Analysis of protein gels formed by interfacial partitioning

被引：10

作者：

Borbás, R

Turza, S

Szamos, J

Kiss, É

机构：

[1] Eotvos Lorand Univ, Dept Colloid Chem, H-1518 Budapest 112, Hungary

[2] Cent Food Res Inst, H-1537 Budapest, Hungary

来源：

COLLOID AND POLYMER SCIENCE | 2001年 / 279卷 / 07期

关键词：

three-phase partitioning; emulsion gel; protein separation; stress-deformation behaviour of bovine serum albumin and ovalbumin gels;

D O I：

10.1007/s003960000475

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

A special combination of alcoholic precipitation and salting out of proteins was described as three-phase partitioning (TPP). Proteins are accumulated in a coherent middle phase in the partitioning system composed of tert-butanol, ammonium sulphate and water. Partitioning systems with various ratios of components were investigated. The composition and the mechanical properties of the middle phase were determined in model systems using bovine serum albumin or ovalbumin. Quantitative analysis revealed that beside the protein content (2-10wt %) other components of the middle phase formed two immiscible liquid phases. The stress-deformation relationship obtained by uniaxial compression showed the elastic behaviour of the middle phase. The results suggested that the middle phase formed in TPP is an emulsion gel. A possible mechanism of the formation of an emulsion gel was outlined.

引用

页码：705 / 713

页数：9

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