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Effect of NaCl and NaNO3 on the Partial Molar Volumes and Partial Molar
Isentropic Compressibilities of Some Amino Acids at Several Different
Temperatures (298.15–328.15) K

Article  in  Journal of Solution Chemistry · August 2012

DOI: 10.1007/s10953-012-9860-1

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J Solution Chem (2012) 41:1144–1155
DOI 10.1007/s10953-012-9860-1

Effect of NaCl and NaNO3 on the Partial Molar Volumes

and Partial Molar Isentropic Compressibilities of Some
Amino Acids at Several Different Temperatures
(298.15–328.15) K

Riyazuddeen · Sadaf Afrin

Received: 13 October 2010 / Accepted: 13 October 2011 / Published online: 18 July 2012
© Springer Science+Business Media, LLC 2012

Abstract The partial molar volumes, ϕvo , and partial molar isentropic compressibilities, ϕko ,
values have been computed using density and speed of sound values of L-phenylalanine/
L-leucine/L-glutamic acid/L-proline in 2 mol · L−1 aqueous NaCl or NaNO3 solutions, mea-
sured as a function of the amino acid concentration at temperatures of 298.15, 303.15,
308.15, 313.15, 318.15, 323.15 and 328.15 K. The variation of ϕvo values among the amino
acids studied was found to follow the order proline < glutamic acid < leucine < pheny-
lalanine. The increase in the partial molar volume of an amino acid with increasing in tem-
perature has been attributed to the volume expansion of the hydrated zwitterions. The ϕvo
and ϕko values of L-phenylalanine, L-leucine, L-glutamic acid, and L-proline in 2 mol · L−1
aqueous NaCl and NaNO3 solutions have been found to be larger than the corresponding
values in water. The larger partial molar volumes of L-phenylalanine, L-leucine, L-glutamic
acid, and L-proline in 2 mol · L−1 aqueous NaCl and NaNO3 solutions have been ascribed to
the possible formation of ‘zwitterion–Na+ /Cl− /NO− + − −
3 ’ and ‘Na /Cl /NO3 –water dipole’
entities in solutions. The formation of these entities in solutions causes the release of wa-
ter associated with zwitterions to the bulk water. The larger partial molar compressibilities
of L-phenylalanine, L-leucine, L-glutamic acid and L-proline in 2 mol · L−1 aqueous NaCl
NaNO3 solutions compared to the corresponding values in water has been attributed to the
formation of these ‘zwitterion–ion’ and ‘ion–water dipole’ entities.

Keywords Partial molar volume · Partial molar isentropic compressibility · Zwitterion–ion

interactions · Amino acid · Salt

Electronic supplementary material The online version of this article

(doi:10.1007/s10953-012-9860-1) contains supplementary material, which is available to authorized
users.
Riyazuddeen () · S. Afrin
Department of Chemistry, Aligarh Muslim University, Aligarh, UP, 202002, India
e-mail: rz1@rediffmail.com
J Solution Chem (2012) 41:1144–1155 1145

1 Introduction

The study of the interactions of proteins with ions is useful in understanding the properties
and functions of proteins in mixed aqueous solutions. The study of (protein + solvent)
interactions is difficult because of the complexity of interactions with such a large bio-
molecule. However, one useful approach, which can help in our understanding of these
interactions, is to study simple compounds like amino acids and peptides that mimic some
specific aspects of the protein structure.
The partial molar volume and partial molar isentropic compressibility are known to be
sensitive to the nature of hydration and are powerful thermodynamic parameters for elu-
cidation of noncovalent interactions occurring in solutions and characterizing the structure
and properties of solutions [1]. A number of authors have studied the partial molar vol-
ume and partial molar compressibility in order to understand the interactions of amino acids
and peptides with salts such as NH4 Cl, NaCl, KCl, Na2 SO4 , KSCN, MgCl2 , and CaCl2
[2–17] which act as stabilizers/destabilizers. The partial molar volumes and partial molar
compressibilities of L-alanine, L-proline, L-valine and L-leucine in 2 mol · L−1 aqueous
KCl and KNO3 [18], and of L-histidine, L-glutamic acid, L-tryptophan and glycylglycine
in 2 mol · L−1 aqueous KCl and KNO3 solutions [19], have been previously studied in our
laboratory. These results have been discussed in terms of solute–solvent and solute–solute
interactions.
In this study, the partial molar volumes and partial molar isentropic compressibilities of
the amino acids L-phenylalanine, L-leucine, L-glutamic acid and L-proline in 2 mol · L−1
aqueous NaCl and NaNO3 solutions are reported as functions of the molal concentration of
the amino acids and temperature (298.15, 303.15, 308.15, 313.15, 318.15, 323.15, 328.15) K
with a view to investigating the zwitterion–ion, zwitterion–water dipole, ion–water dipole,
and ion–ion interactions operating in these systems.

