I. Marin et P. Relkin, Interaction properties of beta-lactoglobulin and benzaldehyde and effect on foaming properties of beta-lactoglobulin, FOOD CHEM, 71(3), 2000, pp. 401-406
Quenching of tryptophan fluorescence intensity and absence of covalently bo
und fluorescent products in beta-lactoglobulin solutions containing bt benz
aldehyde at various molar ratios, indicated that beta-lactoglobulin monomer
and benzaldehyde might associate through a non covalent binding mechanism.
The affinity constant determined from perturbation of tryptophan spectrofl
uorescence spectra was close to that previously observed by other authors f
or retinol binding to beta-lactoglobulin. In parallel foaming properties of
solutions of beta-lactoglobulin alone or in mixture with benzaldehyde were
investigated through a conductimetric method. It was observed that additio
n of benzaldehyde to beta-lactoglobulin led to enhanced foaming properties
in comparison with beta-lactoglobulin alone. These results were discussed i
n terms of formation of non covalently bound complexes with a specific surf
ace activy. (C) 2000 Elsevier Science Ltd. All rights reserved.