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International Journal of Advance Engineering and Research

Development
Volume 2,Issue 6, June -2015

PARTIAL MOLAR VOLUME AND PARTIAL MOLAR COMPRESSIBILITY

OF HOMOLOGOUS AMINO ACIDS IN AQUEOUS XYLOSE SOLUTIONS
AT DIFFERENT TEMPERATURES.
K.Rajagopal 1 and J.Johnson 2
1
Dept. of Physics, Government College of Engineering, Tirunelveli, Tamilnadu, India
2
Dept. of Physics, Research scholar, M. S. University, Tirunelveli, Tamil Nadu, India

Abstract —Values of density(ρ)and ultrasonic speed(u) have been determined for four amino acids (glycine, L-alanine,
L-valine and L-leucine) in aqueous xylose solutions ( 0.05, 0.10, 0.15, 0.20 ) M at T = (298.15, 303.15, 308.15, 313.15 )
K. Apparent molar volume (Vφ), partial molar volumes (Vφ 0), transfer volumes (ΔVφ0)and Hepler’s constant (∂2 Vφ 0 /∂T2 ).
are evaluated using density data. Apparent molar compressibility (Kφ) and partial molar compressibility (Kφ0 ) have been
calculated using ultrasonic speed data. The hydration numbers n H have been evaluated from both volumetric and
compressibility data. Our study concludes the existence of strong solute solvent interaction in the reported systems.
Furthermore, using Hepler’s criteria, it has been shown that glycine and alanine behave as structure maker while valine
and leucine acts as a structure breaker in aqueous xylose solutions.

Keywords- Amino acids, xylose, apparent molar volume, apparent molar compressibility, hydration number.
I.INTRODUCTION

The interaction of protein with water in aqueous solution is an important factor for maintain ing the native confirmation of
proteins. Consequently the characterizat ion of thermodynamic properties of protein hydration can assist in understanding
the conformational stability and unfolding behavior of globular proteins. Since proteins are particularly co mp lex
mo lecules, it is difficu lt to separate the various interactions which participate in protein hydration. Fo r a better
understanding of the hydration behavior of proteins, one useful app roach is to investigate the low mo lecular weight
model co mpounds that contain atomic groups such as amino acid side change and the peptide group of proteins. Amino
acids have been widely used as model co mpound because they represent the fundamental substan ces for building
proteins.[1 – 4]. Further, amino acids differ fro m each other in size, charge, hydrogen bonding capacity, h ydrophobicity
and chemical reactiv ity. Hence these side changes contribute to the structure and function of proteins individually an d
collectively [5]. It has been reported in the literature that the presence of co solutes like carbohydrates/ saccharides,
polyhydroxy alcohols, non electrolytes such as urea and surfactants decrease the denaturation ability of certain proteins
[6.7].Carbohydrates can give a better insight into the effect of electrostatic and hydrophobic interactions on the stabilities
of proteins as carbohydrates are known to influence macro molecules confirmat ions by weaking attraction or repulsion of
inter and intra charge – charge interactions and by affecting hydrophobic interactions through the side chain of the alkyl
group. In addition, carbohydrates are very important to biological systems. They are not only the main energy source
needed for maintain ing biologically activity but also the basic material to form major b iologically active substance such
as NAD, FAD, DNA, RNA and ATP[8]. So me reports are available in literature about the interaction studies of aminbo
acids in aqueous in saccharide solutions. For examp le, Nain etal have studied the volumetric, u ltrasonic and viscometric
behaviour of L-Histidine in aqueous glucose solutions volumetric and visco metric behaviour of l-arg inine + d-xy lose/ l-
arabinose + water solutions at different temperatures and [9, 10],, Pal et al have reported the density , viscosity and speed
of sound of diglycine in aqueous xylose, L(-) arbinose and D (-) ribose solutions [11]; in aqueous glucose, galactose and
fructose solutions [12]; of L – alanine in aqueous fructose, maltose and lactose solutions [13] and the density of L-alan ine
and L-valine in aqueous sucrose solutions[14]. As the protein carbohydrate interactions are important for immunology,
biosynthesis, pharmacology, medicine and cos metic Industry [15, 16], in continuation of our work on ternary systems
comprising amino acids in aqueous saccharides, drugs and electrolytes solutions [17-24], we are report ing for the first
time in literature, the volumetric and compressibility studies of homologous amino acids in aqueous xylose solutions at
four different temperatures. In the present paper, we report the densities, ρ, and ultrasonic speeds, u, of solutions of
Some ho mologous amino acids in water and in aqueous xy lose solvents (0.05, 0.10, 0.15, 0.20 )M at 298.15, 303.15,
308.15 and 313.15 K. These experimental data have been used to calculate the apparent molar volu me, Vφ , limit ing
apparent molar volu me, Vφ 0 , transfer volu me, ΔVφ 0 , Hep ler’s constant, ∂2 Vφ 0 /∂T2 , apparent molar co mpressibility, Kφ ,
limit ing apparent molar co mpres sibility, Kφ 0 , and hydration numbers.. These parameters have been used to discuss the
solute–solute, solute–solvent interactions, structure making and structure breaking ability in these systems.

