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Volumn 7, Issue 5-6, 2002, Pages 438-444

Food protein interactions in sugar solutions

Author keywords

Gelation; Interactions; Proteins; Self assembly; Sugars; Surface activity; Thermal stability

Indexed keywords

BETA LACTOGLOBULIN; CASEIN; MALTODEXTRIN; MILK PROTEIN; OVALBUMIN; POLYSACCHARIDE; PROTEIN; SUGAR; SURFACTANT;

EID: 0036866010     PISSN: 13590294     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0294(02)00079-1     Document Type: Review
Times cited : (74)

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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.
    • (2001) Lait , vol.81 , pp. 651-666
    • Chevalter, F.1    Chobert, J.-M.2    Molle, D.3    Haertle, T.4
  • 48
    • 0034921222 scopus 로고    scopus 로고
    • Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar
    • note
    • 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.
    • (2001) Int Dairy J , vol.11 , pp. 145-152
    • Chevalier, F.1    Chobert, J.-M.2    Popineau, Y.3    Nicolas, M.G.4    Haertle, T.5
  • 49
    • 0033825099 scopus 로고    scopus 로고
    • Dairy glycoconjugate emulsifiers: Casein-maltodextrins
    • note
    • 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.
    • (2000) Food Hydrocoll , vol.14 , pp. 281-286
    • Shepherd, R.1    Robertson, A.2    Ofman, D.3
  • 50
    • 0034779981 scopus 로고    scopus 로고
    • Scavenging of free radicals, antimicrobial, and cytotoxic activities of the Maillard reaction products of β-lactoglobulin glycated with several sugars
    • 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.
    • (2001) J Agric Food Chem , vol.49 , pp. 5031-5038
    • Chevalier, F.1    Chobert, J.-M.2    Genot, C.3    Haertle, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.