J. Chem.

Thermodynamics 36 (2004) 281288

www.elsevier.com/locate/jct

Eect of sodium caproate on the volumetric and

viscometric properties of glycine, D L -a-alanine, and
D L -a-amino-n-butyric acid in aqueous solutions
Jianji Wang
a

a,*

, Zhenning Yan b, Jinsuo Lu

Department of Chemistry, Henan Normal University, Xinxiang, Henan 453002, PR China

Department of Chemistry, Zhengzhou University, Zhengzhou, Henan 450052, PR China

Received 18 December 2002; accepted 10 November 2003

Abstract
The apparent molar volumes (Vm;2 ) and relative viscosities (gr ) at T (298.15 and 308.15) K have been obtained for glycine, D L -aalanine, and D L -a-amino-n-butyric acid in aqueous sodium caproate solutions from measurements of density and the ow time. The


standard partial molar volumes (Vm;2
), standard volumes of transfer (Dt V
), the viscosity B-coecients, and the activation thermodynamic quantities (Dl
62 and DS2
6 ) of viscous ow have been calculated for the amino acids. It is shown that the standard partial molar
volumes, viscosity B-coecients, and activation free energies for viscous ow increase with increasing number of carbon atoms in the alkyl


chain of the amino acids. An increase in Vm;2
and Dt V
with increasing electrolyte concentrations have been explained due to the in

teractions of sodium caproate with the charged center of zwitterions for the amino acids. A comparison of the Vm;2
values for glycine, D L a-alanine, and D L -a-amino-n-butyric acid in dierent aqueous salts solutions showed that carboxylate ions have stronger interactions
with amino acid than chloride, thiocyanate, and nitrate ions. Results of viscosity are discussed in terms of changes in solvent structure.
2004 Elsevier Ltd. All rights reserved.
Keywords: Amino acids; Molar volume; Viscosity; Aqueous sodium caproate solutions

1. Introduction
Properties of amino acids in aqueous solutions have
been extensively studied in order to obtain a better understanding of solutesolvent interactions and their role
on the conformational stability of proteins. Salt solutions
have large eects on the structure and properties of proteins including their solubility, denaturation, dissociation
into subunits, and the activity of enzymes [1,2]. In the
literature there are some reports [314] on the eect of
various simple salts on the physico-chemical properties of
amino acids. However, there are only few studies about
properties of amino acids in (organic salt + water) [1519],
probably due to the complex nature of their interactions.
In continuation of our studies [1723] on the thermodynamic and transport properties for amino acids in
*

Corresponding author. Tel.: +86-373-3325996; fax: +86-3733326445.

E-mail address: Jwang@henannu.edu.cn (J. Wang).
0021-9614/$ - see front matter 2004 Elsevier Ltd. All rights reserved.
doi:10.1016/j.jct.2003.11.001

aqueous protein-denaturant solutions, a study of the

volumetric and viscometric properties for glycine, D L -aalanine, and D L -a-amino-n-butyric acid was carried out
in aqueous sodium caproate (NaC6 ), which is known to
inuence the dissociation of proteins in solutions [24].
Partial molar volumes and viscosity B-coecients for
glycine, D L -a-alanine, and D L -a-amino-n-butyric acid in
aqueous solutions of (0.5, 1.0, 1.5, and 2.2) mol  kg1
sodium caproate are reported at T (298.15 and 308.15)
K. The volumetric data have been compared with those
obtained in some aqueous sodium salts mixtures, and a
deeper insight into the dependence of partial molar
volumes has been suggested on nature of the salt.

2. Experimental
Glycine, D L -a-alanine, and D L -a-amino-n-butyric
acid (Shanghai Chem. Co., A. R.) were twice recrystallized from aqueous ethanol solutions and dried under

282

J. Wang et al. / J. Chem. Thermodynamics 36 (2004) 281288

vacuum at 348 K for 6 h. Then they were stored over

P2 O5 in a desiccator before use. Analytical reagent grade
sodium caproate (Shanghai Chem. Co.) was twice recrystallized from aqueous ethanol solutions and dried
under vacuum at 383 K for two days before use. Water
with a specic conductivity of 1.2 lX1  cm1 was obtained by distilling deionized water from alkaline
KMnO4 to remove any organic matter. All solutions
were prepared freshly by weighing on the molality scale.
The sample densities were measured to 3  106 g 
cm3 with an Anton Paar DMA 60/602 vibrating-tube
digital densimeter. Viscosity measurements were carried
out with a suspended level Ubbelhode viscometer, which
has an eux time of nearly 200 s for water at T 298:15
K. Flow time measurements are performed by a
SCHOTT AVS 310 photoelectric time unit with a resolution of 0.01 s. The viscometer was thermostated in a
SCHOTT thermostat which has a thermal stability of 5
mK. The temperature around the density meter cell was
controlled by circulating water from the same thermostat. The experimental details are given elsewhere [21].
The apparent molar volumes, Vm;2 , were calculated
from the equation
Vm;2 M=q  1000q  q0 =m  q0  q0 ;

