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Volumn 56, Issue 23, 2008, Pages 11192-11197

Effect of sodium bisulfite on properties of soybean glycinin

Author keywords

Adhesive strength; Hydrophobic interaction; Morphology; Physicochemical property; Protein modification; Sodium bisulfite; Soy glycinin protein

Indexed keywords

BISULFITE; GLOBULIN; GLYCININ; SOYBEAN PROTEIN; SULFITE;

EID: 58949095802     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf801137y     Document Type: Article
Times cited : (36)

References (30)
  • 1
    • 0033895991 scopus 로고    scopus 로고
    • Adhesive properties of soy proteins modified by urea and guandidine hydrochloride
    • Huang, W.; Sun, X. Adhesive properties of soy proteins modified by urea and guandidine hydrochloride. J. Am. Oil Chem. Soc. 2000, 77, 101-104.
    • (2000) J. Am. Oil Chem. Soc , vol.77 , pp. 101-104
    • Huang, W.1    Sun, X.2
  • 2
    • 0034224093 scopus 로고    scopus 로고
    • Adhesive properties of soy proteins modified by sodium dodecyl sulfate and sodium dodecylbenzene sulfonate
    • Huang, W.; Sun, X. Adhesive properties of soy proteins modified by sodium dodecyl sulfate and sodium dodecylbenzene sulfonate. J. Am. Oil Chem. Soc. 2000, 77, 705-708.
    • (2000) J. Am. Oil Chem. Soc , vol.77 , pp. 705-708
    • Huang, W.1    Sun, X.2
  • 3
    • 51249170137 scopus 로고
    • Alkali-modified soy protein with improved adhesive and hydrophobic properties
    • Hettiarachchy, N. S.; Kalapathy, U.; Myers, D. J. Alkali-modified soy protein with improved adhesive and hydrophobic properties. J. Am. Oil Chem. Soc. 1995, 72, 1461-1464.
    • (1995) J. Am. Oil Chem. Soc , vol.72 , pp. 1461-1464
    • Hettiarachchy, N.S.1    Kalapathy, U.2    Myers, D.J.3
  • 4
    • 1542543436 scopus 로고    scopus 로고
    • Enzymatically-modified soy protein part 2: Adhesion behaviour
    • Kumar, R.; Choudhary, V.; Mishra, S.; Varma, I. K. Enzymatically-modified soy protein part 2: Adhesion behaviour. J. Adhes. Sci. Technol. 2004, 18, 261-273.
    • (2004) J. Adhes. Sci. Technol , vol.18 , pp. 261-273
    • Kumar, R.1    Choudhary, V.2    Mishra, S.3    Varma, I.K.4
  • 5
    • 33748914644 scopus 로고    scopus 로고
    • Performance of soy protein adhesive enhanced by esterification
    • Wang, Y.; Sun, X. S.; Wang, D. Performance of soy protein adhesive enhanced by esterification. Trans. ASAE 2006, 49, 713-719.
    • (2006) Trans. ASAE , vol.49 , pp. 713-719
    • Wang, Y.1    Sun, X.S.2    Wang, D.3
  • 6
    • 0001148056 scopus 로고
    • The physicochemical and functional properties of soybean 11s globulin - A review
    • Peng, I. C.; Quass, D. W.; Dayton, W. R.; Allen, C. E. The physicochemical and functional properties of soybean 11s globulin - A review. Cereal Chem. 1984, 61, 480-490.
    • (1984) Cereal Chem , vol.61 , pp. 480-490
    • Peng, I.C.1    Quass, D.W.2    Dayton, W.R.3    Allen, C.E.4
  • 7
    • 0000115549 scopus 로고
    • Effect of Oxidative sulfitolysis of disulfide bonds of glycinin on solubility, surface hydrophobicity, and in vitro digestibility
    • Kellar, N. K. D.; Barbeau, W. E.; Kinsella, J. E. Effect of Oxidative sulfitolysis of disulfide bonds of glycinin on solubility, surface hydrophobicity, and in vitro digestibility. J. Agric. Food Chem. 1986, 34, 251-256.
    • (1986) J. Agric. Food Chem , vol.34 , pp. 251-256
    • Kellar, N.K.D.1    Barbeau, W.E.2    Kinsella, J.E.3
  • 8
    • 85004878741 scopus 로고
    • Effect of disulfide bond cleavage on the structure and conformation of glycinin
    • Kellar, N. K. D.; Barbeau, W. E.; Kinsella, J. E. Effect of disulfide bond cleavage on the structure and conformation of glycinin. Int. J. Pept. Protein Res. 1986, 27, 421-432.
    • (1986) Int. J. Pept. Protein Res , vol.27 , pp. 421-432
    • Kellar, N.K.D.1    Barbeau, W.E.2    Kinsella, J.E.3