II.EXPERIMENTAL
Xylose (mass fraction purity > 0.990) was procured fro m S.D. Fine. Chem. Ltd. Mu mbai, glycine ( 99.7% assay ), are
procured fro m Merck Ltd. Mu mbai, L-valine (99% assay) and L-leucine (+99 % assay) are obtained fro m A LDRICH
(U.S.A) . L-alanine (99% assay) is procured fro m SISCO, Mu mbai. The a mino acids and xylose are used after drying in a
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desiccator over P2 O5 for 72 hrs before use. Aqueous fructose solutions of molality 0.05M, 0.10M, 0.15M and 0.20M
are prepared using doubly deionized distilled water with a conductivity of 1.5×10 -4 Ω-1 ·m-1 and are used as solvents to
prepare the molal concentrations of amino acids. For glycine, L-alanine, L-valine, mo lalit ies of (0.02, 0.04, 0.06, 0.08
and 0.1) M and for L-leucine, mo la lit ies of (0.02, 0.04, 0.05, 0.06 and 0.08) M are used respectively. The mass
measurements are made using a high precision and electronic balance (Model HR 300, Japan) with a precision of ± 0.1
mg. The densities of the solutions are measured using a single stem Pycno meter (Pyrex g lass) of bulb capacity of 15×10 -3
dm3 having graduated stem with 5×10-7 dm3 div isions and ultrasonic speeds by a mult ifrequency ultrasonic interfero meter
(M-84, Mittal make, India) at a frequency of 2MHz. The reproducibilit ies of density and ultrasonic speed are within ±
2.8×10-4 g·cm-3 and ± 0.03% respectively [25,26]. The temperatures of the solutions are maintained to an uncertainty of
± 0.01 K in an electronically controlled thermostatic water bath (Eu rotherm, M ittal enterprises, New Delh i).

III. RES ULTS

The densities (ρ)(see table 1)see and u ltrasonic speed (u) of amino acids in aqueous xylose solutions at the
studied temperatures (Data ultrasonic speed (u) may be obtained from authors on request) are used to evaluate apparent
mo lar volu mes (Vφ ) and apparent molar co mp ressibility (Kφ ) using the follo wing equations (1) and (2 )

Vφ = (M/ ρ)-1000 (ρ – ρ0 ) /m ρ ρ0 (1)

Kφ = βs M/ ρ +1000 (βs ρ0 - β0 ρ)/ m ρ ρ0 (2)