where m is the molality of amino acid in solutions, M is

the molar mass of amino acid, q and q0 are the densities
of solution and the solvent, respectively.
The viscosity data were obtained from the relation
g C  q  t  Kq=t;

where C and K are the viscometer constants, which were

obtained by the measurements on water at T (298.15
and 308.15) K, and t is the eux time. The relative
viscosities gr g=g0 were calculated from the solution
and solvent viscosities.
3. Results
The values of density and apparent molar volume
at T (298.15 and 308.15) K are given in table 1. The
results can be tted by the equation


Vm;2 Vm;2
SV  m;


Vm;2

where
is the apparent molar volume of the amino
acids at innite dilution which has the same meaning as
the standard partial molar volume, and SV is an exper

imentally determined parameter. Values of Vm;2
have
been evaluated by weighted least-squares regression
analysis [25]. The standard partial molar volumes for the
amino acids in aqueous solutions of (0.5, 1.0, 1.5, and
2.2) mol  kg1 sodium caproate are presented in table 2
along with their standard deviations.
The standard volumes of transfer for the amino acids
from water to aqueous sodium caproate solutions were
calculated by

in aqueous NaC6  Vm;2
in water;
Dt V
Vm;2

Vm;2

where
(in water) values were taken from our earlier publication [26]. The results have been presented in
table 3
The viscosity data at T (298.15 and 308.15) K obtained for both solvent and solutions are reported in
table 4 as a function of amino acid concentrations. The
viscosity B-coecients for the amino acids in aqueous
sodium caproate solutions were calculated from the
following equation [27]:
gr g=g0 1 Bc;

where c is the molarity of amino acid in solutions. Viscosity B-coecients were obtained by the least-squares
method and are given in table 5 together with their
standard deviations.
On the basis of the Feakins transition-state theory
[28], the contribution per mole of solute to the free energy of activation for viscous ow of the solution, Dl
62 ,
can be calculated by






Dl
62 Dl
61 RT =Vm;1
f1000B  Vm;1
 Vm;2
g;

where Vm;1
is the standard partial molar volume of solvent, and Dl
61 is the free energy of activation per mole
of pure solvent, which is given by


Dl
61 RT lng0 Vm;1
=hNA ;

where h is the Planck constant, NA is Avagadros

number.

4. Discussion


Data in table 2 showed that Vm;2
increase with increasing concentration of sodium caproate at a given
temperature. At neutral pH, amino acids exist as zwitterions and on dissolution in water there is an overall
decrease in the volume of the water. This is due to the
contraction of water near the end group of amino acids,
and is termed as electrostriction. The dissociation of
amino acids in the presence of sodium caproate leads to
the formation of physically bonded ion-pairs between
the charged groups of amino acids and sodium and
caproate ions produced from the dissociation of sodium
caproate. The formation of the ion-pairs reduces the
electrostriction and some of the previously electrostricted water molecules around these charged centers of
amino acids return to their normal structure due to the
hydration cosphere overlap eect. The same result can
also be obtained from the standard volumes of transfer
for the amino acids. As seen from table 3, Dt V
values
from water to aqueous sodium caproate are positive and
increase with increasing concentration of sodium caproate. These suggest that sodium caproate at higher
concentrations has a larger dehydration eect on the

J. Wang et al. / J. Chem. Thermodynamics 36 (2004) 281288

283

TABLE 1
Solution densities q and apparent molar volumes Vm;2 for the a-amino acids in aqueous sodium caproate solutions as a function of molalities of
amino acids (ma ) and sodium caproate (ms ) at T (298.15 and 308.15) K
ma /(mol  kg1 )

q/(g cm3 )
298.15 K

308.15 K

ma /(mol  kg1 )

Vm;2 /(cm3  mol1 )