2 Materials and Methods

The amino acids L-phenylalanine, L-leucine, L-glutamic acid and L-proline, and the salts
sodium chloride and sodium nitrate, were of high purity (>99 % by weight) and were pur-
chased from SRL (India) and E. Merck (India), respectively. The amino acids were recrys-
talyzed twice from ethanol + water mixtures, dried at 383.15 K and kept in vacuum des-
iccator over P2 O5 for at least 72 h before use. The salts were recrystalyzed twice from
triply-distilled water, dried at 423.15 K for at least 3 h, and then kept over P2 O5 in a vacuum
desiccator at room temperature for a minimum of 48 h prior to their use. Stock solutions of
2 mol · L−1 aqueous NaCl and 2 mol · L−1 aqueous NaNO3 were prepared in triply distilled
water and were used as solvents for the preparation of amino acid solutions. The correspond-
ing molal concentrations of 2 mol · L−1 NaCl and 2 mol · L−1 NaNO3 are 2.0874 mol · kg−1
and 2.1408 mol · kg−1 , respectively. The specific conductivity of the triply distilled water
used was less than 1.0 × 10−6 S · cm−1 . All of the solutions were stored in special airtight
bottles to avoid exposure of solutions to air and evaporation.
The density and speed of sound of L-glutamic acid in 2 mol · L−1 aqueous NaCl and
2 mol · L−1 aqueous NaNO3 solutions were measured using an oscillating-tube digital den-
simeter (Model DSA 5000M, Anton Paar, Austria) with a precision of (1 × 10−3 kg · m−3 )
and accuracy of (3 × 10−3 kg · m−3 ). The temperature of water around the densimeter cell
was controlled to within ±0.01 K. The densimeter was calibrated with pure water periodi-
cally.
1146 J Solution Chem (2012) 41:1144–1155

An ultrasonic interferometer (Mittal’s model: M-77, India) based on the variable-path

principle was used for measurement of the speed of sound at a frequency of 4 MHz at several
different temperatures using a method described elsewhere [20, 21] for other systems. Water
from an ultra-thermostat (Type U-10) was circulated through the brass jacket surrounding
the cell and the quartz crystal. The jacket was well insulated and the temperature of the
solution under study was maintained to an accuracy of ±0.01 ◦ C. An average of 10 readings
was taken as a final value of the speed of sound. The instrument was calibrated with the
triple-distilled water. The speed-of-sound values of water at different temperatures were
taken from the literature for calibration [22].
The densities of the solutions were measured with a pyknometer using a method de-
scribed elsewhere [20]. The densities of pure water at various required temperatures were
taken from the literature for the calibration [23, 24]. The thermostatted water bath used for
measurements of the speed of sound, and the thermostatted paraffin bath used for measure-
ments of densities, were maintained at a desired temperature (±0.01 ◦ C) for about 30 min
at each temperature of study, prior to recording of readings. Several very close readings of
density, determined at each temperature, were averaged. The uncertainties in speed of sound
and the density are within ±0.5 m · s−1 and ±0.0001 kg · m−3 , respectively, for amino acid
solutions measured with the pyknometer and ultrasonic interferometer.

3 Results and Discussion

The apparent molar volumes of the amino acids: L-phenylalanine (phe), L-leucine (leu),
L-glutamic acid (glu) and L-proline (pro), in 2 mol · L−1 aqueous NaCl and 2 mol · L−1
aqueous NaNO3 solutions, have been calculated by using the experimental density values of
solutions and solvent using the following equation:
 
ϕv = (M/ρ) − (ρ − ρo )/mρρo (1)

where m is the molality (mol · kg−1 ) of the solution, M is the relative molar mass of solute
(kg · mol−1 ), and ρo and ρ are the densities (kg · m−3 ) of the solvent and solution, respec-
tively. The density and speed of sound values are listed in Tables S1 and S2, respectively, of
the supplementary material. The apparent molar volume values were fitted to the following
equation by the least-square method:

