Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 531358
Title Modelling the effects of ethanol on the solubility of the proteinogenic amino acids with the NRTL, Gude and Jouyban-Acree models
Author(s) Bowden, Nathan A.; Sevillano, David Mendez; Sanders, Johan P.M.; Bruins, Marieke E.
Source Fluid Phase Equilibria 459 (2018). - ISSN 0378-3812 - p. 158 - 169.
DOI http://dx.doi.org/10.1016/j.fluid.2017.11.036
Department(s) Biobased Chemistry and Technology
Biobased Products
VLAG
FBR Food Technology
Publication type Refereed Article in a scientific journal
Publication year 2018
Availibility Full text available from 2019-12-22
Keyword(s) Aqueous-solutions - Equilibria - Excess solubility - Organic solvents - Thermodynamics
Abstract The addition of organic solvents, such as ethanol, to molecules in solution is an effective process for crystallization and is used in industrial settings (i.e. pharmaceutical production, downstream processing, etc.). In this study, we use solubility data of all proteinogenic α-amino acids in binary ethanol/water systems to model their excess solubility. We use the empirical and regressive models of Gude and NRTL and the predictive Jouyban-Acree model. Based on the results, we hypothesize that amino acids that are spherical and lack a reactive side chain show little or no excess solubility. Being rod-like and/or having a reactive side chain leads to a positive excess solubility in a mixed solvent of ethanol and water. The empirical and regressed models, NRTL and Gude, fit the data well and the predictive Jouyban-Acree model, not originally intended to be used for small molecules, is less accurate but offers insights into the thermodynamic properties of the amino acids.
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