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Título
New Anthocyanin–Human Salivary Protein Complexes
Autor(es)
Materia
Salivary proteins
Astringency
Mass spectrometry
Saturation-transfer difference
Clasificación UNESCO
2302 Bioquímica
Fecha de publicación
2015
Citación
Ferrer Gallego, R. [et al.] (2015) New Anthocyanin - Human Salivary Protein Complexes, Langmuir 31(30), pp. 8392-8401. doi:10.1021/acs.langmuir.5b01122
Resumen
[EN] 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.
URI
ISSN
0743-7463
DOI
10.1021/acs.langmuir.5b01122
Versión del editor
Colecciones
- DQANB. Artículos [61]