ϕv = ϕvo + Sv m (2)
where ϕvo is the apparent molar volume at infinite dilution, which is also referred to as the
partial molar volume of the solute, and Sv is the volumetric pair-wise interaction coefficient
[25, 26].
The ϕvo and Sv values of the systems under investigation are presented in Table 1.
The observed and literature values of ϕvo of the studied amino acids in different sol-
vents are listed in Table 2 for the purpose of comparison. The ϕvo values are posi-
tive for 2 mol · L−1 aqueous NaCl and NaNO3 solutions at all temperatures. The par-
tial molar volumes of L-phenylalanine, L-leucine, L-glutamic acid and L-proline in
2 mol · L−1 aqueous of NaCl and NaNO3 solutions at each studied temperature are
higher than the corresponding values in aqueous medium. The higher ϕvo values of L-
phenylalanine, L-leucine, L-glutamic acid and L-proline in 2 mol · L−1 aqueous solutions
of NaCl and NaNO3 may be ascribed to: (1) ion–ion interactions between zwitterionic
groups (COO− , NH+ + − −
3 ) and the Na , Cl and NO3 ions; (2) hydrophilic–ion interactions
J Solution Chem (2012) 41:1144–1155 1147

Table 1 ϕvo and Sv values of amino acids at different temperatures

T (K) ϕvo × 106 Sv × 106 σ × 106

(m3 · mol−1 ) (m3 · mol−2 · kg) (m3 · mol−1 )

(i) L-Phenylalanine in 2.0 mol · L−1 aqueous NaCl solution

298.15 124.31 −108.55 3.94
303.15 124.34 −108.46 1.84
308.15 124.51 −194.39 6.70
313.15 125.01 −79.62 1.64
318.15 125.27 −95.84 2.36
323.15 125.30 −82.91 3.07
328.15 125.70 −54.97 2.88

(ii) L-Phenylalanine in 2.0 mol · L−1 aqueous NaNO3 solution

298.15 126.31 −111.87 6.80
303.15 126.41 −118.13 6.63
308.15 126.56 −124.44 6.25
313.15 126.77 −105.57 5.20
318.15 126.90 −135.06 6.86
323.15 127.22 −89.11 0.49
328.15 127.40 −46.06 0.47

(iii) L-Leucine in 2.0 mol · L−1 aqueous NaCl solution

298.15 108.41 −77.67 1.65
303.15 108.64 −70.31 0.96
308.15 108.68 −54.74 1.93
313.15 109.21 −28.24 0.35
318.15 109.38 −47.34 0.61
323.15 109.52 −13.09 1.53
328.15 109.60 −52.19 4.46

(iv) L-Leucine in 2.0 mol · L−1 aqueous NaNO3 solution

298.15 109.80 −39.79 1.09
303.15 109.90 −32.76 1.38
308.15 110.11 −32.17 1.27
313.15 110.23 1.01 2.94
318.15 110.42 −3.82 2.45
323.15 110.69 9.24 3.70
328.15 110.75 7.72 2.21

(v) L-Glutamic acid in 2.0 mol · L−1 aqueous NaCl solution

298.15 90.25 −39.88 1.80
303.15 91.34 −26.60 1.38
308.15 91.58 4.20 1.08
313.15 92.06 −1.47 0.56
318.15 92.37 −16.32 0.41
323.15 92.83 23.63 0.53
328.15 93.24 58.96 0.98
1148 J Solution Chem (2012) 41:1144–1155

Table 1 (Continued)

T (K) ϕvo × 106 Sv × 106 σ × 106

(m3 · mol−1 ) (m3 · mol−2 · kg) (m3 · mol−1 )

(vi) L-Glutamic acid in 2.0 mol · L−1 aqueous NaNO3 solution

298.15 104.47 −22.87 1.36
303.15 105.42 −34.57 1.20
308.15 106.97 −60.99 1.09
313.15 107.66 −66.37 0.87
318.15 108.62 −34.92 0.73
323.15 109.86 −97.39 0.72
328.15 110.35 −121.57 0.75

(vii) L-Proline in 2.0 mol · L−1 aqueous NaCl solution

298.15 85.64 −0.44 0.46
303.15 86.15 −0.56 0.46
308.15 86.54 −0.62 0.50
313.15 86.70 −0.54 0.50
318.15 86.70 −0.39 0.49
323.15 86.81 −0.13 0.58
328.15 86.88 0.18 0.81