298.15 K

308.15 K

q/(g cm3 )
298.15 K

308.15 K

Vm;2 /(cm3  mol1 )

298.15 K

308.15 K

Glycine
0.0000
0.03517
0.06782
0.1028
0.1553
0.2099
0.2565
0.3031
0.3675
0.4073

ms 0:5000 mol  kg1

1.014396
1.010739
1.015440
1.011771
45.13
1.016426
1.012719
44.83
1.017463
1.013746
44.89
1.018990
1.015286
45.06
1.020582
1.016843
45.09
1.021932
1.018196
45.12
1.023294
1.019521
45.08
1.025148
1.021324
45.09
1.026285
1.022465
45.11

0.0000
0.03431
0.06595
0.09989
0.1514
0.2002
0.2524
0.3010
0.3507
0.3999

ms 1:5000 mol  kg1

1.041883
1.036699
1.042764
1.037593
48.37
1.043578
1.038406
48.30
1.044443
1.039290
48.33
1.045768
1.040622
48.24
1.047047
1.041867
48.06
1.048389
1.043205
48.01
1.049592
1.044409
48.10
1.050911
1.045713
47.92
1.052156
1.046944
47.91

0.03490
0.06650
0.1015
0.1552
0.2055
0.2534
0.3019
0.3603
0.4077

ms 0:5000 mol  kg1

1.015339
1.011660
61.52
1.016191
1.012495
61.48
1.017124
1.013418
61.55
1.018548
1.014813
61.58
1.019877
1.016130
61.57
1.021136
1.017361
61.57
1.022372
1.018579
61.67
1.023897
1.020096
61.63
1.025104
1.021283
61.65

62.27
62.18
62.14
62.20
62.13
62.15
62.24
62.15
62.18

0.03484
0.06535
0.09970
0.1486
0.2004
0.2483
0.2967
0.3478
0.4000

ms 1:0000 mol  kg1

1.030289
1.025836
62.74
1.031055
1.026600
62.72
1.031910
1.027452
62.75
1.033129
1.028675
62.72
1.034401
1.029933
62.75
1.035573
1.031114
62.76
1.036747
1.032274
62.77
1.037977
1.033482
62.79
1.039229
1.034748
62.79

63.00
62.98
63.00
62.92
63.01
62.96
63.02
63.08
63.03

0.03488
0.06655
0.1005
0.1502
0.1983
0.2460
0.3131
0.3544
0.4101

ms 1:5000 mol  kg1

1.042679
1.037498
64.43
1.043406
1.038222
64.33
1.044188
1.038994
64.24
1.045337
1.040129
64.12
1.046418
1.041218
64.17
1.047506
1.042292
64.11
1.049023
1.043807
64.06
1.049960
1.044731
64.02
1.051191
1.045956
64.03

64.57
64.54
64.54
64.48
64.45
64.44
64.38
64.35
64.36

0.03411
0.06492
0.09897
0.1548
0.2004
0.2502
0.3152
0.3738
0.4216

ms 2:1773 mol  kg1

1.054911
1.049390
66.34
1.055534
1.050006
66.26
1.056217
1.050686
66.26
1.057381
1.051808
65.95
1.058333
1.052775
65.80
1.059385
1.053809
65.62
1.060743
1.055156
65.49
1.019683
1.056374
65.38
1.062947
1.057354
65.35

66.97
66.82
66.74
66.60
66.39
66.13
66.97
65.85
65.78

0.03472
0.06637
0.1014
0.1521
0.2017
0.2521
0.3061
0.3541
0.4020

ms 0:5000 mol  kg1

1.015298
1.011625
76.35
1.016116
1.012422
76.35
1.017011
1.013317
76.40
1.018308
1.014566
76.36
1.019571
1.015819
76.33
1.020823
1.017055
76.40
1.022127
1.018350
76.53
1.023307
1.019496
76.53
1.024469
1.020646
76.55

ms 1:0000 mol  kg1

1.030239
1.025788
77.39
1.030975
1.026519
77.45
1.031803
1.027339
77.41
1.032967
1.028487
77.41
1.034161
1.029656
77.33
1.035351
1.030839
77.42
1.036487
1.031957
77.48
1.037643
1.033074
77.47
1.038680
1.034107
77.49

