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Time-dependent polymerization of beta-lactoglobulin through disulphide bonds at the oil-water interface in emulsions.

Abstract：

:Time-dependent intermolecular sulphydryl-disulphide interchange involving beta-lactoglobulin adsorbed at the oil-water interface in n-tetradecane-in-water emulsions (10 wt% oil, 0.5 wt% protein, pH 7.0) has been investigated using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). While only monomers are detected in the adsorbed protein immediately after emulsion formation with pure beta-lactoglobulin, on storing the emulsion the amount of polymerized beta-lactoglobulin and the sizes of the oligomers are found to increase with time. There is no polymerization of adsorbed protein in emulsions made with pure alpha-lactalbumin after 72 h, or in emulsions made with beta-lactoglobulin in the presence of a reagent (N-ethylmaleimide) for modifying sulphydryl groups. Analysis by two-dimensional SDS-PAGE of adsorbed protein from aged emulsions made with a mixture of alpha-lactalbumin + beta-lactoglobulin shows some linking by disulphide bonds between alpha-lactalbumin and beta-lactoglobulin at the interface. Taken together with earlier time-dependent surface viscosity measurements, the results indicate the important role of free sulphydryl groups in the development of the high surface viscoelasticity of adsorbed globular proteins at the oil-water interface.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Dickinson E,Matsumura Y

doi

10.1016/0141-8130(91)90006-g

subject

Has Abstract

pub_date

1991-02-01 00:00:00

pages

26-30

issue

1

eissn

0141-8130

issn

1879-0003

pii

0141-8130(91)90006-G

journal_volume

13

pub_type

杂志文章

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