040320327 scopus 로고    scopus 로고
    • Phase separation in aqueous gelatin-K-carrageenan systems
    • Antonov Y.A., and Gonçalves M.P. Phase separation in aqueous gelatin-K-carrageenan systems. Food Hydrocolloids 13 (1999) 517-524
    • (1999) Food Hydrocolloids , vol.13 , pp. 517-524
    • Antonov, Y.A.1    Gonçalves, M.P.2
  • 4
    • 0032712182 scopus 로고    scopus 로고
    • On the one-phase state of aqueous protein-uncharged polymer systems: casein-guar gum system
    • Antonov Y.A., Lefebvre J., and Doublier J.-L. On the one-phase state of aqueous protein-uncharged polymer systems: casein-guar gum system. Journal of Applied Polymer Science 71 (1999) 471-482
    • (1999) Journal of Applied Polymer Science , vol.71 , pp. 471-482
    • Antonov, Y.A.1    Lefebvre, J.2    Doublier, J.-L.3
  • 5
    • 33644640543 scopus 로고    scopus 로고
    • Interactions and compatibility of 11 S globulin from Vicia faba seeds and sodium salt of carboxymethylcellulose in an aqueous medium
    • Antonov Yu.A., Dmitrochenko A.P., and Leontiev A.L. Interactions and compatibility of 11 S globulin from Vicia faba seeds and sodium salt of carboxymethylcellulose in an aqueous medium. International Journal of Biological Macromolecules 38 1 (2006) 18-24
    • (2006) International Journal of Biological Macromolecules , vol.38 , Issue.1 , pp. 18-24
    • Antonov, Yu.A.1    Dmitrochenko, A.P.2    Leontiev, A.L.3
  • 6
    • 0034641186 scopus 로고    scopus 로고
    • Interactions and compatibility of ribuloso-1,5- bisphosphate carboxylase: oxygenase from alfalfa with pectin in aqueous medium
    • Antonov Yu.A., and Soshinsky A.A. Interactions and compatibility of ribuloso-1,5- bisphosphate carboxylase: oxygenase from alfalfa with pectin in aqueous medium. International Journal of Biological Macromolecules 27 4 (2000) 279-285
    • (2000) International Journal of Biological Macromolecules , vol.27 , Issue.4 , pp. 279-285
    • Antonov, Yu.A.1    Soshinsky, A.A.2
  • 7
    • 0023056522 scopus 로고
    • The legumin gene family: structure of a B type gene of Vicia faba and a possible legumin gene specific regulatory element
    • Baumlein H., Wobus U., Pustell J., and Kafatos F.C. The legumin gene family: structure of a B type gene of Vicia faba and a possible legumin gene specific regulatory element. Nucleic Acid Research 14 (1986) 2707-2720
    • (1986) Nucleic Acid Research , vol.14 , pp. 2707-2720
    • Baumlein, H.1    Wobus, U.2    Pustell, J.3    Kafatos, F.C.4
  • 9
    • 33846814867 scopus 로고    scopus 로고
    • How does dextran sulfate prevent heat induced aggregation of protein? The mechanism and its limitation as aggregation inhibitor
    • Chung K., Kim J., Cho B.K., Ko B.J., Hwang B.Y., and Kim B.G. How does dextran sulfate prevent heat induced aggregation of protein? The mechanism and its limitation as aggregation inhibitor. BBA 1774 (2007) 249-257
    • (2007) BBA , vol.1774 , pp. 249-257
    • Chung, K.1    Kim, J.2    Cho, B.K.3    Ko, B.J.4    Hwang, B.Y.5    Kim, B.G.6
  • 10
    • 0032444513 scopus 로고    scopus 로고
    • Stability and rheological implications of electrostatic milk protein-polysaccharide interactions
    • Dickinson E. Stability and rheological implications of electrostatic milk protein-polysaccharide interactions. Trends in Food Science and Technology 9 (1998) 347-354
    • (1998) Trends in Food Science and Technology , vol.9 , pp. 347-354
    • Dickinson, E.1
  • 11
    • 0028741079 scopus 로고
    • Protein purification by selective phase separation with polyelectrolytes
    • Dubin P.L., Gao J., and Mattison K. Protein purification by selective phase separation with polyelectrolytes. Separation and Purification Methods 23 1 (1994) 1-16