77.67
77.78
77.78
77.84
77.84
77.90
77.98
78.04
78.04

45.50
45.61
45.51
45.41
45.53
45.48
45.51
45.60
45.56

48.11
48.25
48.15
48.12
48.15
48.13
48.22
48.08
48.10

0.0000
0.03431
0.06581
0.1003
0.1494
0.2011
0.2522
0.3011
0.3533
0.3983

ms 1:0000 mol  kg1

1.029412
1.024963
1.030372
1.025925
46.49
1.031252
1.026805
46.46
1.032208
1.027769
46.49
1.033567
1.029116
46.50
1.035024
1.030559
46.34
1.036402
1.031959
46.45
1.037744
1.033250
46.44
1.039166
1.034689
46.43
1.040405
1.035913
46.39

46.51
46.52
46.47
46.60
46.50
46.52
46.66
46.59
46.58

0.0000
0.03402
0.06531
0.09998
0.1542
0.2007
0.2495
0.3235
0.3738
0.4328

ms 2:1773 mol  kg1

1.054224
1.048717
1.055022
1.049516
50.07
1.055760
1.050251
49.98
1.056583
1.051067
49.87
1.057857
1.052354
49.83
1.058980
1.053456
49.66
1.060175
1.054675
49.47
1.061962
1.056375
49.32
1.063176
1.057609
49.24
1.064604
1.059027
49.15

50.20
50.15
50.10
49.96
49.89
49.59
49.69
49.53
49.44

D L -a-alanine

D L -a-aminobutyric

76.98
77.07
76.94
77.10
76.98
77.02
77.10
77.15
77.15

acid

0.03434
0.06524
0.09988
0.1491
0.1993
0.2512
0.3013
0.3517
0.3979

284

J. Wang et al. / J. Chem. Thermodynamics 36 (2004) 281288

TABLE 1 (continued)
ma /(mol  kg1 )

q/(g cm3 )
298.15 K

0.03454
0.06618
0.1007
0.1491
0.2004
0.2502
0.3089
0.3603
0.4121

Vm;2 /(cm3  mol1 )

308.15 K

ms 1:5000 mol  kg
1.042629
1.037452
1.043306
1.038133
1.044047
1.038880
1.045079
1.039893
1.046146
1.040962
1.047190
1.041971
1.048418
1.043156
1.049486
1.044228
1.050526
1.045233

298.15 K

ma /(mol  kg1 )

308.15 K

q/(g cm3 )
298.15 K

1

Vm;2 /(cm3  mol1 )

308.15 K

298.15 K

308.15 K

80.93
80.98
80.96
80.79
80.62
80.77
80.61
80.54
80.50

81.82
81.77
81.68
81.62
81.52
81.33
81.28
81.17
81.10

1

79.01
79.06
79.03
78.99
79.05
79.04
78.99
78.96
79.00

79.12
79.20
79.16
79.29.
79.35
79.46
79.52
79.45
79.54

0.03491
0.06636
0.1009
0.1538
0.2054
0.2529
0.3261
0.3763
0.4286

ms 2:1773 mol  kg
1.054877
1.049349
1.055459
1.049919
1.056098
1.050549
1.057096
1.051507
1.058083
1.052450
1.058914
1.053347
1.060293
1.054667
1.061223
1.055599
1.062181
1.056552

TABLE 2
Standard partial molar volumes for the amino acids in aqueous sodium caproate solutions at T (298.15 and 308.15) K


/(cm3  mol1 )
Vm;2

Amino acids
1

ms 1:5 mol  kg1

ms 2:2 mol  kg1

T 298:15 K
46.48  0.03
62.71  0.01
77.32  0.04

48.35  0.04
64.26  0.06
79.06  0.02

50.07  0.04
66.25  0.08
80.97  0.05

T 308:15 K
46.51  0.03
62.92  0.03
77.69  0.02

48.19  0.09
64.55  0.01
79.20  0.05

50.19  0.06
66.92  0.08
81.84  0.03

ms 0:5 mol  kg

ms 1:0 mol  kg

Glycine
Alanine
Aminobutyric acid

45.00  0.07
61.50  0.02
76.24  0.04

Glycine
Alanine
Aminobutyric acid

45.41  0.05
62.18  0.05
76.91  0.05

1

TABLE 3
Standard volumes of transfer for the amino acids from water to aqueous sodium caproate solutions at T (298.15 and 308.15) K
Dt V /(cm3  mol1 )

