Rheological Properties of Thiolated and Succinylated Caseins

Autor:	V. H. Holsinger, E. D. Strange, D. H. Kleyn
Rok vydání:	1996
Předmět:	Chromatography Chemistry Lysine Succinic anhydride Chemical modification Concentration effect General Chemistry chemistry.chemical_compound Succinylation Rheology Reagent Casein Polymer chemistry General Agricultural and Biological Sciences
Zdroj:	Journal of Agricultural and Food Chemistry. 44:54-58
ISSN:	1520-5118 0021-8561
DOI:	10.1021/jf950046p
Popis:	Gelation of casein may be improved by introduction of functional groups that are capable of forming disulfide bonds. Thiolated whole caseins were prepared with S-acetylmercaptosuccinic anhydride and succinylated whole caseins with succinic anhydride. Thiolated caseins formed gels at protein concentrations of 5% or more at ambient temperatures after treatment with a deacetylating agent, due to air oxidation of the sulfhydryl groups to form disulfide bonds. Gelation rate and gel strength increased with increasing concentration of casein. Gels formed at 10% protein concentration when only 2.6 lysines/mol were modified by the thiolating reagent. However, increased lysine modification was only slightly related to more rapid gelling rate or increased gel strength. Gels formed had mechanical spectra that resembled those of weak gels (gums) in terms of moduli behavior during frequency sweeps, although absolute values were greater. Succinylated caseins and native casein did not form gels under these experimental conditions.
Databáze:	OpenAIRE
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