Table 1: Density (ρ) of α – amino acids in aqueous xylose solutions at different temperatures
ρ *103 / (kg m-3 ) at various mS / mol·kg -1
T = 298.15 K
Glycine
m / (mol kg -1 ) 0.00 0.05 0.10 0.15 0.20
0.00 0.99704 0.99976 1.00245 1.00511 1.00774
0.02 0.99768 1.00049 1.00317 1.00582 1.00844
0.04 0.99831 1.00120 1.00387 1.00651 1.00911
0.06 0.99894 1.00188 1.00455 1.00718 1.00976
0.08 0.99956 1.00254 1.00521 1.00783 1.01038
0.10 1.00018 1.00318 1.00585 1.00846 1.01097
Alanine
0.00 0.99704 0.99976 1.00245 1.00511 1.00774
0.02 0.99761 1.00040 1.00308 1.00573 1.00834
0.04 0.99816 1.00102 1.00369 1.00633 1.00892
0.06 0.99870 1.00161 1.00427 1.00690 1.00946
0.08 0.99921 1.00217 1.00481 1.00744 1.00995
0.10 0.99972 1.00272 1.00535 1.00796 1.01045
Valine
0.00 0.99704 0.99976 1.00245 1.00511 1.00774
0.02 0.99756 1.00034 1.00302 1.00567 1.00828
0.04 0.99805 1.00091 1.00357 1.00622 1.00881
0.06 0.99851 1.00146 1.00411 1.00675 1.00932
0.08 0.99894 1.00199 1.00464 1.00726 1.00982
0.10 0.99934 1.00253 1.00515 1.00777 1.01031
Leucine
0.00 0.99704 0.99976 1.00245 1.00511 1.00774
0.02 0.99748 1.00027 1.00294 1.00559 1.00820
0.04 0.99785 1.00077 1.00340 1.00605 1.00863
0.06 0.99813 1.00101 1.00363 1.00627 1.00882
0.08 0.99835 1.00125 1.00384 1.00648 1.00900
0.10 0.99850 1.00172 1.00425 1.00687 1.00936
T = 303.15 K
Glycine
0.00 0.99564 0.99834 1.00100 1.00363 1.00622
0.02 0.99627 0.99905 1.00170 1.00432 1.00690
0.04 0.99689 0.99974 1.00238 1.00500 1.00756
0.06 0.99751 1.00041 1.00304 1.00566 1.00821
0.08 0.99812 1.00106 1.00369 1.00631 1.00885

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0.10 0.99873 1.00169 1.00432 1.00695 1.00947