Amino acids
ms 0:5 mol  kg1

ms 1:0 mol  kg1

ms 1:5 mol  kg1

ms 2:2 mol  kg1

Glycine
Alanine
Aminobutyric acid

1.52  0.07
0.83  0.04
0.55  0.13

T 298:15 K
3.00  0.04
2.04  0.04
1.04  0.13

4.87  0.04
3.59  0.07
1.44  0.13

6.59  0.04
5.58  0.09
2.32  0.14

Glycine
Alanine
Aminobutyric acid

1.21  0.08
0.85  0.06
0.48  0.10

T 308:15 K
2.31  0.05
1.59  0.05
1.40  0.08

3.99  0.11
3.22  0.04
1.84  0.07

5.99  0.08
5.57  0.09
3.34  0.08

amino acids in solutions. A similar conclusion has been

reported for some amino acids in aqueous NaCl [10],
NH4 Cl [14], KCl [10], Na2 SO4 [29], and NaNO3 [30]
solutions.
It is found that introduction of a methyl group in
glycine introduces hydrophobic hydrations in D L -alanine. In the case of overlaping of the hydration cosphere
of sodium or caproate ions with that of D L -alanine,
some of the water molecules are also released from the
cosphere of the side chain of the amino acid, making a
negative contribution to Dt V
. This gives rise to a decrease in the Dt V
against glycine. Among the amino
acids studied, D L -a-aminobutyric acid has the longest

hydrophobic chain, so the smallest Dt V
values have

been found for this amino acid. This also indicates that
more hydrophobic amino acids undergo more dehydration eect of sodium caproate. It should be noted
that in spite of the existence of ionhydrophobic group
interactions, the values of Dt V
are positive for the
amino acids studied. This suggests that interactions between ion and the end group of the amino acids are
stronger than those between ion and hydrophobic group
of the amino acids.


It can be seen from gure 1 that values of Vm;2
increase linearly with increasing number of carbon atoms
(nc ) in the alkyl chain for the amino acids in the presence

J. Wang et al. / J. Chem. Thermodynamics 36 (2004) 281288

285

TABLE 4
Viscosities g for (amino acids + sodium caproate + water) systems as a function of concentrations of amino acids (c) and sodium caproate (ms ) at
T (298.15 and 308.15) K
ms 0:5000 mol  kg1
g

c
3

(mol  dm )

(mPa  S)

ms 1:0000 mol  kg1

g

c
3

ms 1:5000 mol  kg1

g

c
3

(mol  dm )

ms 2:1773 mol  kg1

g

c
3

(mol  dm )

(mPa  S)

(mPa  S)

(mol  dm )

(mPa  S)

2.102
2.113
2.123
2.135
2.152
2.169
2.187

0.0000
0.03580
0.06861
0.1048
0.1613
0.2093
0.2596

3.187
3.210
3.227
3.246
3.282
3.303
3.350

2.122
2.140
2.160
2.190
2.219
2.250

0.03587
0.06813
0.1036
0.1614
0.2084
0.2592

3.215
3.247
3.279
3.334
3.380
3.431

acid (T 298:15 K)
0.03589
2.128
0.06857
2.153
0.1041
2.180
0.1535
2.219
0.2054
2.262
0.2554
2.302

0.03670
0.06957
0.1055
0.1600
0.2129
0.2610

3.228
3.269
3.314
3.387
3.453
3.518

0.0000
0.03562
0.06859
0.1038
0.1565
0.2109
0.2572

1.212
1.217
1.222
1.229
1.238
1.248
1.256

0.0000
0.03526
0.06754
0.1027
0.1527
0.2051
0.2565

Glycine (T 298:15 K)
1.607
0.0000
1.614
0.03568
1.622
0.06848
1.629
0.1036
1.641
0.1566
1.653
0.2065
1.666
0.2597

0.03533
0.06717
0.1023
0.1559
0.2058
0.2530

1.222
1.232
1.243
1.260
1.276
1.292

0.03578
0.06699
0.1020
0.1515
0.2037
0.1516

D L -a-alanine (T 298:15 K)
1.621
0.03626
1.634
0.06902
1.648
0.1040
1.670
0.1550
1.692
0.2039
1.714
0.2522

0.03513
0.06698
0.1021
0.1524
0.2014
0.2508

1.225
1.239
1.255
1.277
1.299
1.322

0.03525
0.06681
0.1020
0.1517
0.2020
0.2535

1.626
1.644
1.664
1.692
1.723
1.754

0.0000
0.03549
0.06834
0.1034
0.1559
0.2101
0.2562

0.956
0.961
0.965
0.970
0.977
0.986
0.992

0.0000
0.03511
0.06724
0.1023
0.1521
0.2042
0.2554

Glycine (T 308:15 K)
1.240
0.0000
1.246
0.03551
1.252
0.06814
1.259
0.1030
1.268
0.1558
1.278
0.2055
1.287
0.2585

