4.7 Article

Understanding the molecular interactions between a yeast protein extract and phenolic compounds

Journal

FOOD RESEARCH INTERNATIONAL
Volume 143, Issue -, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.foodres.2021.110261

Keywords

Polyphenol-protein interactions; Plant-based beverages; Astringency; Bitterness; Fining; Fluorescence quenching

Funding

  1. EU FEDER funds [POCI-01-0247-FEDER-017687]
  2. [UIDB/50006/2020]
  3. Fundação para a Ciência e a Tecnologia [UIDB/50006/2020] Funding Source: FCT

Ask authors/readers for more resources

Phenolic compounds, including tannins, phenolic acids, and anthocyanins, are partially removed during fining process, affecting the organoleptic properties of beverages. Molecular studies are necessary to understand the effect of fining agents on the phenolic composition and resulting sensory changes. The interaction between these compounds and a yeast protein extract (YPE) as a potential new fining agent was studied, showing different binding affinities and effects based on temperature and solvent conditions.
Phenolic compounds are partially removed during fining, which may influence the organoleptic properties of beverages. Among phenolic compounds, tannins have been widely associated to the taste of beverages (namely astringency and bitterness). Furthermore, phenolic acids and anthocyanins may also influence bitterness and the latter are also responsible for beverages' color. Thus, it is necessary to perform molecular studies to better understand the effect of fining agents in the overall phenolic composition of beverages and the resulting organoleptic changes. The molecular interactions between these three classes of phenolic compounds and a yeast protein extract (YPE), designed as a new fining agent, was studied. The binding affinities were assessed by fluorescence quenching at two temperatures (21 degrees C and 37 degrees C) and in two reaction media (water and wine model solution). The size of aggregates formed was characterized by Dynamic Light Scattering and the selectivity of protein interaction was analyzed by electrophoresis. Overall, pentagalloylglucoside (tannin) showed the highest binding affinity for YPE, followed by malvidin 3-glucoside (anthocyanin), p-coumaric acid (phenolic acid) and gallic acid (phenolic acid). The studied temperatures and solvents affected the interaction affinities as well as the aggregates' size. Binding selectivity of proteins from YPE was not found. These results open new perspectives to control the fining process by using the YPE as a fining agent taking into account the further effect in the organoleptic properties of beverages.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available