    • (1994) Separation and Purification Methods , vol.23 , Issue.1 , pp. 1-16
    • Dubin, P.L.1    Gao, J.2    Mattison, K.3
  • 12
    • 0006460027 scopus 로고    scopus 로고
    • Limited tryptic hydrolysis of legumin from faba beanVicia faba L Formation of anunequal subunit pattern
    • Dudek S., Horstmann C., and Schwenke K.D. Limited tryptic hydrolysis of legumin from faba beanVicia faba L Formation of anunequal subunit pattern. Nahrung 40 (1996) 171-176
    • (1996) Nahrung , vol.40 , pp. 171-176
    • Dudek, S.1    Horstmann, C.2    Schwenke, K.D.3
  • 13
    • 0026777917 scopus 로고
    • The legumin precursor from white lupin seed. Identity of the subunits, assembly and proteolysis
    • Duranti M., Guerrieri N., Cerletti P., and Vecchio G. The legumin precursor from white lupin seed. Identity of the subunits, assembly and proteolysis. European Journal of Biochemistry 206 (1992) 941-947
    • (1992) European Journal of Biochemistry , vol.206 , pp. 941-947
    • Duranti, M.1    Guerrieri, N.2    Cerletti, P.3    Vecchio, G.4
  • 14
    • 0035136241 scopus 로고    scopus 로고
    • SANS study of surfactant ordering in κ-carrageenan/cetylpyridinium chloride complexes
    • Eremenko G., Theunissen E., Mortensen K., and Reynaers H. SANS study of surfactant ordering in κ-carrageenan/cetylpyridinium chloride complexes. Polymer 42 (2001) 2907-2913
    • (2001) Polymer , vol.42 , pp. 2907-2913
    • Eremenko, G.1    Theunissen, E.2    Mortensen, K.3    Reynaers, H.4
  • 16
    • 0001407328 scopus 로고
    • Selective precipitation of whey proteins with carboxymethylcellulose
    • Hidalgo J., and Hansen P.M.T. Selective precipitation of whey proteins with carboxymethylcellulose. Journal of Dairy Science 54 9 (1971) 1270-1274
    • (1971) Journal of Dairy Science , vol.54 , Issue.9 , pp. 1270-1274
    • Hidalgo, J.1    Hansen, P.M.T.2
  • 17
    • 0035743381 scopus 로고    scopus 로고
    • Measurement and analysis of results obtained on biological substances with differential scanning calorimetry
    • Hinz H.J., and Schwarz F.P. Measurement and analysis of results obtained on biological substances with differential scanning calorimetry. Pure and Applied Chemistry 73 (2001) 745-759
    • (2001) Pure and Applied Chemistry , vol.73 , pp. 745-759
    • Hinz, H.J.1    Schwarz, F.P.2
  • 18
    • 0001151208 scopus 로고
    • Specific subunit pairs of legumin from Vicia faba
    • Horstmann C. Specific subunit pairs of legumin from Vicia faba. Phytochemistry 22 (1983) 1861-1866
    • (1983) Phytochemistry , vol.22 , pp. 1861-1866
    • Horstmann, C.1
  • 19
    • 0037465799 scopus 로고    scopus 로고
    • Characterization of polymer solutions containing a small amount of aggregates by static and dynamic light scattering
    • Kanao M., Matsuda Y., and Sato T. Characterization of polymer solutions containing a small amount of aggregates by static and dynamic light scattering. Macromolecules 36 (2003) 2093-2102
    • (2003) Macromolecules , vol.36 , pp. 2093-2102
    • Kanao, M.1    Matsuda, Y.2    Sato, T.3
  • 20
    • 0041386471 scopus 로고    scopus 로고
    • Influence of chain stiffness on the interaction of oppositely charged micelles and proteins
    • Kayitmazer A.B., Seyrek E., Dubin P.L., and Staggemeier B.A. Influence of chain stiffness on the interaction of oppositely charged micelles and proteins. Journal of Physical Chemistry B 107 (2003) 8158-8165
    • (2003) Journal of Physical Chemistry B , vol.107 , pp. 8158-8165
    • Kayitmazer, A.B.1    Seyrek, E.2    Dubin, P.L.3    Staggemeier, B.A.4
  • 21
    • 0032383760 scopus 로고    scopus 로고
    • Use of polyelectrolytes for isolation of a trypsin inhibitor from industrial waste of alfalfa leaf protein fractionation
    • [Russian, Engl.Transl.]
