Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Effects of Disulfide Reduction on the Emulsifying Properties of Bovine Serum Albumin
Jin Young LEEMasaaki HIROSE
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1992 Volume 56 Issue 11 Pages 1810-1813

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Abstract

Bovine serum albumin was reduced by incubating with various concentrations (0-200 mM) of 2-mercaptoethanol, and its emulsifying properties were examined for an oil-in-water emulsion system. A particle size analysis revealed that albumin reduced at 30 mM of the thiol yielded smaller oil particles than either native protein, or the protein reduced at 70 or 200 mM of the thiol. Furthermore, the particle size was almost constant during 35 days of storage with albumin reduced at 30 mM of the thiol, while an emulsion prepared using the native protein, or the protein reduced at 70 or 200 mM of the thiol was unstable during the same storage period. Gel filhation chromatography and transmission electron micrography show that serum albumin made aggregates with high molecular size by its disulfide reduction with 70 or 200 mM, but not with 30 mM of 2-mercaptoethanol. It was, therefore, concluded that time emulsifying property of serum albumin can be improved by a mild disufide reduction.

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