Print Email Facebook Twitter The adsorption-induced secondary structure of β-casein and of distinct parts of its sequence in relation to foam and emulsion properties 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 Biologyβ-CaseinCircular dichroismPeptideProtein structureStructure-function relationshipTeflon interfaceCaseinsCircular DichroismEmulsionsHydrogen-Ion ConcentrationOsmolar ConcentrationPeptide FragmentsProtein Structure, Secondary To reference this document use: http://resolver.tudelft.nl/uuid:d801b484-e9e5-4fa5-9ee4-5f39cea07912 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 Files To receive the publication files, please send an e-mail request to TNO Library.