    • Kiknadze E.V., and Antonov Y.A. Use of polyelectrolytes for isolation of a trypsin inhibitor from industrial waste of alfalfa leaf protein fractionation. [Russian, Engl.Transl.]. Applied Biochemistry and Microbiology 34 5 (1998) 462-465
    • (1998) Applied Biochemistry and Microbiology , vol.34 , Issue.5 , pp. 462-465
    • Kiknadze, E.V.1    Antonov, Y.A.2
  • 22
    • 0010368070 scopus 로고
    • Chemical Thermodynamics Division, NIST, Gaithersburg, USA [DSC Analysis Version]
    • Kirchoff W.H. EXAM (1988), Chemical Thermodynamics Division, NIST, Gaithersburg, USA [DSC Analysis Version]
    • (1988) EXAM
    • Kirchoff, W.H.1
  • 23
    • 0019890801 scopus 로고
    • Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor
    • Kosen P.A., Creighton T.E., and Blout E.R. Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor. Biochemistry 29 (1981) 5744-5754
    • (1981) Biochemistry , vol.29 , pp. 5744-5754
    • Kosen, P.A.1    Creighton, T.E.2    Blout, E.R.3
  • 24
    • 0022342665 scopus 로고
    • Thermal denaturation of the core protein of lac repressor
    • Manly S.P., Matthews K.S., and Sturtevant J.M. Thermal denaturation of the core protein of lac repressor. Biochemistry 24 (1985) 3842-3846
    • (1985) Biochemistry , vol.24 , pp. 3842-3846
    • Manly, S.P.1    Matthews, K.S.2    Sturtevant, J.M.3
  • 25
    • 11144289607 scopus 로고    scopus 로고
    • Unperturbed dimensions of carrageenans in different salt solutions
    • Marcelo G., Saiz E., and Tarazona M.P. Unperturbed dimensions of carrageenans in different salt solutions. Biophysical Chemistry 113 (2005) 201-208
    • (2005) Biophysical Chemistry , vol.113 , pp. 201-208
    • Marcelo, G.1    Saiz, E.2    Tarazona, M.P.3
  • 26
    • 0032492820 scopus 로고    scopus 로고
    • Complex formation between bovine serum albumin and strong polyelectrolytes: effect of polymer charge density
    • Mattison K.W., Dubin P.L., and Brittain I.J. Complex formation between bovine serum albumin and strong polyelectrolytes: effect of polymer charge density. Journal of Physical Chemistry B 102 (1998) 3830-3836
    • (1998) Journal of Physical Chemistry B , vol.102 , pp. 3830-3836
    • Mattison, K.W.1    Dubin, P.L.2    Brittain, I.J.3
  • 27
    • 0036838126 scopus 로고    scopus 로고
    • Gelatin/carrageenan interactions in coil and ordered conformations followed by a methylene blue spectrophotometric method
    • Michon C., Konate K., Cuvelier G., and Launay B. Gelatin/carrageenan interactions in coil and ordered conformations followed by a methylene blue spectrophotometric method. Food Hydrocolloids 16 (2002) 613-618
    • (2002) Food Hydrocolloids , vol.16 , pp. 613-618
    • Michon, C.1    Konate, K.2    Cuvelier, G.3    Launay, B.4
  • 30
    • 0001064980 scopus 로고    scopus 로고
    • Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds
    • Müntz K. Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds. Journal of Experimental Botany 47 (1996) 605-622
    • (1996) Journal of Experimental Botany , vol.47 , pp. 605-622
    • Müntz, K.1
  • 31
    • 0001162505 scopus 로고
    • Relationship between the amino acid sequence and the domain structure of the subunits of the 11S seed globulins
