메뉴 건너뛰기




Volumn 89, Issue 4, 2005, Pages 497-501

Removal and recovery of antinutritional factors from soybean flour

Author keywords

Antinutritional factors; Immobilized metal affinity chromatography; Soybean agglutinin; Soybean flour; Soybean trypsin inhibitor; Zinc alginate beads

Indexed keywords

ALGINIC ACID; EDETIC ACID; IMIDAZOLE; LECTIN; PROTEINASE INHIBITOR; SOYBEAN AGGLUTININ; TRYPSIN INHIBITOR; ZINC COMPLEX;

EID: 4544252643     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2004.02.055     Document Type: Article
Times cited : (44)

References (21)
  • 1
    • 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. Analytical Biochemistry. 72:1976;248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0038062785 scopus 로고    scopus 로고
    • Preparative purification of soybean agglutinin by affinity chromatography and its immobilization for polysaccharide isolation
    • Franco-Fraguas L., Plá A., Ferreira F., Massaldi H., Suárez N., Batista-Viera F. Preparative purification of soybean agglutinin by affinity chromatography and its immobilization for polysaccharide isolation. Journal of Chromatography B. 90(1-2):2003;365-372
    • (2003) Journal of Chromatography B , vol.90 , Issue.12 , pp. 365-372
    • Franco-Fraguas, L.1    Plá, A.2    Ferreira, F.3    Massaldi, H.4    Suárez, N.5    Batista-Viera, F.6
  • 5
    • 0019888762 scopus 로고
    • The isolation and characterization of a root lectin from soybean (Glycine max (L) Cultivar Chippewa)
    • Gade W., Jack M.A., Dahl J.B., Schmidt E.L., Wold F. The isolation and characterization of a root lectin from soybean (Glycine max (L) Cultivar Chippewa). The Journal of Biological Chemistry. 256(24):1981;12905-12910
    • (1981) The Journal of Biological Chemistry , vol.256 , Issue.24 , pp. 12905-12910
    • Gade, W.1    Jack, M.A.2    Dahl, J.B.3    Schmidt, E.L.4    Wold, F.5
  • 7
    • 0036007991 scopus 로고    scopus 로고
    • Immobilized metal affinity chromatography without chelating ligands: Purification of soybean trypsin inhibitor on zinc alginate beads
    • Gupta M.N., Jain S., Roy I. Immobilized metal affinity chromatography without chelating ligands: Purification of soybean trypsin inhibitor on zinc alginate beads. Biotechnology Progress. 18:2002;78-91
    • (2002) Biotechnology Progress , vol.18 , pp. 78-91
    • Gupta, M.N.1    Jain, S.2    Roy, I.3
  • 9
    • 0028501408 scopus 로고
    • Affinity precipitation of trypsin with soybean trypsin inhibitor linked Eudragit S-100
    • Kumar A., Gupta M.N. Affinity precipitation of trypsin with soybean trypsin inhibitor linked Eudragit S-100. Journal of Biotechnology. 37(2):1994;185-189
    • (1994) Journal of Biotechnology , vol.37 , Issue.2 , pp. 185-189
    • Kumar, A.1    Gupta, M.N.2
  • 13
    • 0036768809 scopus 로고    scopus 로고
    • Thermal inactivation of tepary bean (Phaseolus acutifolius), soybean and lima bean protease inhibitors: Effect of acidic and basic pH
    • Osman M.A., Reid P.M., Weber C.W. Thermal inactivation of tepary bean (Phaseolus acutifolius), soybean and lima bean protease inhibitors: Effect of acidic and basic pH. Food Chemistry. 78:2002;419-423
    • (2002) Food Chemistry , vol.78 , pp. 419-423
    • Osman, M.A.1    Reid, P.M.2    Weber, C.W.3
  • 15
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography: A new approach to protein fractionation
    • Porath J., Carlsson J., Olsson I., Belfrage G. Metal chelate affinity chromatography: A new approach to protein fractionation. Nature. 258:1975;598-599
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 16
    • 0036145798 scopus 로고    scopus 로고
    • Three-phase affinity partitioning of proteins
    • Roy I., Gupta M.N. Three-phase affinity partitioning of proteins. Analytical Biochemistry. 300:2002;11-14
    • (2002) Analytical Biochemistry , vol.300 , pp. 11-14
    • Roy, I.1    Gupta, M.N.2
  • 18
    • 0024479002 scopus 로고
    • Isolation and purification of endo- polygalacturonase by affinity chromatography in fluidized bed reactor
    • Somers W., Van't Riet K., Rozie H., Rombouts F., Visser J. Isolation and purification of endo- polygalacturonase by affinity chromatography in fluidized bed reactor. Chemical Engineering Journal. 40:1989;B7-B19
    • (1989) Chemical Engineering Journal , vol.40
    • Somers, W.1    Van'T Riet, K.2    Rozie, H.3    Rombouts, F.4    Visser, J.5
  • 19
    • 0002334609 scopus 로고    scopus 로고
    • Soy products as fat and protein sources in fish feed for intensive aquaculture
    • J.K. Drackley. Savoy, IL: Federation of Animal Science Society
    • Storebakken T., Refstie S., Ruyter B. Soy products as fat and protein sources in fish feed for intensive aquaculture. Drackley J.K. Soy in Animal Nutrition. 2000;127-170 Federation of Animal Science Society, Savoy, IL
    • (2000) Soy in Animal Nutrition , pp. 127-170
    • Storebakken, T.1    Refstie, S.2    Ruyter, B.3
  • 20
    • 0016564484 scopus 로고
    • The use of glutaraldehyde treated erythocytes for assaying the agglutinating activity of lectins
    • Turner R.H., Liener I.E. The use of glutaraldehyde treated erythocytes for assaying the agglutinating activity of lectins. Analytical Biochemistry. 68:1975;651-653
    • (1975) Analytical Biochemistry , vol.68 , pp. 651-653
    • Turner, R.H.1    Liener, I.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.