1.601
1.612
1.620
1.629
1.644
1.657
1.671

0.0000
0.03561
0.06825
0.1043
0.1604
0.2082
0.2583

2.402
2.418
2.432
2.448
2.472
2.493
2.515

0.03520
0.06693
0.1020
0.1553
0.2050
0.2521

0.964
0.972
0.980
0.993
1.005
1.017

0.03563
0.06670
0.1015
0.1509
0.2028
0.2549

D L -a-alanine (T 308:15 K)
1.252
0.03607
1.261
0.06868
1.272
0.1035
1.287
0.1542
1.304
0.2029
1.320
0.2510

1.617
1.631
1.646
1.667
1.688
1.711

0.03568
0.06777
0.1031
0.1606
0.2073
02579

2.425
2.449
2.472
2.511
2.544
2.580

0.3500
0.6674
0.1017
0.1519
0.2007
0.2499

0.9665
0.9767
0.9882
1.005
1.021
1.037

0.03510
0.06652
0.1016
0.1510
0.2011
0.2524

acid (T 308:15 K)
0.03571
1.622
0.06823
1.640
0.1036
1.660
0.1527
1.687
0.2044
1.718
0.2542
1.747

0.03650
0.06920
0.1049
0.1592
0.2117
0.2596

2.437
2.463
2.496
2.547
2.592
2.637

D L -a-aminobutyric

D L -a-aminobutyric

1.254
1.268
1.282
1.303
1.325
1.347

of sodium caproate. The slopes of the straight lines,

which are the volume contributions by the CH2 group of
the amino acids, are independent of the molalities of
sodium caproate, and also not sensitive to temperature.
They are found to be 15.4 and 15.5 cm3  mol1 at
T (298.15 and 308.15) K, respectively. These are almost the same values as those reported for amino acids

in water [26]. On the other hand, the intercepts of the

straight lines, which are the volume contributions by the
end groups of the amino acids, increase with increasing
sodium caproate concentrations. These results also
suggest that the interactions between the end group of
the amino acids and sodium caproate are the main


contribution to Vm;2
values of amino acids.

286

J. Wang et al. / J. Chem. Thermodynamics 36 (2004) 281288

TABLE 5
Viscosity B-coecients for the amino acids in aqueous sodium caproate solutions at T (298.15 and 308.15) K
B/(dm3  mol1 )

Amino acid
ms 1:0 mol  kg1

ms 1:5 mol  kg1

ms 2:2 mol  kg1

Glycine
Alanine
Aminobutyric acid

0.140  0.001
0.260  0.002
0.357  0.003

T 298:15 K
0.142  0.001
0.262  0.002
0.358  0.003

0.155  0.001
0.274  0.002
0.369  0.003

0.169  0.006
0.290  0.003
0.392  0.003

Glycine
Alanine
Aminobutyric acid

0.145  0.002
0.248  0.002
0.336  0.003

T 308:15 K
0.150  0.001
0.257  0.001
0.341  0.001

0.169  0.001
0.270  0.001
0.355  0.001

0.182  0.001
0.285  0.001
0.376  0.002

100

90

90

80

80

V m,2 /cm mol

-1

100

70

50
40

70
60
50
40

30

30
0

(a)

caused by the NH
3 of the amino acids will be largely
reduced, which results in a larger increase in volume.


The values of Vm;2
for the amino acids in aqueous
NaNO3 [30], NaCl [10], KCl [10], and KSCN [12] together with those in NaC2 [20,22] and NaC4 [21,23]
solutions are given in table 6. It can be seen that the


trend of Vm;2
for the amino acids at given temperature
and the same salt concentration follows the order:

60

V m,2 /cm mol

-1

ms 0:5 mol  kg1

nc

(b)

nc

FIGURE 1. The linear relationship between Vm;2

and nC in aqueous
sodium caproate solutions at 298.15 K (a) and 308.15 K (b): (r) 0.5
mol  kg1 ; (j) 1.0 mol  kg1 ; (N) 1.5 mol  kg1 ; (d) 2.2 mol  kg1 .

