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New Anthocyanin–Human Salivary Protein Complexes

2015; American Chemical Society; Volume: 31; Issue: 30 Linguagem: Inglês

10.1021/acs.langmuir.5b01122

1520-5827

Raúl Ferrer‐Gallego, Susana Soares, Nuno Mateus, Julián C. Rivas‐Gonzalo, M. Teresa Escribano-Bailón, Víctor de Freitas,

Biochemical Analysis and Sensing Techniques

The interaction between phenolic compounds and salivary proteins is considered the basis of the poorly understood phenomenon of astringency. Furthermore, this interaction is an important factor in relation to their bioavailability. In this work, interactions between anthocyanin and human salivary protein fraction were studied by mass spectrometry (MALDI-TOF-MS and FIA-ESI-MS) and saturation-transfer difference (STD) NMR spectroscopy. Anthocyanins were able to interact with saliva proteins. The dissociation constant (KD) between malvidin 3-glucoside and salivary proline-rich proteins was 1.92 mM for the hemiketal form (pH 3.4) and 1.83 mM for the flavylium cation (pH 1.0). New soluble complexes between these salivary proteins and malvidin 3-glucoside were identified for the first time.