Phase behavior of α-amino acids in multicomponent aqueous alkanol solutions

Gude, Michael T.; Wielen, Luuk A.M. van der; Luyben, Karel C.-H. A. M.

doi:10.1016/0378-3812(95)02878-1

Cited by 38 publications

(47 citation statements)

References 24 publications

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“…Several studies included the partition of amino acids in aqueous two-phase systems (ATPS), by using either polymer-salt, polymer-polymer, ionic liquid-salt or hydrophobic ionic liquid-water ATPS systems [4][5][6][7][8][9][10][11]. However, just a few liquid-liquid equilibrium data have been reported in the literature [12][13][14][15]. Solid-liquid equilibrium data have been also reported [16].…”

Section: Introductionmentioning

confidence: 89%

Liquid–Liquid Equilibria of Water + 1-Butanol + Amino Acid (Glycine or dl-Alanine or l-Leucine) at 313.15 K

2014

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Amino acids play an important role both in animal metabolism and in industrial processes. Since they are rarely found in nature in a free form, they must be obtained by biosynthesis or protein hydrolysis, often resulting in aqueous mixtures containing various solutes including several types of amino acids. As a consequence, the cost of the separation processes and concentration of amino acids can be as high as 90 % of their total manufacturing cost. In this way, the design of such processes requires knowledge of the partitioning behavior in two-phase systems and thermodynamic models should support this optimization procedure. However, both the complexity of biomolecules, due to their multiple functional groups, and the crucial role of water make the standard available thermodynamic models unattractive for the computation of phase behavior. Therefore, new thermodynamic models for the description of the phase behavior of systems containing biomolecules are required. In this work, liquid-liquid equilibrium data of the ternary systems 1-butanol ? water ? amino acid (glycine, DL-alanine or L-leucine) were measured at 313.15 K. The experimental results were correlated and interaction parameters were estimated for the modified-NRTL, UNIFAC and UNIFAC-Campinas models. The modified-NRTL model was able to describe the data better than the UNIFAC and UNIFACCampinas models.

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Section: Introductionmentioning

confidence: 89%

Liquid–Liquid Equilibria of Water + 1-Butanol + Amino Acid (Glycine or dl-Alanine or l-Leucine) at 313.15 K

2014

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“…The chapters included in Section II reflect three main research trends that have been pursued during the last 20 years to improve models for successful correlations: (i) the extension of existing excess models (NRTL, UNIQUAC, etc., see, e.g., [8]), (ii) osmotic virial models, and, closely related, models based on considering attractive and repulsive interactions 234 U. von Stockar between solutes via potentials of mean force (see, e.g., [9]), and (iii) correlative methods [10,11]. For instance, swelling behavior of charged and uncharged gels can be described with a combination of the Flory-Huggins theory, elastic deformation, and electrostatic effects (Chapter 6).…”

Section: Chaptersmentioning

confidence: 99%

The role of thermodynamics in biochemical engineering

Stockar

2013

Journal of Non-Equilibrium Thermodynamics

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This article is an adapted version of the introductory chapter of a book whose publication is imminent. It bears the title "BiothermodynamicsThe role of thermodynamics in biochemical engineering." The aim of the paper is to give a very short overview of the state of biothermodynamics in an engineering context as reflected in this book. Seen from this perspective, biothermodynamics may be subdivided according to the scale used to formalize the description of the biological system into three large areas: (i) biomolecular thermodynamics (most fundamental scale), (ii) thermodynamics of metabolism (intermediary scale), and (iii) whole-cell thermodynamics ("black-box" description of living entities). In each of these subareas, the main available theoretical approaches and the current and the potential applications are discussed. Biomolecular thermodynamics (i) is especially well developed and is obviously highly pertinent for the development of downstream processing. Its use ought to be encouraged as much as possible. The subarea of thermodynamics of live cells (iii), although scarcely applied in practice, is also expected to enhance bioprocess research and development, particularly in predicting culture performances, for understanding the driving forces for cellular growth, and in developing, monitoring, and controlling cellular cultures. Finally, there is no question that thermodynamic analysis of cellular metabolism (ii) is a promising tool for systems biology and for many other applications, but quite a large research effort is still needed before it may be put to practical use. IntroductionThermodynamics has had an enormous impact on a very wide variety of fields, including chemistry, biology, physics, geology, and in particular on applied engineering sciences such as chemical engineering [1]. Systematic application of chemical thermodynamics to process technology is one of the reasons why petrochemical plants can often be designed and petrochemical processes be developed with a bare minimum, if any, of experimental work.In biochemical engineering, the situation is radically different. The need for experimental trials is so overwhelming in bioprocess development that more often than not, extensive use is made of massively parallel experimentation involving such tools as microtiter plates, minireactors, robotic set-ups, and statistical experimental design. Therefore, the development of high-throughput systems and analytical equipment is now pursued at a very high pace. It can be speculated, however, that rigorous application of thermodynamics in biochemical engineering may be able to rationalize greatly bioprocess development and obviate a substantial fraction of this need for tedious experimental work [2].It was this vision that motivated a number of scientists about twenty years ago to organize an advanced course in thermodynamics for biochemical engineers to stimulate them to use thermodynamics more systematically in their work, and also to encourage further research in this area [2]. In the last 20 ye...

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“…34 Alanine, glycine in water-ethanol mixed solvent Chen et al 35 Electrolyte-NRTL Chen et al 35 16 amino acid-water systems and water þ salts, eight amino acid pairs, mixed water-ethanol solvents Modified UNIFAC Gupta and Heidemann 11 Glycine, serine, alanine, proline, hydroxylproline, valine, threonine, amino-butyric acid þ water Wilson, three-suffix Margules, NRTL Orella and Kirwan 30,31 Glycine, L-alanine, L-isoleucine, L-phenylalanine, Laspargine in alcohol-water solvents (miscible solutions) Electrolyte-UNIQUAC Peres and Macedo 36 Nine amino acid-water, five peptides-water UNIFAC þ Debye-H€ uckel Pinho et al 37 15 amino acid-water, five peptides-water Flory-Huggins þ Margules Gude et al 32,33 Seven amino acids (serine, glycine, alanine, tyrosine, isoleucine, phenylalanine, tryptophan) in water-ethanol, water-propanol, waterbutanol and water-octanol (partially miscible solutions) Polymer-type modified Wilson Xu et al 38 14 amino acids and peptides þ water, two mixed amino acids þ water Pitzer-Simonsen-Clegg Ferreira et al 39 Glycine, DL-alanine þ water-KCl and water-Na 2 SO 4 NRTL Ferreira et al 40 12 amino acids and diglycine þ water-alcohols Electrolyte-UNIQUAC SRK þ Kirkwood Moreover, the recovery and separation of amino acids often involve crystallization for which the solubility is the key property.…”

Section: Chemistry and Basic Relationshipsmentioning

confidence: 99%