메뉴 건너뛰기




Volumn 56, Issue 16, 2008, Pages 7113-7118

Formation of whey protein isolate (WPI)-dextran conjugates in aqueous solutions

Author keywords

Conjugates; Dextran; Functionality; Maillard reaction; Whey protein isolates

Indexed keywords

DEXTRAN; MILK PROTEIN; WATER; WHEY PROTEIN;

EID: 51649086473     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf800909w     Document Type: Article
Times cited : (187)

References (23)
  • 1
    • 0000041385 scopus 로고
    • Emulsifying properties of protein-polysaccharide complexes and hybrids
    • Kato, A.; Sato, T.; Kobayashi, K. Emulsifying properties of protein-polysaccharide complexes and hybrids. Agric. Biol. Chem. 1989, 53, 2147-2152.
    • (1989) Agric. Biol. Chem , vol.53 , pp. 2147-2152
    • Kato, A.1    Sato, T.2    Kobayashi, K.3
  • 2
    • 0011733867 scopus 로고
    • Emulsifying properties of covalent protein-dextran hybrids
    • Dickinson, E.; Semenova, M. G. Emulsifying properties of covalent protein-dextran hybrids. Colloids Surf. 1992, 64, 299-310.
    • (1992) Colloids Surf , vol.64 , pp. 299-310
    • Dickinson, E.1    Semenova, M.G.2
  • 3
    • 0346976253 scopus 로고    scopus 로고
    • Functional improvements in food proteins in multiple aspects by conjugation with saccharides: Case studies of β-lactoglobulin-acidic polysaccharides conjugates
    • Hattori, M. Functional improvements in food proteins in multiple aspects by conjugation with saccharides: case studies of β-lactoglobulin-acidic polysaccharides conjugates. Food Sci. Technol. Res. 2002, 8, 291-299.
    • (2002) Food Sci. Technol. Res , vol.8 , pp. 291-299
    • Hattori, M.1
  • 4
    • 12344318373 scopus 로고    scopus 로고
    • β-Lactoglobulin-dextran conjugates: Effect of polysaccharide size on emulsion stability
    • Dunlap, C. A.; Côté, G. L. β-Lactoglobulin-dextran conjugates: effect of polysaccharide size on emulsion stability. J. Agric. Food Chem. 2005, 53, 419-423.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 419-423
    • Dunlap, C.A.1    Côté, G.L.2
  • 5
    • 0042161834 scopus 로고    scopus 로고
    • Emulsifying properties of whey protein-dextran conjugates at low pH and different salt concentrations
    • Akhtar, M.; Dickinson, E. Emulsifying properties of whey protein-dextran conjugates at low pH and different salt concentrations. Colloids Surf. B 2003, 31, 125-132.
    • (2003) Colloids Surf. B , vol.31 , pp. 125-132
    • Akhtar, M.1    Dickinson, E.2
  • 6
    • 0000668338 scopus 로고
    • Enhanced antioxidative effect of ovalbumin due to covalent binding of polysaccharides
    • Nakamura, S.; Kato, A.; Kobayashi, K. Enhanced antioxidative effect of ovalbumin due to covalent binding of polysaccharides. J. Agric. Food Chem. 1992, 40, 2033-2037.
    • (1992) J. Agric. Food Chem , vol.40 , pp. 2033-2037
    • Nakamura, S.1    Kato, A.2    Kobayashi, K.3
  • 7
    • 0031858644 scopus 로고    scopus 로고
    • Induction of new physicochemical and functional properties by the glycosylation of whey proteins
    • Nacka, F.; Chobert, J.-M.; Burova, T.; Léonil, J.; Haertlé, T. Induction of new physicochemical and functional properties by the glycosylation of whey proteins. J. Protein Chem. 1998, 17, 495-503.
    • (1998) J. Protein Chem , vol.17 , pp. 495-503
    • Nacka, F.1    Chobert, J.-M.2    Burova, T.3    Léonil, J.4    Haertlé, T.5
  • 8
    • 0033484302 scopus 로고    scopus 로고
    • Functional properties of milk proteins glycated in mild conditions
    • Groubet, R.; Chobert, J.-M.; Haertlé, T. Functional properties of milk proteins glycated in mild conditions. Sci. Aliment. 1999, 19, 423-438.
    • (1999) Sci. Aliment , vol.19 , pp. 423-438
    • Groubet, R.1    Chobert, J.-M.2    Haertlé, T.3
  • 9
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular crowding: Qualitative and semiquantitative successes, quantitative challenges
    • Hall, D.; Minton, A. P. Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. Biochim. Biophys. Acta 2003, 1649, 127-139.
    • (2003) Biochim. Biophys. Acta , vol.1649 , pp. 127-139
    • Hall, D.1    Minton, A.P.2
  • 10
    • 0032003977 scopus 로고    scopus 로고
    • Lactolation of β-lactoglobulin monitored by electrospray ionization mass spectrometry
    • Morgan, F.; Bouhallab, S.; Molle, D.; Henry, G.; Maubois, J.-L.; Léonil, J. Lactolation of β-lactoglobulin monitored by electrospray ionization mass spectrometry. Int. Dairy J. 1998, 8, 95-98.
    • (1998) Int. Dairy J , vol.8 , pp. 95-98
