Abstract
Bovine β-lactoglobulin (βLG) is a major allergen in cow's milk. It is crucial to develop new methods that would reduce the allergenicity and not destroy the functional properties of βLG. To reduce allergenicity of βLG, tea catechins were bound to βLG to form βLG–catechin complex. The structure of βLG–catechin complex was analysed by circular dichroism (CD) spectra and fluorescence spectra assays. The results suggested that βLG was bound by catechin without apparent disruption of native conformation. Enzyme-linked immunosorbent assay (ELISA) indicated that the IgE-binding and IgG-binding activities of βLG were decreased upon catechin binding. Our study may be helpful for development of a new method to prepare milk proteins with reduced allergenicity.
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