(viii) L-Proline in 2.0 mol · L−1 aqueous NaNO3 solution

298.15 87.04 −0.63 0.33
303.15 87.24 −0.20 0.35
308.15 87.30 0.14 0.64
313.15 87.31 0.34 0.76
318.15 87.43 0.41 0.71
323.15 87.66 0.38 0.53
328.15 87.78 0.20 0.44

occurring between the hydrophilic groups of amino acids and the Na+ , Cl− and NO− 3 ions.
The observed ϕvo values vary as: pro < glu < leu < phe, and in the same order the solute-
solvent interactions increase in the solutions.
The hydration spheres of zwitterions will be affected by ions that strongly interact with
the charged centers of zwitterions. The electrostriction of water decreases and causes the
release of water molecules into the bulk solution leading to an increase in volume. Edsall
and Wymann [27] reported that smaller ions produce larger electrostriction of the solvent
because of stronger electrical fields near the ions, and hence cause increased orientation and
compression effects. They also reported that the amino group causes more electrostriction
than the carboxyl group. Thus, the strong interactions of NaCl and NaNO3 with various
amino acids in the studied systems results in an increased volume and the positive values of
ϕvo [28–37]. The increase in ϕvo with increasing temperature suggests release of some wa-
ter molecules from the loose solvation layers of the solutes occurs in solution [4, 38–41],
and hence results in a reduction in the electrostriction of water caused by these ions. Thus,
increasing temperature favors the process of releasing water molecules rather than binding
J Solution Chem (2012) 41:1144–1155 1149

to the charged end groups. The experimental slope, Sv is a measure of solute–solute inter-
actions. The trends of variation in both solvents (2 mol · L−1 aqueous NaCl and 2 mol · L−1
aqueous NaNO3 solutions) are irregular.

Table 2 Comparison of our observed partial molal volumes of amino acids in aqueous systems with literature
values at different temperatures

T (K) This work Literature values Ref.

Solvent ϕvo × 106 Solvent ϕvo × 106
(m3 · mol−1 ) (m3 · mol−1 )

L-Phenylalanine
298.15 2 mol · L−1 NaCl 124.31 Aqueous medium 121.48 [30–32]
2 mol · L−1 NaNO3 123.81 0.5 mol · kg−1 123.65 ± 0.05 [33]
Mg(CH3 COO)2
1.0 mol · kg−1 124.62 ± 0.05 [33]
Mg(CH3 COO)2
2 mol · L−1 122.58 ± 0.03 [35]
CH3 COONa
0.5 mol · kg−1 121.49 ± 0.04 [34]
glycerol
1.0 mol · kg−1 119.94 ± 0.03 [34]
glycerol
2.0 mol · kg−1 120.61 ± 0.04 [34]
glycerol
2.5 mol · kg−1 121.59 ± 0.03 [34]
glycerol
3.5 mol · kg−1 123.24 ± 0.03 [34]
glycerol
5.0 mol · kg−1 124.03 ± 0.01 [34]
glycerol
L-Leucine
298.15 2 mol · L−1 NaCl 109.80 Aqueous medium 108.97 [31]
2 mol · L−1 NaNO3 110.23 Aqueous medium 108.4 [8, 36, 37]
1.0 mol · kg−1 108.40 ± 0.38 [2]
NaCl
6.0 mol · kg−1 110.72 ± 0.11 [38]
guanidine
hydrochloride
2 mol · L−1 KCl 111.72 [20]
2 mol · L−1 113.13 [20]
KNO3
0.1 mol · kg−1 109.33 [36]
ZnCl2
0.5 mol · kg−1 111.7 [36]
ZnCl2
1.0 mol · kg−1 111.00 [36]
ZnCl2
1.5 mol · kg−1 111.91 [36]
ZnCl2
1150 J Solution Chem (2012) 41:1144–1155

Table 2 (Continued)

T (K) This work Literature values Ref.