  • 9
    • 84985287289 scopus 로고
    • Surface active properties of food proteins: Effects of reduction of disulfide bonds on film properties and foam stability of glycinin
    • Kim, S. H.; Kinsella, J. E. Surface active properties of food proteins: effects of reduction of disulfide bonds on film properties and foam stability of glycinin. J. Food Sci. 1987, 52, 128-131.
    • (1987) J. Food Sci , vol.52 , pp. 128-131
    • Kim, S.H.1    Kinsella, J.E.2
  • 10
    • 58949091841 scopus 로고    scopus 로고
    • Latex based adhesives derived from soybeans. U.S. Patent, PCT filed
    • PCT pub. no. 35091, pending
    • Sun, X.; Zhu, L.; Wang, D. Latex based adhesives derived from soybeans. U.S. Patent, PCT filed 2006, PCT pub. no. 35091, pending.
    • (2006)
    • Sun, X.1    Zhu, L.2    Wang, D.3
  • 11
    • 33750493256 scopus 로고    scopus 로고
    • Soybean glycinin subunits: Characterization of physicochemical and adhesion properties
    • Mo, X.; Zhong, Z.; Wang, D.; Sun, X. S. Soybean glycinin subunits: Characterization of physicochemical and adhesion properties. J. Agric. Food Chem. 2006, 54, 7589-7593.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 7589-7593
    • Mo, X.1    Zhong, Z.2    Wang, D.3    Sun, X.S.4
  • 12
    • 0017019007 scopus 로고
    • Major proteins of soybean seeds. A straightforward fractionation and their characterization
    • Thanh, V. H.; Shibsaki, K. Major proteins of soybean seeds. A straightforward fractionation and their characterization. J. Agric. Food Chem. 1976, 24, 1117-1121.
    • (1976) J. Agric. Food Chem , vol.24 , pp. 1117-1121
    • Thanh, V.H.1    Shibsaki, K.2
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 13044296146 scopus 로고
    • Thermal dissociation and association behavior of soy proteins
    • German, B.; Damodaran, S.; Kinsella, J. E. Thermal dissociation and association behavior of soy proteins. J. Agric. Food Chem. 1982, 30, 807-811.
    • (1982) J. Agric. Food Chem , vol.30 , pp. 807-811
    • German, B.1    Damodaran, S.2    Kinsella, J.E.3
  • 15
    • 0001750488 scopus 로고
    • Determination of protein hydrophobicity using a sodium dodecyl sulfate binding method
    • Kato, A.; Matsuda, T.; Matsudomi, N.; Kobayashi, K. Determination of protein hydrophobicity using a sodium dodecyl sulfate binding method. J. Agric. Food Chem. 1984, 32, 284-288.
    • (1984) J. Agric. Food Chem , vol.32 , pp. 284-288
    • Kato, A.1    Matsuda, T.2    Matsudomi, N.3    Kobayashi, K.4
  • 16
    • 58949095297 scopus 로고    scopus 로고
    • Annual Book of ASTM Standards; ASTM International: West Conshohocken, PA, 2002; 15.06, pp 158-160, D2339-98.
    • Annual Book of ASTM Standards; ASTM International: West Conshohocken, PA, 2002; Vol. 15.06, pp 158-160, D2339-98.
  • 17
    • 58949096198 scopus 로고    scopus 로고
    • Annual Book of ASTM Standards; ASTM International: West Conshohocken, PA, 2002; 15.06, pp 70-73, D1183-96.
    • Annual Book of ASTM Standards; ASTM International: West Conshohocken, PA, 2002; Vol. 15.06, pp 70-73, D1183-96.
  • 18
    • 58949088921 scopus 로고    scopus 로고
    • Annual Book of ASTM Standards; ASTM International: West Conshohocken, PA, 2002; 15.06, pp 67-69, D1151-00.
    • Annual Book of ASTM Standards; ASTM International: West Conshohocken, PA, 2002; Vol. 15.06, pp 67-69, D1151-00.
  • 19
    • 0019888351 scopus 로고
    • Identification of the acidic and basic subunit complexes of glycinin
    • Staswick, P. E.; Hermodson, M. A.; Nielsen, N. C. Identification of the acidic and basic subunit complexes of glycinin. J. Biol. Chem. 1981, 256, 8752-8755.
    • (1981) J. Biol. Chem , vol.256 , pp. 8752-8755
    • Staswick, P.E.1    Hermodson, M.A.2    Nielsen, N.C.3
  • 20
    • 0001707594 scopus 로고
    • Sulfhydryl content of glycinin: Effect of reducing agent