    • Plietz P., Drescher B., and Damaschun G. Relationship between the amino acid sequence and the domain structure of the subunits of the 11S seed globulins. International Journal of Biological Macromolecules 9 (1987) 161-165
    • (1987) International Journal of Biological Macromolecules , vol.9 , pp. 161-165
    • Plietz, P.1    Drescher, B.2    Damaschun, G.3
  • 32
    • 0021774163 scopus 로고
    • Shape, symmetry, hydration and secondary structure of the legumin from Vicia faba in solution
    • Plietz P., Zirwer D., Schlesier B., Gast K., and Damaschun G. Shape, symmetry, hydration and secondary structure of the legumin from Vicia faba in solution. Biochimica et Biophysica Acta 784 (1984) 140-146
    • (1984) Biochimica et Biophysica Acta , vol.784 , pp. 140-146
    • Plietz, P.1    Zirwer, D.2    Schlesier, B.3    Gast, K.4    Damaschun, G.5
  • 34
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the thermal denaturation of thermolysin
    • Sanches-Ruiz J.M., Lopez-Lacomba J.L., Cortijo M., and Mateo P.L. Differential scanning calorimetry of the thermal denaturation of thermolysin. Biochemistry 27 (1988) 1648-1652
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sanches-Ruiz, J.M.1    Lopez-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 35
    • 0002644199 scopus 로고
    • The conformation of hyaluronic acid and chondroitin sulfate C: the metachromatic reaction
    • Schoenberg M.D., and Moore R.D. The conformation of hyaluronic acid and chondroitin sulfate C: the metachromatic reaction. Biochimica et Biophysica Acta 83 (1964) 42-51
    • (1964) Biochimica et Biophysica Acta , vol.83 , pp. 42-51
    • Schoenberg, M.D.1    Moore, R.D.2
  • 36
    • 84984450310 scopus 로고
    • Isolation of faba bean legumin - a comparative study of various methods
    • Schwenke K.D., Dudek S., Seifert A., Mothes R., and Staatz A. Isolation of faba bean legumin - a comparative study of various methods. Nahrung 38 (1994) 559-567
    • (1994) Nahrung , vol.38 , pp. 559-567
    • Schwenke, K.D.1    Dudek, S.2    Seifert, A.3    Mothes, R.4    Staatz, A.5
  • 38
    • 84984434262 scopus 로고
    • Isolation of lactic whey proteins in the form of complexes with apple pectin
    • Serov A.V., AntonovYu A., and Tolstoguzov V.B. Isolation of lactic whey proteins in the form of complexes with apple pectin. Nahrung 29 1 (1985) 19-30
    • (1985) Nahrung , vol.29 , Issue.1 , pp. 19-30
    • Serov, A.V.1    AntonovYu, A.2    Tolstoguzov, V.B.3
  • 39
    • 0025835348 scopus 로고
    • Molecular characterisation of κ- and λ-carrageenan by gel permeation chromatography, light scattering, sedimentation analysis and osmometry
    • Slootmaekers D., Dijk J.A.P.P., Varkevisser F.A., Bloys van Treslong C.J., and Reynaers H. Molecular characterisation of κ- and λ-carrageenan by gel permeation chromatography, light scattering, sedimentation analysis and osmometry. Biophysical Chemistry 41 (1991) 51-59
    • (1991) Biophysical Chemistry , vol.41 , pp. 51-59
    • Slootmaekers, D.1    Dijk, J.A.P.P.2    Varkevisser, F.A.3    Bloys van Treslong, C.J.4    Reynaers, H.5
  • 40
    • 85169514798 scopus 로고    scopus 로고
    • Snoeren, T. H. M. (1976). Kappa-carrageenan. A study on its physico-chemical properties, sol-gel transition and interaction with milk proteins. PhD thesis, University of Wageningen, 102 pp.