Solvent ϕvo × 106 Solvent ϕvo × 106
(m3 · mol−1 ) (m3 · mol−1 )

L-Glutamic acid
298.15 2 mol · L−1 NaCl 93.14 Aqueous medium 85.88 [30, 32]
2 mol · L−1 NaNO3 104.47 Aqueous medium 89.0 [39]
Aqueous medium 90.06 [40]
1.0 mol · kg−1 94.15 ± 0.02 [41]
sodium acetate
1.0 mol · kg−1 95.24 ± 0.01 [41]
sodium
propionate
0.5 mol · kg−1 95.46 ± 0.01 [41]
sodium butyrate
1.0 mol · kg−1 93.76 ± 0.01 [42]
lithium acetate
dihydrate
1.0 mol · kg−1 95.08 ± 0.01 [42]
magnesium
acetate
tetrahydrate
1.0 mol · kg−1 94.57 ± 0.01 [42]
calcium acetate
2 mol · L−1 KCl 123.82 [21]
2 mol · L−1 KNO3 91.85 [21]

L-Proline
298.15 2 mol · L−1 NaCl 85.64 Aqueous medium 82.83 [30, 32, 43]
2 mol · L−1 NaNO3 87.04 2 mol · L−1 KCl 91.58 [37]
2 mol · L−1 KNO3 89.56 [37]
2 mol · L−1 LiCl 84.37 [7]
2 mol · L−1 NaCl 85.30 [7]

The apparent molar isentropic compressibilities, ϕk , have been calculated using the rela-
tion:
 
ϕk = (ks − ko )/mρo + ks ϕv (3)

where m is the molality of the solution (mol · kg−1 ), ρo is the density of the solvent
(kg · m−3 ), and the ks (= 1/(ρu2 )) and ko (= 1/(ρo u2o )) are the isentropic compressibili-
ties (m2 · N−1 ) of the solution and solvent, respectively. The values of ϕk have been fitted by
the least-squares method with the following equation:

ϕk = ϕko + Sk m (4)
where ϕko is the apparent molar isentropic compressibility at infinite dilution, which is also
referred to as the partial molar isentropic compressibility, and is a measure of solute–solvent
interactions. The experimental slope Sk represents solute–solute interactions in the solutions
J Solution Chem (2012) 41:1144–1155 1151

Table 3 ϕko and Sk values of amino acids at different temperatures

T (K) ϕko × 106 Sk × 106 σ × 106

(m3 · mol−1 ) (m3 · mol−2 · kg) (m3 · mol−1 )

(i) L-Phenylalanine in 2.0 mol · L−1 aqueous NaCl solution

298.15 −5.311 −13.00 3.95
303.15 −4.252 −85.64 9.64
308.15 −0.121 −117.86 5.58
313.15 −5.107 4.82 1.93
318.15 −5.073 −105.85 0.73
323.15 −8.607 38.81 2.16
328.15 −8.952 95.74 2.22

(ii) L-Phenylalanine in 2.0 mol · L−1 aqueous NaNO3 solution

298.15 −3.796 −96.38 4.69
303.15 −3.942 −127.65 3.35
308.15 3.629 −158.41 5.74
313.15 7.898 −185.40 3.53
318.15 −17.41 1.41 0.78
323.15 −5.297 −68.20 0.11
328.15 −8.601 −21.00 0.03

(iii) L-Leucine in 2.0 mol · L−1 aqueous NaCl solution

298.15 −2.815 1.58 0.12
303.15 −3.137 12.98 0.35
308.15 −3.407 21.29 0.61
313.15 −3.848 35.10 1.01
318.15 −3.666 28.38 0.81
323.15 −3.915 31.05 0.92
328.15 −3.304 21.60 0.42

(iv) L-Leucine in 2.0 mol · L−1 aqueous NaNO3 solution

298.15 −3.272 14.94 0.48
303.15 −3.144 16.54 0.32
308.15 −3.069 18.38 0.79
313.15 −3.866 24.49 0.71
318.15 −2.553 17.03 0.59
323.15 −2.387 18.62 0.26
328.15 −2.485 29.72 1.88

(v) L-Glutamic acid in 2.0 mol · L−1 aqueous NaCl solution

298.15 −3.083 11.47 0.12
303.15 −2.719 8.84 0.10
308.15 −2.386 8.23 0.20
313.15 −2.170 5.78 0.11
318.15 −2.135 4.24 0.15
323.15 −1.921 7.13 0.17
328.15 −1.863 10.43 0.21
1152 J Solution Chem (2012) 41:1144–1155

Table 3 (Continued)

T (K) ϕko × 106 Sk × 106 σ × 106

(m3 · mol−1 ) (m3 · mol−2 · kg) (m3 · mol−1 )

(vi) L-Glutamic acid in 2.0 mol · L−1 aqueous NaNO3 solution

298.15 −3.950 5.02 0.17
303.15 −3.561 13.93 0.18
308.15 −2.706 −1.35 0.07
313.15 −2.235 −3.06 0.08
318.15 −1.995 −1.01 0.09
323.15 −1.529 −5.24 0.06
328.15 −1.267 −6.31 0.07