    • Wolf, W. J. Sulfhydryl content of glycinin: Effect of reducing agent. J. Agric. Food Chem. 1993, 41, 168-176.
    • (1993) J. Agric. Food Chem , vol.41 , pp. 168-176
    • Wolf, W.J.1
  • 21
    • 58949087075 scopus 로고    scopus 로고
    • Method for isolation and modification of proteins
    • U.S. Patent, US 6797810 B1
    • Savolainen, J. Method for isolation and modification of proteins. U.S. Patent, US 6797810 B1, 2004.
    • (2004)
    • Savolainen, J.1
  • 22
    • 0001561686 scopus 로고
    • Gelation phenomena of soybean globulins I: Protein-protein interactions
    • Catsimpoolas, N.; Meyer, E. W. Gelation phenomena of soybean globulins I: Protein-protein interactions. Cereal Chem. 1970, 47, 559-569.
    • (1970) Cereal Chem , vol.47 , pp. 559-569
    • Catsimpoolas, N.1    Meyer, E.W.2
  • 23
    • 48849114029 scopus 로고    scopus 로고
    • Morphology and phase separation of hydrophobic clusters of soy globular protein polymers
    • Sun, X. S.; Wang, D.; Zhang, L.; Mo, X.; Zhu, L.; Boyle, D. Morphology and phase separation of hydrophobic clusters of soy globular protein polymers. Macromol. Biosci. 2008, 8, 295-303.
    • (2008) Macromol. Biosci , vol.8 , pp. 295-303
    • Sun, X.S.1    Wang, D.2    Zhang, L.3    Mo, X.4    Zhu, L.5    Boyle, D.6
  • 24
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: Casting light on the black boxes, the structure in dairy products
    • Horne, D. S. Casein interactions: Casting light on the black boxes, the structure in dairy products. Int. Dairy J. 1998, 8, 171-177.
    • (1998) Int. Dairy J , vol.8 , pp. 171-177
    • Horne, D.S.1
  • 25
    • 0043152270 scopus 로고
    • Purification of the 11s component of soybean protein
    • Eldridge, A. C.; Wolf, W. J. Purification of the 11s component of soybean protein. Cereal Chem. 1967, 44, 645-652.
    • (1967) Cereal Chem , vol.44 , pp. 645-652
    • Eldridge, A.C.1    Wolf, W.J.2
  • 26
    • 85007744884 scopus 로고
    • Occurrence of dissociable and undissociable soybean glycinin
    • Utsumi, S.; Nakamura, T.; Harada, K.; Mori, T. Occurrence of dissociable and undissociable soybean glycinin. Agric. Biol. Chem. 1987, 51, 2139-2144.
    • (1987) Agric. Biol. Chem , vol.51 , pp. 2139-2144
    • Utsumi, S.1    Nakamura, T.2    Harada, K.3    Mori, T.4
  • 27
    • 84907421471 scopus 로고
    • Partial reduction of soy protein isolate disulfide bonds
    • Petruccelli, S.; Anon, M. C. Partial reduction of soy protein isolate disulfide bonds. J. Agric. Food Chem. 1995, 43, 2001-2006.
    • (1995) J. Agric. Food Chem , vol.43 , pp. 2001-2006
    • Petruccelli, S.1    Anon, M.C.2
  • 28
    • 0001230130 scopus 로고
    • Differential scanning calorimetry: A useful tool for studying protein denaturation
    • Relkin, P. Differential scanning calorimetry: A useful tool for studying protein denaturation. Thermochim. Acta 1994, 246, 371-386.
    • (1994) Thermochim. Acta , vol.246 , pp. 371-386
    • Relkin, P.1
  • 29
    • 2642515521 scopus 로고    scopus 로고
    • Thermal properties and adhesion strength of modified soybean storage proteins
    • Mo, X.; Sun, X.; Wang, D. Thermal properties and adhesion strength of modified soybean storage proteins. J. Am. Oil Chem. Soc. 2004, 81, 395-400.
    • (2004) J. Am. Oil Chem. Soc , vol.81 , pp. 395-400
    • Mo, X.1    Sun, X.2    Wang, D.3
  • 30
    • 0030214826 scopus 로고    scopus 로고
    • Alkali-modified soy protein: Effect of salts and disulfide bond cleavage on adhesion and viscosity
    • Kalapathy, U.; Hettiarachchy, N. S.; Myers, D. J.; Rhee, K. C. Alkali-modified soy protein: Effect of salts and disulfide bond cleavage on adhesion and viscosity. J. Am. Oil Chem. Soc. 1996, 73, 1063-1066.
    • (1996) J. Am. Oil Chem. Soc , vol.73 , pp. 1063-1066
    • Kalapathy, U.1    Hettiarachchy, N.S.2    Myers, D.J.3    Rhee, K.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.