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Maillard glycation of β-lactoglobulin induces conformation changes
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Chevalier F, Chobert J-M, Dalgalarrondo M, Choiset Y, Haertle T. Maillard glycation of β-lactoglobulin induces conformation changes. Nahrung/Food 2002;46:58-63.
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(2002)
Nahrung/Food
, vol.46
, pp. 58-63
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Chevalier, F.1
Chobert, J.-M.2
Dalgalarrondo, M.3
Choiset, Y.4
Haertle, T.5
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46
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0035530454
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Characterization of the Maillard reaction products of β-lactoglobulin glucosylated in mild conditions
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Chevalier F, Chobert J-M, Dalgarrondo M, Haertle T. Characterization of the Maillard reaction products of β-lactoglobulin glucosylated in mild conditions. J Food Biochem 2001;25:33-55.
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(2001)
J Food Biochem
, vol.25
, pp. 33-55
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Chevalier, F.1
Chobert, J.-M.2
Dalgarrondo, M.3
Haertle, T.4
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47
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0035603339
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Maillard glycation of β-lactoglobulin with several sugars: Comparative study of the properties of the obtained polymers and of the substituted sites
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note
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Chevalter F, Chobert J-M, Molle D, Haertle T. Maillard glycation of β-lactoglobulin with several sugars: Comparative study of the properties of the obtained polymers and of the substituted sites. Lait 2001;81:651-666. Maillard reactions represent a major cause of structural and chemical modifications of proteins during industrial food processing and storage. In this study, β-lactoglobulin was heated in solution at 60 °C in the presence of arabinose, galactose, glucose, lactose, rhamnose and ribose. An electrophoretic study of the different polymers separated by gel filtration was performed and binding site specificity of the different sugars was analyzed by mass spectrometry.
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(2001)
Lait
, vol.81
, pp. 651-666
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Chevalter, F.1
Chobert, J.-M.2
Molle, D.3
Haertle, T.4
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48
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0034921222
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Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar
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note
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Chevalier F, Chobert J-M, Popineau Y, Nicolas MG, Haertle T. Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar. Int Dairy J 2001;11:145-152. The great improvement of solubility, thermal stability, emulsifying and foaming properties of the protein was achieved using non-toxic chemical modifications through Maillard reaction with different in nature sugars (arabinose, galactose, glucose, lactose , rhamnose or ribose) that is of a great interest for the food industry. The data of this paper suggest that the nature of the sugar is an essential factor for improving the functional properties of food proteins.
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(2001)
Int Dairy J
, vol.11
, pp. 145-152
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Chevalier, F.1
Chobert, J.-M.2
Popineau, Y.3
Nicolas, M.G.4
Haertle, T.5
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49
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0033825099
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Dairy glycoconjugate emulsifiers: Casein-maltodextrins
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note
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Shepherd R, Robertson A, Ofman D. Dairy glycoconjugate emulsifiers: Casein-maltodextrins. Food Hydrocoll 2000;14:281-286. An economical, food-grade process based on the Amadori rearrangement of the Maillard reaction of the proteins with reducing sugars was suggested for a great improvement of functional properties of casein. The maltodextrin (dextrose equivalent of 10, that is an average degree of polymerization of 11 glucose units) was used for protein-glycoconjugate formation, because maltodextrins are cheap, non-toxic and widely available.
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(2000)
Food Hydrocoll
, vol.14
, pp. 281-286
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Shepherd, R.1
Robertson, A.2
Ofman, D.3
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50
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0034779981
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Scavenging of free radicals, antimicrobial, and cytotoxic activities of the Maillard reaction products of β-lactoglobulin glycated with several sugars
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Chevalier F, Chobert J-M, Genot C, Haertle T. Scavenging of free radicals, antimicrobial, and cytotoxic activities of the Maillard reaction products of β-lactoglobulin glycated with several sugars. J Agric Food Chem 2001;49:5031-5038.
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(2001)
J Agric Food Chem
, vol.49
, pp. 5031-5038
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Chevalier, F.1
Chobert, J.-M.2
Genot, C.3
Haertle, T.4
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