(vii) L-Proline in 2.0 mol · L−1 aqueous NaCl solution

298.15 −2.746 0.91 1.12
303.15 −2.827 1.24 0.30
308.15 −2.026 1.52 0.25
313.15 2.671 −1.15 1.97
318.15 2.004 −0.27 1.27
323.15 2.423 −0.08 0.48
328.15 1.819 0.59 0.22

(viii) L-Proline in 2.0 mol · L−1 aqueous NaNO3 solution

298.15 −4.094 2.48 0.02
303.15 −2.407 2.11 0.32
308.15 −2.776 2.46 0.36
313.15 −2.821 2.39 0.33
318.15 −2.725 2.57 0.17
323.15 −2.560 2.83 0.08
328.15 −2.557 2.90 0.06

Table 4 The observed and literature values of the partial molal isentropic compressibilities of amino acids
in aqueous solutions at different temperatures

T (K) This work Literature values Ref.

Solvent ϕko × 1011 Solvent ϕko × 1011
(bar−1 · m3 · mol−1 ) (bar−1 · m3 · mol−1 )

L-Phenylalanine
298.15 2 mol · L−1 NaCl −5.311 Aqueous medium −3.454 [30, 31]
2 mol · L−1 NaNO3 −3.796 Aqueous medium −3.37 ± 0.5 [46]
0.5 mol · kg−1 −3.467 [44]
glycerol
1.0 mol · kg−1 −2.865 [45]
glycerol
2.0 mol · kg−1 −2.157 [45]
glycerol
3.5 mol · kg−1 −1.510 [45]
glycerol
5.0 mol · kg−1 −0.967 [45]
glycerol
J Solution Chem (2012) 41:1144–1155 1153

Table 4 (Continued)

T (K) This work Literature values Ref.

Solvent ϕko × 1011 Solvent ϕko × 1011
(bar−1 · m3 · mol−1 ) (bar−1 · m3 · mol−1 )

L-Leucine
298.15 2 mol · L−1 NaCl −2.815 Aqueous medium −3.178 [30]
2 mol · L−1 NaNO3 −3.272 Aqueous medium −3.05 [46]
Aqueous medium −3.03 [46]
2 mol · L−1 KCl −2.075 [20]
2 mol·KL−1 KNO3 −5.566 [20]
1.0 mol · kg−1 −2.618 [45]
glycerol
2.0 mol · kg−1 −2.037 [45]
glycerol
3.5 mol · kg−1 −1.564 [45]
glycerol
5.0 mol · kg−1 −0.937 [45]
glycerol
0.5 mol · kg−1 −3.216 [44]
glycerol
L-Glutamic acid
298.15 2 mol · L−1 NaCl −3.083 Aqueous medium −3.178 [30]
2 mol · L−1 NaNO3 −3.950 Aqueous medium −2.950 [46]
2 mol · L−1 KCl −0.888 [21]
2 mol · L−1 KNO3 −0.893 [21]

L-Proline
298.15 2 mol · L−1 NaCl −2.746 Aqueous medium 2.325 [30]
2 mol · L−1 NaNO3 −4.094 Aqueous medium −2.34 ± 0.4 [46]
2 mol · L−1 KCl −0.886 [20]
2 mol · L−1 KNO3 −0.777 [20]

[42, 43]. The ϕko and Sk values are listed in Table 3. The observed and literature values
of ϕko of the studied amino acids are listed in Table 4 for the purpose of comparison. The
negative values of the partial molar isentropic compressibilities of the investigated amino
acids in 2 mol · L−1 aqueous NaCl and 2 mol · L−1 aqueous NaNO3 indicate that the water
molecules around the charged ionic end groups of the amino acids are less compressible
than the water molecules in the bulk solution [44–46]. The ϕko values are negative in all of
the studied systems studied except for L-glutamic acid and L-proline in 2 mol · L−1 aqueous
NaCl solutions at 328.15 K. The large negative values of ϕko indicate strong structural effects
due to ion–solvent interactions. The values of Sk are both negative and positive, thus indi-
cating the presence of both ion–solute and solute–solute interactions in all of the systems
studied.

Acknowledgements The authors are thankful to the Chairman, Department of Chemistry for providing the
necessary facilities required in this research project. One of the authors (S.A.) thanks UGC for awarding the
UGC fellowship.
1154 J Solution Chem (2012) 41:1144–1155

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