    • Snoeren, T. H. M. (1976). Kappa-carrageenan. A study on its physico-chemical properties, sol-gel transition and interaction with milk proteins. PhD thesis, University of Wageningen, 102 pp.
  • 41
    • 0001393646 scopus 로고
    • Electrostatic interaction between kappa-carrageenan and kappa-casein
    • Snoeren T.H.M., Payens T.A.J., Jevnink J., and Both P. Electrostatic interaction between kappa-carrageenan and kappa-casein. Milchwissenschaft 30 (1975) 393-395
    • (1975) Milchwissenschaft , vol.30 , pp. 393-395
    • Snoeren, T.H.M.1    Payens, T.A.J.2    Jevnink, J.3    Both, P.4
  • 42
    • 0015997959 scopus 로고
    • Aromatic contributions to circular dichroism spectra of proteins
    • Strickland E.H. Aromatic contributions to circular dichroism spectra of proteins. Critical Reviews Biochemistry 2 (1974) 113-175
    • (1974) Critical Reviews Biochemistry , vol.2 , pp. 113-175
    • Strickland, E.H.1
  • 43
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant J.M. Biochemical applications of differential scanning calorimetry. Annual Review of Physical Chemistry 38 (1987) 463-488
    • (1987) Annual Review of Physical Chemistry , vol.38 , pp. 463-488
    • Sturtevant, J.M.1
  • 44
    • 0003588637 scopus 로고    scopus 로고
    • Hill S.E., Ledward D.A., and Mitchel J.R. (Eds), Aspen Publishers Inc., Gaithersburg, MD
    • Tolstoguzov V.B. In: Hill S.E., Ledward D.A., and Mitchel J.R. (Eds). Functional properties of food macromolecules (1998), Aspen Publishers Inc., Gaithersburg, MD
    • (1998) Functional properties of food macromolecules
    • Tolstoguzov, V.B.1
  • 45
    • 0018780588 scopus 로고
    • Thermodynamics of the denaturation of lysozyme in alcohol-water mixtures
    • Velicelebi G., and Sturtevant J. Thermodynamics of the denaturation of lysozyme in alcohol-water mixtures. Biochemistry 18 7 (1979) 1180-1186
    • (1979) Biochemistry , vol.18 , Issue.7 , pp. 1180-1186
    • Velicelebi, G.1    Sturtevant, J.2
  • 46
    • 84985715962 scopus 로고
    • Physicochemical investigation of k-carrageenan in the random state
    • Vreeman H.J., Snoeren T.H.M., and Payens T.A.J. Physicochemical investigation of k-carrageenan in the random state. Biopolymers 19 (1980) 1357-1374
    • (1980) Biopolymers , vol.19 , pp. 1357-1374
    • Vreeman, H.J.1    Snoeren, T.H.M.2    Payens, T.A.J.3
  • 48
    • 2942558433 scopus 로고    scopus 로고
    • Effect of sulfated polysaccharides on heat-induced structural changes in ß-lactoglobulin
    • Zhang G., Foegeding E.A., and Hardin C. Effect of sulfated polysaccharides on heat-induced structural changes in ß-lactoglobulin. Journal of Agricultural and Food Chemistry 52 (2004) 3975-3981
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 3975-3981
    • Zhang, G.1    Foegeding, E.A.2    Hardin, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.