From the comparison of Vm;2
and Dt V
values for the
amino acids in aqueous sodium acetate (NaC2 ) [20,22],
sodium butyrate (NaC4 ) [21,23], and sodium caproate
(NaC6 ) solutions, it is found that these volumetric
properties increase with increasing side chain length of
the carboxylate anion. In the ternary (amino acid + sodium carboxylate + water), two types of interactions
may be occurring: (a) ionion interactions between Na
and the COO group of the amino acids and those between carboxylate ion and the NH
3 group of the amino
acids; (b) ionnonpolar group interactions. Because the
interaction of the Na for dierent sodium carboxylates
with a given amino acid is the same, it can be deduced


that the increased Vm;2
and Dt V
come from the dierence in interactions of carboxylate ion with NH
3 group
and side chain of the amino acids. According to Ide
et al. [31], hydration shells of ammonium and carboxylate groups overlap that of side chains of amino acids.
The carboxylate anions of salts interact mainly with the
charged groups of amino acids. In other words, ionion
interaction predominates that of the ion-side chains of
amino acids. So the dierence in volumetric properties
observed above mainly comes from the dierence in
interaction (a). Caporate ion has a bigger hydrophobic
hydration sphere and a large destructive eect on the
hydration sphere of NH
3 of the amino acids than butyrate and acetate ions. The electrostriction of water

CH3 CH2 4 COO > CH3 CH2 2 COO >

CH3 COO > Cl > NO
3;

and Cl > SCN , respectively.

Because there is a small dierence in Vm;2
values for
the amino acids in aqueous NaCl and in aqueous KCl
solutions (see table 6), it can be concluded that eect of
Na is close to that of K . Based on this observation


and on the fact that there is a large dierence for Vm;2
of
the amino acids in aqueous NaNO3 and in aqueous
KSCN solutions, it can be seen that the order for interaction between the anion and the amino acid is
CH3 CH2 4 COO > CH3 CH2 2 COO >
CH3 COO > Cl > SCN >
NO
9
3:
This order is consistent with that of the hydration ability
of these anions [32,33]. Robinson and Jencks [34] studied the eect of a number of salt solutions on the activity
coecient of acetyltetraglycine ethyl ester (ATGEE),
which is a model compound for the peptide and proteins. From their salting-out constants, the order of
salting-out eect CH3 COO > Cl > SCN > NO
3 was
obtained. These indicated that the dehydration eect of
ions on amino acids is one of the important reasons for
the salting-out of amino acids. In fact, sodium nitrate
has a salting-in eect on amino acids [35].
It can be seen from table 5 that B-coecients of
amino acids increase with increasing concentration of
NaC6 , indicating the promotion of liquid structure in
the presence of NaC6 . At any given temperature, B-coecients are found to increase with increasing size of the
amino acids. It is well established that B-coecients is

J. Wang et al. / J. Chem. Thermodynamics 36 (2004) 281288

287

TABLE 6


Standard partial molar volumes, Vm;2
(cm3  mol1 ), for the amino acids in aqueous salt solutions at T (298.15 and 308.15) K
Salt

NaNO3
NaCl
KCl
KSCN
NaC2
NaC4

Molality/(mol  kg1 )

1
2
1
2
1
2
1
1.0
2.0
1.0
2.0

D L -a-Alanine

Glycine
298.15 K

308.15 K

25.95
25.71
45.05
46.24
44.89
46.12
44.63
45.50
47.05
45.96
48.17

31.25
29.93

45.16
45.92
47.40
46.15
48.56

directly dependent on the size, shape and charge of the

solute molecules. Since the charged groups for the
amino acids studied here are the same, the order of
viscosity B-coecients may just be explained in terms of
the shape and size of alkyl group of amino acids. Considering the fact that the alkyl group is the longest in
aminobutyric acid, shorter in alanine and the smallest in
glycine, the order of B-coecients observed here is quite
reasonable.
B-coecients can provide direct evidence regarding
their structural eects in solutions. However, dB/dT is a
better criterion for determining the solute eect on
structure of solutions compared with B-coecients [36].
The positive dB/dT value for glycine and negative dB/dT
for D L -alanine and D L -aminobutyric acid, respectively,
in the aqueous salt solutions point out that glycine is
structure-breaker, while alanine and aminobutyric acid
are structure-makers. The same conclusion has been
obtained in acetonitrile by Dey and Saikia [15] and in
aqueous sodium acetate solutions by us [37]. However,
negative dB/dT values have been reported for glycine,
D L -alanine, and D L -aminobutyric acid in aqueous guanidine hydrochloride [18] and glycine and D L -alanine in
aqueous potassium thiocyanate [12] solutions. It seems

