Sweet proteins are the sweetest natural molecules. This aspect prompted several proposals for their use as food additives, mainly because the amounts to be added to food would be very small and safe for people suffering from sucrose-linked diseases. During studies of sweet proteins as food additives we found that their sweetness is affected by water salinity, while there is no influence on protein’s structure. Parallel tasting of small size sweeteners revealed no influence of the water quality. This result is explained by the interference of ionic strength with the mechanism of action of sweet proteins and provides an experimental validation of the wedge model for the interaction of proteins with the sweet receptor.
Striking Dependence of Protein Sweetness on Water Quality: The Role of the Ionic Strength / Delfi, Masoud; Emendato, Alessandro; Temussi, PIERO ANDREA; Picone, Delia. - In: FRONTIERS IN MOLECULAR BIOSCIENCES. - ISSN 2296-889X. - 8:705102(2021), pp. 1-7. [10.3389/fmolb.2021.705102]
Striking Dependence of Protein Sweetness on Water Quality: The Role of the Ionic Strength
Masoud DelfiPrimo
Investigation
;Alessandro EmendatoSecondo
Investigation
;Piero Andrea TemussiPenultimo
Conceptualization
;Delia Picone
Ultimo
Supervision
2021
Abstract
Sweet proteins are the sweetest natural molecules. This aspect prompted several proposals for their use as food additives, mainly because the amounts to be added to food would be very small and safe for people suffering from sucrose-linked diseases. During studies of sweet proteins as food additives we found that their sweetness is affected by water salinity, while there is no influence on protein’s structure. Parallel tasting of small size sweeteners revealed no influence of the water quality. This result is explained by the interference of ionic strength with the mechanism of action of sweet proteins and provides an experimental validation of the wedge model for the interaction of proteins with the sweet receptor.File | Dimensione | Formato | |
---|---|---|---|
pubblicato.pdf
accesso aperto
Descrizione: Articolo principale
Tipologia:
Versione Editoriale (PDF)
Licenza:
Dominio pubblico
Dimensione
1.97 MB
Formato
Adobe PDF
|
1.97 MB | Adobe PDF | Visualizza/Apri |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.