Mendez Sevillano D.,Julianalaan |
van der Wielen L.A.M.,Julianalaan |
Hooshyar N.,Unilever |
Fluid Phase Equilibria | Year: 2014
Modified UNIFAC (Mod. UNIFAC) is a proven model for the prediction of activity coefficients of molecules in non-ideal mixtures. However, Mod. UNIFAC is often not accurate when hydrogen bonding or strong hydrophobic interactions are present. An interesting group of molecules called polyphenols presents both types of interactions and therefore, Mod. UNIFAC predictions are not always accurate. A polyphenol-specific UNIFAC-based method (MPP-UNIFAC) has been developed in this study for its application on polyphenol-like molecules. Interaction parameters were regressed from 410 solubility data points from polyphenols in literature showing a good fit. The average error of the fit is 0.094 log units, better than the average value for Mod. UNIFAC (0.5 log units). Moreover, the model was validated against three datasets that were not used for the regression giving more accurate predictions than the Mod. UNIFAC it was developed from. © 2014 Elsevier B.V.
Sevillano D.M.,Julianalaan |
Van Der Wielen L.A.M.,Julianalaan |
Hooshyar N.,Unilever |
Food and Bioproducts Processing | Year: 2014
This work focuses on the rapid selection of a resin from a defined set of macroporous polymeric resins for the decaffeination of catechins from green tea. High-throughput experimentation and design of experiments are used in order to retrieve as much information as possible from a small set of experiments on the interaction of components with the resins. A multicomponent Langmuir isotherm model is used to describe the adsorption and parameters are regressed with high accuracy. These parameters are subsequently used for the definition of criteria to calculate a weighted resin score. The optimal resin is Diaion 20HP with a score of 90.50%, mainly due to its good selectivity for caffeine over catechin (3). © 2014 The Institution of Chemical Engineers.
Li F.,Dreijenplein |
Dea Wolf F.A.,Dreijenplein |
Marcelis A.T.M.,Dreijenplein |
Sudholter E.J.R.,Julianalaan |
And 2 more authors.
Angewandte Chemie - International Edition | Year: 2010
Trigger the block: Stable biocompatible protein polymersomes can be generated by a triggered templated self-assembly route (see picture). Pluronic L121 vesicles (red core with blue corona) take up a biosynthetic triblock copolymer CSXSXC into their unilamellar shell. In response to changes in pH (trigger), the Sa block becomes hydrophobic and adapts to the template vesicle, thus directing the formation of protein polymersomes. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.