Alanine
0.00 0.99564 0.99834 1.00100 1.00363 1.00622
0.02 0.99620 0.99897 1.00162 1.00423 1.00681
0.04 0.99674 0.99958 1.00222 1.00481 1.00737
0.06 0.99725 1.00016 1.00281 1.00535 1.00792
0.08 0.99774 1.00073 1.00338 1.00585 1.00842
0.10 0.99821 1.00128 1.00393 1.00636 1.00894
Valine
0.00 0.99564 0.99834 1.00100 1.00363 1.00622
0.02 0.99616 0.99891 1.00155 1.00417 1.00675
0.04 0.99666 0.99947 1.00209 1.00469 1.00725
0.06 0.99713 1.00001 1.00260 1.00517 1.00774
0.08 0.99757 1.00055 1.00307 1.00560 1.00820
0.10 0.99799 1.00107 1.00354 1.00605 1.00867
Leucine
0.00 0.99564 0.99907 1.00251 1.00363 1.00622
0.02 0.99607 0.99955 1.00298 1.00409 1.00666
0.04 0.99642 1.00001 1.00343 1.00452 1.00706
0.06 0.99668 1.00023 1.00364 1.00472 1.00722
0.08 0.99686 1.00045 1.00384 1.00490 1.00739
0.10 0.99696 1.00085 1.00426 1.00525 1.00768
T = 308.15 K
Glycine
0.00 0.99402 0.99670 0.99934 1.00193 1.00448
0.02 0.99464 0.99739 1.00002 1.00260 1.00514
0.04 0.99525 0.99807 1.00069 1.00326 1.00579
0.06 0.99586 0.99873 1.00135 1.00391 1.00644
0.08 0.99646 0.99938 1.00200 1.00455 1.00707
0.10 0.99705 1.00001 1.00264 1.00518 1.00770
Alanine
0.00 0.99402 0.99670 0.99934 1.00193 1.00448
0.02 0.99457 0.99731 0.99994 1.00251 1.00504
0.04 0.99511 0.99791 1.00053 1.00307 1.00558
0.06 0.99564 0.99850 1.00111 1.00360 1.00608
0.08 0.99616 0.99907 1.00168 1.00409 1.00657
0.10 0.99667 0.99962 1.00222 1.00459 1.00700
Valine
0.00 0.99402 0.99670 0.99934 1.00193 1.00448
0.02 0.99452 0.99725 0.99988 1.00246 1.00499
0.04 0.99498 0.99778 1.00040 1.00297 1.00548
0.06 0.99538 0.99829 1.00090 1.00345 1.00594
0.08 0.99575 0.99880 1.00138 1.00393 1.00636
0.10 0.99607 0.99927 1.00184 1.00437 1.00679
Leucine
0.00 0.99402 0.99670 0.99934 1.00193 1.00448
0.02 0.99444 0.99718 0.99980 1.00239 1.00492
0.04 0.99477 0.99762 1.00023 1.00284 1.00534
0.06 0.99502 0.99783 1.00043 1.00306 1.00552
0.08 0.99516 0.99804 1.00062 1.00327 1.00571
0.10 0.99525 0.99847 1.00098 1.00370 1.00607
T = 313.15 K
Glycine
0.00 0.99220 0.99486 0.99747 1.00005 1.00258
0.02 0.99281 0.99552 0.99812 1.00069 1.00321
0.04 0.99341 0.99617 0.99876 1.00132 1.00383
0.06 0.99401 0.99680 0.99939 1.00194 1.00445
0.08 0.99460 0.99741 1.00000 1.00255 1.00506

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0.10 0.99518 0.99801 1.00061 1.00315 1.00566

Alanine
0.00 0.99220 0.99486 0.99747 1.00005 1.00258
0.02 0.99273 0.99544 0.99803 1.00060 1.00311
0.04 0.99325 0.99601 0.99858 1.00114 1.00363
0.06 0.99376 0.99657 0.99911 1.00165 1.00411
0.08 0.99426 0.99713 0.99962 1.00216 1.00457
0.10 0.99475 0.99766 1.00011 1.00263 1.00502
Valine
0.00 0.99220 0.99486 0.99747 1.00005 1.00258
0.02 0.99269 0.99540 0.99800 1.00057 1.00309
0.04 0.99313 0.99592 0.99851 1.00107 1.00358
0.06 0.99350 0.99642 0.99899 1.00155 1.00406
0.08 0.99382 0.99689 0.99946 1.00201 1.00452
0.10 0.99409 0.99735 0.99988 1.00242 1.00496
Leucine
0.00 0.99220 0.99486 0.99747 1.00005 1.00258
0.02 0.99261 0.99532 0.99792 1.00049 1.00301
0.04 0.99294 0.99576 0.99834 1.00090 1.00340
0.06 0.99318 0.99597 0.99853 1.00108 1.00358
0.08 0.99332 0.99616 0.99873 1.00127 1.00376
0.10 0.99338 0.99654 0.99907 1.00162 1.00409

Where M is the mo lar mass of the solute, m is the solution molality and ρ , ρ0 , βs and β0 are the densities and coefficients
of adiabatic co mpressibilit ies of the solution and solvent(aqueous xy lose) respectively. The ad iabatic co mpressibilities βs
and β0 of the solution and solvent are determined fro m the experimental valu es of the u ltrasonic speed and density using
the Newton-Lap lace equation β= 1/ρ u 2
The partial molar quantities (Yφ 0 ) are obtained using the equation (3)
Yφ = Yφ0 +S y m (3)

