Higher Order Structures of the Caseins: A Paradox?
- H. M. FarrellJrAffiliated withU.S.D.A., Eastern Regional Research Center Email author
- , E. M. BrownAffiliated withU.S.D.A., Eastern Regional Research Center
- , E. L. MalinAffiliated withU.S.D.A., Eastern Regional Research Center
Historically caseins were classified as random coils. Recent advances in the field of protein chemistry have produced a “New View” of protein structure. Casein structures are interpreted with regard to the latter theory and are now considered to be members of the class of proteins referred to as natively unfolded or molten globule. The caseins display the characteristics of this class of proteins as they react with each other using defined structural elements to form large, open, hydrated, flexible structures. These casein–casein interactions give the product, sodium caseinate, its reliable properties as a food ingredient. Overall, the concept that the caseins are both structured and flexible is explained using the architectural concepts of tensegrity.
- Higher Order Structures of the Caseins: A Paradox?
- Book Title
- Advanced Dairy Chemistry
- Book Subtitle
- Volume 1A: Proteins: Basic Aspects, 4th Edition
- pp 161-184
- Print ISBN
- Online ISBN
- Springer US
- Copyright Holder
- Springer Science+Business Media New York
- Additional Links
- Industry Sectors
- eBook Packages
- Editor Affiliations
- ID1. School of Food and Nutritional Sciences
- ID2. Fac. Food Technology & Nutrition, Dept. Food Science, University College Cork
- Author Affiliations
- 00051. U.S.D.A., Eastern Regional Research Center, Wyndmoor, PA, 19038, USA
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