Heat-Induced Aggregation of Whey Proteins Is Enhanced by Addition of Thiolated β-Casein

Bovine β-casein has been chemically thiolated by reaction with thiolactone. The purified product was found to contain a variable number of free thiol groups in addition to a number of disulfide bridges. Gel electrophoresis under nonreducing conditions showed the presence of monomeric, dimeric, and t...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 1996-09, Vol.44 (9), p.2825-2828
Main Authors: Stevenson, E. M, Law, A. J. R, Leaver, J
Format: Article
Language:English
Subjects:
Biological and medical sciences
CASEIN
CASEINA
CASEINE
CONCENTRADOS DE PROTEINA
CONCENTRE DE PROTEINE
DENATURATION
DESNATURALIZACION
Food industries
Fundamental and applied biological sciences. Psychology
HEAT TREATMENT
Milk and cheese industries. Ice creams
PROTEIN CONCENTRATES
PROTEINAS DE SUERO DE LECHE
PROTEINE DE LACTOSERUM
TRAITEMENT THERMIQUE
TRATAMIENTO TERMICO
WHEY PROTEIN
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Summary:Bovine β-casein has been chemically thiolated by reaction with thiolactone. The purified product was found to contain a variable number of free thiol groups in addition to a number of disulfide bridges. Gel electrophoresis under nonreducing conditions showed the presence of monomeric, dimeric, and tetrameric forms of the protein. Heating whey protein concentrate in the presence of this thiolated casein resulted in a significant increase in the rate of aggregation of all of the whey proteins with the exception of α-lactalbumin, where in general the rate of aggregation decreased. This enhancement of the heat-induced aggregation was found to vary with the concentration of thiolated casein. The results are discussed with relevance to decreasing the costs of manufacture of whey protein concentrate. Keywords: Whey protein; β-casein; thiolation; heating; aggregation
ISSN:0021-8561
1520-5118
DOI:10.1021/jf950798j