    • Morgan, F.1    Bouhallab, S.2    Molle, D.3    Henry, G.4    Maubois, J.-L.5    Léonil, J.6
  • 12
    • 0002818849 scopus 로고
    • Structural analysis of dextrans from strains of Leuconostoc and related genera, that contain 3-O-α- D-glucosylated-D-glucopyranosyl residues at the branched points or in consecutive linear position
    • Seymour, F. R.; Knapp, R. D. Structural analysis of dextrans from strains of Leuconostoc and related genera, that contain 3-O-α- D-glucosylated-D-glucopyranosyl residues at the branched points or in consecutive linear position. Carbohydr. Res. 1980, 81, 105-129.
    • (1980) Carbohydr. Res , vol.81 , pp. 105-129
    • Seymour, F.R.1    Knapp, R.D.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
    • 33947486567 scopus 로고
    • Pyridoxine and pyridoxal analogs. VI. Electronic absorption spectra of Schiff bases
    • Heinert, D.; Martell, A. E. Pyridoxine and pyridoxal analogs. VI. Electronic absorption spectra of Schiff bases. J. Am. Chem. Soc. 1963, 85, 183-188.
    • (1963) J. Am. Chem. Soc , vol.85 , pp. 183-188
    • Heinert, D.1    Martell, A.E.2
  • 15
    • 0030949759 scopus 로고    scopus 로고
    • Inhibition of rabbit muscle aldolase phosphorylated aromatic compounds
    • Blonski, C.; De Moissac, D.; Perie, J.; Sygusch, J. Inhibition of rabbit muscle aldolase phosphorylated aromatic compounds. Biochem. J. 1997, 323, 71-77.
    • (1997) Biochem. J , vol.323 , pp. 71-77
    • Blonski, C.1    De Moissac, D.2    Perie, J.3    Sygusch, J.4
  • 17
    • 28444444586 scopus 로고    scopus 로고
    • Kinetics of formation and functional properties of conjugates prepared by dry-state incubation of β-lactoglobulin/acacia gum electrostatic complexes
    • Schmitt, C.; Bovay, C.; Frossard, P. Kinetics of formation and functional properties of conjugates prepared by dry-state incubation of β-lactoglobulin/acacia gum electrostatic complexes. J. Agric. Food Chem. 2005, 53, 9089-9099.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 9089-9099
    • Schmitt, C.1    Bovay, C.2    Frossard, P.3
  • 18
    • 0642281206 scopus 로고    scopus 로고
    • Use of multi-angle laser light scattering and size-exclusion chromatography to characterize the molecular weight and types of aggregates present in commercial whey protein products
    • Wang, T.; Lucey, J. A. Use of multi-angle laser light scattering and size-exclusion chromatography to characterize the molecular weight and types of aggregates present in commercial whey protein products. J. Dairy Sci. 2003, 86, 3091-3101.
    • (2003) J. Dairy Sci , vol.86 , pp. 3091-3101
    • Wang, T.1    Lucey, J.A.2
  • 19
    • 0001489984 scopus 로고    scopus 로고
    • Studies on the relationship between molecular weight and the color potency of fractions obtained by thermal treatment of glucose/amino acid and glucose/protein solutions by using ultracentrifugation and color dilution techniques
    • Hofmann, T. Studies on the relationship between molecular weight and the color potency of fractions obtained by thermal treatment of glucose/amino acid and glucose/protein solutions by using ultracentrifugation and color dilution techniques. J. Agric. Food Chem. 1998, 46, 3891-3895.
    • (1998) J. Agric. Food Chem , vol.46 , pp. 3891-3895
    • Hofmann, T.1
  • 20
    • 0000008540 scopus 로고    scopus 로고
    • Thermal unfolding of β-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation
    • Prabakaran, S.; Damodaran, S. Thermal unfolding of β-lactoglobulin: characterization of initial unfolding events responsible for heat-induced aggregation. J. Agric. Food Chem. 1997, 45, 4303-4308.
    • (1997) J. Agric. Food Chem , vol.45 , pp. 4303-4308
    • Prabakaran, S.1    Damodaran, S.2
  • 21
    • 17144422829 scopus 로고    scopus 로고
    • Denaturation and aggregation of three α-lactalbumin preparations at neutral pH
    • McGuffey, M. K.; Epting, K. L.; Kelly, R. M.; Foegeding, E. A. Denaturation and aggregation of three α-lactalbumin preparations at neutral pH. J. Agric. Food Chem. 2005, 53, 3182-3190.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 3182-3190
    • McGuffey, M.K.1    Epting, K.L.2    Kelly, R.M.3    Foegeding, E.A.4
  • 22
    • 0003019884 scopus 로고
    • Whey proteins and their thermal denaturation - a review
    • Mulvihill, D. M.; Donovan, M. Whey proteins and their thermal denaturation - a review. Ir. J. Food Sci. Technol. 1987, 11, 43-75.
    • (1987) Ir. J. Food Sci. Technol , vol.11 , pp. 43-75
    • Mulvihill, D.M.1    Donovan, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.