Title
The adsorption-induced secondary structure of β-casein and of distinct parts of its sequence in relation to foam and emulsion properties
Author
Caessens, P.W.J.R.
de Jongh, H.H.J.
Norde, W.
Gruppen, H.
TNO Voeding
Publication year
1999
Abstract
Changes in the secondary structure upon adsorption of β-casein (βCN) and of distinct parts of its sequence were investigated by far-ultraviolet circular dichroism in order to find suggested relationships with foam and emulsion-forming and -stabilising properties of the same protein/peptides. A teflon/water interface was used as a model system for foam and emulsion interfaces. The maximum surface loads of β-casein and its derived peptides were investigated. The main secondary structure element of all samples in solution was the unordered random coil, but upon adsorption ordered structure, especially α-helix, was induced. At lower pH more ordered structure was induced, just as at lower ionic strength. Apparently, both hydrophobic and hydrophilic groups influence the change of secondary structure induced at a hydrophobic interface. The results suggest that the hydrophobic C-terminal half of βCN accounted for the high maximum surface load on teflon, while the N-terminal half of βCN seemed to be responsible for the secondary structure induction upon adsorption. A relation between the maximum surface load and the foam-stabilising properties was found, but an influence of the secondary structure properties on the foam and emulsion-forming and -stabilising properties was not observed. Copyright (C) 1999 Elsevier Science B.V.
Subject
Biology
β-Casein
Circular dichroism
Peptide
Protein structure
Structure-function relationship
Teflon interface
Caseins
Circular Dichroism
Emulsions
Hydrogen-Ion Concentration
Osmolar Concentration
Peptide Fragments
Protein Structure, Secondary
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DOI
https://doi.org/10.1016/s0167-4838(98)00274-x
TNO identifier
234942
ISSN
0167-4838
Source
Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1430 (1), 73-83
Document type
article