메뉴 건너뛰기




Volumn 60, Issue 24, 2012, Pages 6204-6209

Structural changes imposed on whey proteins by UV irradiation in a continuous UV light reactor

Author keywords

denaturation; UV irradiation; UV reactor; whey proteins

Indexed keywords

AROMATIC AMINO ACID; CONTINUOUS-FLOW; DITYROSINE; INTRINSIC FLUORESCENCE; MIXING SPEED; OXIDATION PRODUCTS; PHYSICOCHEMICAL PROPERTY; PROTEIN CONFORMATION; STRUCTURAL CHANGE; SURFACE HYDROPHOBICITY; TERTIARY STRUCTURES; THIOL GROUPS; UV EXPOSURE; UV IRRADIATION; UV REACTORS; UV TREATMENT; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

EID: 84862573582     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf300278k     Document Type: Article
Times cited : (96)

References (25)
  • 1
    • 0034194538 scopus 로고    scopus 로고
    • Existing and potential applications of ultraviolet light in the food industry - A critical review
    • Bintsis, T.; Litopoulou-Tzanetaki, E.; Robinson, R. K. Existing and potential applications of ultraviolet light in the food industry - a critical review J. Sci. Food Agric. 2000, 80, 637-645
    • (2000) J. Sci. Food Agric. , vol.80 , pp. 637-645
    • Bintsis, T.1    Litopoulou-Tzanetaki, E.2    Robinson, R.K.3
  • 3
    • 8144223174 scopus 로고    scopus 로고
    • Influence of apple cultivars on inactivation of different strains of Escherichia coli O157:H7 in apple cider by UV irradiation
    • Basaran, N.; Quintero-Ramos, A.; Moake, M. M.; Churey, J. J.; Worobo, R. W. Influence of apple cultivars on inactivation of different strains of Escherichia coli O157:H7 in apple cider by UV irradiation Appl. Environ. Microbiol. 2004, 70, 6061-6065
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 6061-6065
    • Basaran, N.1    Quintero-Ramos, A.2    Moake, M.M.3    Churey, J.J.4    Worobo, R.W.5
  • 5
    • 0343959372 scopus 로고
    • Ultraviolet irradiation of milk
    • Burton, H. Ultraviolet irradiation of milk Dairy Sci. Abstr. 1951, 13, 229-244
    • (1951) Dairy Sci. Abstr. , vol.13 , pp. 229-244
    • Burton, H.1
  • 6
    • 0016790104 scopus 로고
    • Studies on the ripening of 'Grana Padano' cheese manufactured from milk irradiated with UV light
    • Caserio, G.; Bianchi, M. A.; Beretta, G.; Dragoni, I. Studies on the ripening of 'Grana Padano' cheese manufactured from milk irradiated with UV light Eur. J. Appl. Microbiol. 1975, 1, 247-257
    • (1975) Eur. J. Appl. Microbiol. , vol.1 , pp. 247-257
    • Caserio, G.1    Bianchi, M.A.2    Beretta, G.3    Dragoni, I.4
  • 9
    • 0036712109 scopus 로고    scopus 로고
    • Photoexcitation of tryptophan groups induces reduction of two disulfide bonds in goat α-lactalbumin
    • Vanhooren, A.; Devreese, B.; Vanhee, K.; Van Beeumen, J.; Hanssens, I. Photoexcitation of tryptophan groups induces reduction of two disulfide bonds in goat α-lactalbumin Biochemistry 2002, 41, 11035-11043
    • (2002) Biochemistry , vol.41 , pp. 11035-11043
    • Vanhooren, A.1    Devreese, B.2    Vanhee, K.3    Van Beeumen, J.4    Hanssens, I.5
  • 11
    • 0037292549 scopus 로고    scopus 로고
    • Modelling of mixing in a Taylor-Couette reactor with axial flow
    • Syed, A.; Fruh, W. G. Modelling of mixing in a Taylor-Couette reactor with axial flow J. Chem. Technol. Biotechnol. 2003, 78, 227-235
    • (2003) J. Chem. Technol. Biotechnol. , vol.78 , pp. 227-235
    • Syed, A.1    Fruh, W.G.2
  • 12
    • 0001406422 scopus 로고    scopus 로고
    • Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation
    • Dalgleish, D. G.; Senaratne, V.; Francois, S. Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation J. Agric. Food Chem. 1997, 45, 3459-3464
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 3459-3464
    • Dalgleish, D.G.1    Senaratne, V.2    Francois, S.3
  • 13
    • 2342527129 scopus 로고    scopus 로고
    • Probing structural features of water-insoluble proteins by front-face fluorescence
    • Bonomi, F.; Mora, G.; Pagani, M. A.; Iametti, S. Probing structural features of water-insoluble proteins by front-face fluorescence Anal. Biochem. 2004, 329, 104-111
    • (2004) Anal. Biochem. , vol.329 , pp. 104-111
    • Bonomi, F.1    Mora, G.2    Pagani, M.A.3    Iametti, S.4
  • 14
  • 17
    • 0026439297 scopus 로고
    • Deuterium isotope effects in constrained tryptophan derivatives: Implications for tryptophan photophysics
    • McMahon, L. P.; Colucci, W. J.; McLaughlin, M. L.; Barkley, M. D. Deuterium isotope effects in constrained tryptophan derivatives: implications for tryptophan photophysics J. Am. Chem. Soc. 1992, 114, 8442-8448
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8442-8448
    • McMahon, L.P.1    Colucci, W.J.2    McLaughlin, M.L.3    Barkley, M.D.4
  • 18
    • 0029904741 scopus 로고    scopus 로고
    • The peptide bond quenches indole fluorescence
    • Chen, Y.; Liu, B.; Yu, H.; Barkley, M. D. The peptide bond quenches indole fluorescence J. Am. Chem. Soc. 1996, 118, 9271-9278
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9271-9278
    • Chen, Y.1    Liu, B.2    Yu, H.3    Barkley, M.D.4
  • 19
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen, Y.; Barkley, M. D. Toward understanding tryptophan fluorescence in proteins Biochemistry 1998, 37, 9976-9982
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 21
    • 33751158541 scopus 로고
    • Heat-induced conformational changes in whey protein isolate and its relation to foaming properties
    • Zhu, H.; Damodaran, S. Heat-induced conformational changes in whey protein isolate and its relation to foaming properties J. Agric. Food Chem. 1994, 42, 846-855
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 846-855
    • Zhu, H.1    Damodaran, S.2
  • 22
    • 1542575976 scopus 로고    scopus 로고
    • Heat-induced denaturation/aggregation of β-lactoglobulin A and B: Kinetics of the first intermediates formed
    • Croguennec, T.; O'Kennedy, B. T.; Mehra, R. Heat-induced denaturation/aggregation of β-lactoglobulin A and B: kinetics of the first intermediates formed Int. Dairy J. 2004, 14, 399-409
    • (2004) Int. Dairy J. , vol.14 , pp. 399-409
    • Croguennec, T.1    O'Kennedy, B.T.2    Mehra, R.3
  • 23
    • 0021344070 scopus 로고
    • Photochemistry of proteins: A review
    • Grossweiner, L. I. Photochemistry of proteins: a review Curr. Eye Res. 1984, 3, 137-144
    • (1984) Curr. Eye Res. , vol.3 , pp. 137-144
    • Grossweiner, L.I.1
  • 25
    • 0000443256 scopus 로고
    • Structural and conformational basis of the resistance of β-lactoglobulin to peptic and chymotryptic digestion
    • Reddy, I. M.; Kella, N. K. D.; Kinsella, J. E. Structural and conformational basis of the resistance of β-lactoglobulin to peptic and chymotryptic digestion J. Agric. Food Chem. 1988, 36, 737-741
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 737-741
    • Reddy, I.M.1    Kella, N.K.D.2    Kinsella, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.