Abstract
The aim of this work is to investigate the driving forces involved in amino acid solubilization in cationic reversed micelles, and to determine in which way different parameters affect the reversed micellar structure and amino acid solubilization, in order to select the best conditions to optimize amino acid extraction. To this end, extraction equilibrium experiments were performed using different experimental conditions and three amino acids with different structures: aspartic acid - a hydrophilic amino acid, phenylalanine - a slightly hydrophobic amino acid, and tryptophan - a hydrophobic amino acid. The study of the effect of amino acid related parameters, such as pH and the initial amino acid concentration in the aqueous phase, and the effect of parameters that influence the reversed micellar structure, such as surfactant concentration, ionic strength and co-surfactant concentration, provides useful information about the driving forces involved, solute-micelle interfacial interactions and solute location in the cationic system trioctylmethylammonium chloride (TOMAC)I hexanol/n-heptane. These parameters can be adjusted to optimize amino acid extraction. It is shown that amino acids with the same isoelectric point can be selectively separated by exploring the different interactions they establish with the reversed micellar interface.
| Original language | English |
|---|---|
| Pages (from-to) | 801-811 |
| Number of pages | 11 |
| Journal | Journal of Chemical Technology and Biotechnology |
| Volume | 74 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - 1 Aug 1999 |
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Keywords
- Amino acid solubilization
- Cationic surfactants
- Hyrdrophobic effect
- Reversed micelles
Cite this
}
Amino acid solubilization in cationic reversed micelles : Factors affecting amino acid and water transfer. / Cardoso, Maria M.; Barradas, Mário J.; Kroner, Karl H.; Crespo, João G.
In: Journal of Chemical Technology and Biotechnology, Vol. 74, No. 8, 01.08.1999, p. 801-811.Research output: Contribution to journal › Article
TY - JOUR
T1 - Amino acid solubilization in cationic reversed micelles
T2 - Factors affecting amino acid and water transfer
AU - Cardoso, Maria M.
AU - Barradas, Mário J.
AU - Kroner, Karl H.
AU - Crespo, João G.
PY - 1999/8/1
Y1 - 1999/8/1
N2 - The aim of this work is to investigate the driving forces involved in amino acid solubilization in cationic reversed micelles, and to determine in which way different parameters affect the reversed micellar structure and amino acid solubilization, in order to select the best conditions to optimize amino acid extraction. To this end, extraction equilibrium experiments were performed using different experimental conditions and three amino acids with different structures: aspartic acid - a hydrophilic amino acid, phenylalanine - a slightly hydrophobic amino acid, and tryptophan - a hydrophobic amino acid. The study of the effect of amino acid related parameters, such as pH and the initial amino acid concentration in the aqueous phase, and the effect of parameters that influence the reversed micellar structure, such as surfactant concentration, ionic strength and co-surfactant concentration, provides useful information about the driving forces involved, solute-micelle interfacial interactions and solute location in the cationic system trioctylmethylammonium chloride (TOMAC)I hexanol/n-heptane. These parameters can be adjusted to optimize amino acid extraction. It is shown that amino acids with the same isoelectric point can be selectively separated by exploring the different interactions they establish with the reversed micellar interface.
AB - The aim of this work is to investigate the driving forces involved in amino acid solubilization in cationic reversed micelles, and to determine in which way different parameters affect the reversed micellar structure and amino acid solubilization, in order to select the best conditions to optimize amino acid extraction. To this end, extraction equilibrium experiments were performed using different experimental conditions and three amino acids with different structures: aspartic acid - a hydrophilic amino acid, phenylalanine - a slightly hydrophobic amino acid, and tryptophan - a hydrophobic amino acid. The study of the effect of amino acid related parameters, such as pH and the initial amino acid concentration in the aqueous phase, and the effect of parameters that influence the reversed micellar structure, such as surfactant concentration, ionic strength and co-surfactant concentration, provides useful information about the driving forces involved, solute-micelle interfacial interactions and solute location in the cationic system trioctylmethylammonium chloride (TOMAC)I hexanol/n-heptane. These parameters can be adjusted to optimize amino acid extraction. It is shown that amino acids with the same isoelectric point can be selectively separated by exploring the different interactions they establish with the reversed micellar interface.
KW - Amino acid solubilization
KW - Cationic surfactants
KW - Hyrdrophobic effect
KW - Reversed micelles
UR - http://www.scopus.com/inward/record.url?scp=0032839922&partnerID=8YFLogxK
U2 - 10.1002/(SICI)1097-4660(199908)74:8<801::AID-JCTB107>3.0.CO;2-Y
DO - 10.1002/(SICI)1097-4660(199908)74:8<801::AID-JCTB107>3.0.CO;2-Y
M3 - Article
VL - 74
SP - 801
EP - 811
JO - Journal of Chemical Technology and Biotechnology
JF - Journal of Chemical Technology and Biotechnology
SN - 0142-0356
IS - 8
ER -