298.15 K

308.15 K

62.08
63.19
61.97
63.14
61.86
62.13
63.43
62.44
63.78

D L -a-Aminobutyric

298.15 K

acid

308.15 K

76.30

62.29
62.68
63.79
62.74
64.77

76.79
77.95
76.78
78.06

77.49
78.17
77.54
79.57

reasonable to state that sign of dB/dT for amino acid

might vary under dierent experimental conditions.
Free energy of activation of viscous ow (Dl
62 ) is
another useful parameter to assess the complexity of liquid structure. The data given in table 7 show that Dl
62
values increase with increasing sodium caproate concentrations, again suggesting enhancement of liquid
structure by sodium caproate. On the other hand, Dl
62
increase gradually from glycine to aminobutyric acid.
Because the interactions of the charged end groups for
dierent amino acids with sodium caproate and water are
the same, the increasing Dl
62 comes from the dierence
in interactions of the alkyl groups of the amino acids with
sodium caproate and water molecules in the aqueous salt
solutions. The interaction between amino acids and water is known to increase with the size of the nonpolar part
of the amino acid molecules [38]. The studies on the interaction between amino acids and electrolytes [10,20,22]
showed that more hydrophobic amino acids undergo
more dehydration eect of electrolyte. Therefore, the
interactions of the alkyl groups with sodium caproate
and water molecules increase with increasing alkyl chains
length of the amino acids, and values of Dl
62 increase
gradually from glycine to aminobutyric acid.

TABLE 7
Activation free energies, Dl
62 (kJ  mol1 ), for viscous ow of the amino acids in aqueous sodium caproate solutions at T (298.15 and 308.15) K
Dl
62 /(kJ  mol1 )

Amino acid
ms 0:5 mol  kg1

ms 1:0 mol  kg1

ms 1:5 mol  kg1

ms 2:2 mol  kg1

Glycine
Alanine
Aminobutyric acid

31.9  0.1
49.9  0.3
64.7  0.4

T 298:15 K
32.2  0.1
49.5  0.3
63.5  0.4

33.9  0.1
50.4  0.2
63.8  0.4

35.7  0.7
51.5  0.3
65.1  0.3

Glycine
Alanine
Aminobutyric acid

33.1  0.3
49.3  0.3
63.3  0.4

T 308:15 K
33.57  0.07
49.7  0.1
62.6  0.1

35.9  0.1
50.7  0.1
63.2  0.1

37.60  0.01
51.9  0.1
64.5  0.2

288

J. Wang et al. / J. Chem. Thermodynamics 36 (2004) 281288

TABLE 8
Activation entropy, DS2
6 (kJ  mol1  K1 ), for viscous ow of the amino acids in aqueous sodium caproate solutions
DS2
6 /(kJ  mol1  K1 )

Amino acid

Glycine
Alanine
Aminobutyric acid

ms 0:5 mol  kg1

ms 1:0 mol  kg1

ms 1:5 mol  kg1

ms 2:2 mol  kg1

)0.12
0.06
0.14

)0.14
)0.02
0.09

)0.20
)0.03
0.06

)0.19
)0.04
0.06

From the values of Dl
62 at T (298.15 and 308.15)

K, entropies of activation DS2
6 (T 303:15 K) of viscous ow were calculated by
DS2
6 T 303:15 K  fDl
62 T 308:15 K 
Dl
62 T 298:15 Kg=10:
10
Entropies of activation of viscous ow thus calculated
are negative for glycine and alanine (table 8), indicating
that the formation of the transition state for these amino
acids in aqueous NaC6 solutions is associated with bond
making and an increase in order. This suggests that the
ground state is somewhere in the disordered region.
Small magnitude of DS2
6 (T 303:15 K) for alanine
suggests weak bond making tendency in transition state
in comparison to glycine. The positive DS2
6 (T 303:15
K) values for aminobutyric acid indicates that the formation of the transition state in aqueous sodium caproate solutions are associated with the solutesolvent
bonds breaking.
Acknowledgements
We acknowledge the nancial support from the
Youth Science Foundation of Henan Province and the
Nature Science Foundation of the Education Commission of Henan Province (20021500005).
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