‘New views’ on structure–function relationships in milk proteins

• Published in: Trends in Food Science & Technology Vol. 12; no. 9; pp. 339 - 346
• Main Authors: Qi, P.X, Brown, E.M, Farrell, H.M
• Format: Book Review Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01-09-2001; Elsevier
• Subjects: Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts; Biological and medical sciences; Food industries; Fundamental and applied biological sciences. Psychology; Milk and cheese industries. Ice creams; Aggregation; Milk protein; Casein; Hydration; Molecular structure; Lactalbumin; Disulfide bond; Technological properties
• ISSN: 0924-2244; 1879-3053
• DOI: 10.1016/S0924-2244(02)00009-2

The molten globule state has been regarded as a major intermediate in protein folding. It is characterized by native-like secondary structure with a compact molecular size but little specific tertiary structure. α-lactalbumin under various denaturing conditions has been considered a paradigm of the classical molten globule state. It has been shown that caseins share many of the same properties and may therefore exist naturally in a molten globule-like state with defined secondary structure and limited fluctuating tertiary structure, which lead to their propensity for polymerization. The architectural concepts of tensegrity may be used to describe, in part, the structure of casein polymers.