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Lookup NU author(s): Dr Julia Schuckel, Professor William WillatsORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
This study evaluates the capacity of four hydrolytic enzymes to limit the interactions between grape cell-walls and tannins and/or to favor tannin desorption. Adsorption and desorption tests were conducted by mixing a commercial seed tannin with purified skin cell-walls from Syrah grapes, in the presence or absence of hydrolytic enzymes, in a model-wine solution. The effects of the enzymes were evaluated by measuring the tannins in solution by High Performance Liquid Chromatography (HPLC) and the changes in the cell wall polysaccharide network by Comprehensive Microarray Polymer Profiling (COMPP) while the polysaccharides liberated from cell walls were analyzed by Size Exclusion Chromatography (SEC). The results showed that the enzymes limited the interaction between tannins and cell walls, especially cellulase, pectinase and xylanase, an effect associated with the cell wall structural modifications caused by the enzymes, which reduced their capacity to bind tannins. With regards to the tannin desorption process, enzymes did not play a significant role in liberating bound tannins. Those enzymes that showed the highest effect in limiting the adsorption of tannins and in disorganizing the cell wall structure, cellulase and pectinase, did not lead to a desorption of bound tannins, although they still showed a capacity of affecting cell wall structure. The results indicate that enzymes are not able to access those polysaccharides where tannins are bound, thus, they are not a useful tool for desorbing tannins from cell walls. The practical importance implications of these findings are discussed in the manuscript.
Author(s): Osete-Alcaraz A, Gomez-Plaza E, Martinez-Perez P, Weiller F, Schuckel J, Willats WGT, Moore JP, Ros-Garcia JM, Bautista-Ortin AB
Publication type: Article
Publication status: Published
Journal: Molecules
Year: 2021
Volume: 26
Issue: 3
Online publication date: 02/02/2021
Acceptance date: 29/01/2021
Date deposited: 08/04/2021
ISSN (electronic): 1420-3049
Publisher: MDPI AG
URL: https://doi.org/10.3390/molecules26030770
DOI: 10.3390/molecules26030770
PubMed id: 33540867
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