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A model system for studying protein binding to hydrophobic surfaces in emulsions
Author(s) -
Brock Christopher J.,
Enser Michael
Publication year - 1987
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740400309
Subject(s) - globular protein , chemistry , bovine serum albumin , hydrophobic effect , chemical engineering , covalent bond , kinetics , biophysics , porous glass , chromatography , porosity , crystallography , organic chemistry , biology , physics , quantum mechanics , engineering
A method is described for chemical modification of porous glass particles so that they are coated with a covalently linked layer of close‐packed, long chains of mixed alkyl and alkoxy types. This hydrophobic controlled‐pore glass is a useful model system for physico‐chemical studies of the hydrophobic interactions between proteins and fat particles in emulsions. Under non‐denaturing conditions non‐globular proteins (myosin, α‐, β‐ and χ‐caseins) bind more strongly than globular proteins (G‐actin, bovine serum albumin) in this system. Binding kinetics as well as binding strength are important in determining the composition of interfacial films in complex emulsions containing many proteins.