Where Yφ0 (Yφ 0 denotes Vφ0 or Kφ0 ) is the infinite dilution value that is equal to the partial mo lar p roperty at infin ite
dilution and S y (S y denotes S vor S k) is the experimental slope [27]. Equation (3) is fitted to Yφ (Yφ denotes Vφ or Kφ ) values
by the method of least squares to evaluate Vφ0 and Kφ 0 values. The evaluated values of partial molar volu mes Vφ 0 and
partial mo lar co mpressibility Kφ0 along with standard deviations of linear regression , σ , are given in tables 1 and 5
respectively. The values of Vφ 0 and Kφ 0 of the four amino acids in water at all the temperatures agree (see tables 2 and 6)
fairly well with literature values [28-37], thus validating our experimental p rocedures.

The partial mo lar volu mes of transfer ΔVφ0 of amino acids from pure water to xy lose water mixtures are
calculated using equation (4).
ΔVφ0 = Vφ 0 (in aqueous xylose) - Vφ 0 (in pure water) (4)
The partial molar volu mes of transfer ΔVφ 0 result is given in table 3.

The temperature dependence of Vφ 0 [38] for homo logous amino acids in aqueous xylose solution can be expressed by the
equation (5).
Vφ 0 = a + bT + cT2 (5)

Where a,b and c may be estimated by the least squares fitting of partial mo lar volu me in the above equation. The value
(∂2 Vφ 0 /∂T2 ), called Hepler’s constant [39] gives the information about the structure making / breaking properties of
solute in aqueous xy lose solution. On the basis of these criteria, a structure making solute will exhib it positive
(∂2 Vφ 0 /∂T2 ) values and structure breaking solute will show negative (∂2 Vφ 0 /∂T2 ) values. The values of Hepler’s constant
are given in table 4.

The hydration number n H may be evaluated fro m the volu met ric data using the following standard equations
reflected in literature [20, 24].
n H = Vφ0 (elect) / (V0 E – V0 B ) (6)

Where Vφ0 (elect) is the electrostriction partial mo lar volu me due to the hydration of amino acids, V0 E is the molal volu me
of the electrostricted water and V0B is the molar volu me of bulk water. This procedure has been used by Wang et

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al.[40].The reported values of (V0E – V0 B ) -3.3 cm3 ·mo l-1 at T = 298.15 K , by Millero etal[ 3] It is found that (V0E –
V0 B ) -4 cm3 · mo l-1 at T = 308.15 K. This value of(V0 E – V0B ) has been retained at the other studied temperatures, as
suggested by Lark et al.[41], to evaluate n H values and are given in table 4
Further fro m co mpressibility data, the number of water mo lecules n H hydrated to amino acids [32] are calculated
using equation (6), and this method has been proposed by Millero et al. and are included in the table 5.
n H = -Kφ 0 (elect) / V0 B K0 B (7)
Where K0 B is the compressibility of bulk water. The value of V0 B K0B is taken as 8.1x10-6 m3 ·mo l-1 ·GPa-1 at 298.15 K
[42]. The electrostriction partial molar co mpressibility Kφ 0 (elect) can be estimated fro m the value of Kφ 0 fro m
Kφ0 (elect) = Kφ 0 (amino acid)- Kφ 0 (int) (8)

As Kφ0 (int) is very s mall, that is less than 5x10-6 m3 ·mol-1 ·GPa-1 for ionic crystal and many organic solutes in
0
water[3].So one can assume Kφ (int)=0.Therefore,the equation(8) becomes
Kφ0 (elect) = Kφ 0 (amino acid) (9)
The values of n H calculated fro m equation(8) are g iven in table 7,which is described in detail elsewhere [42].

It must be noted that, the evaluation of hydration number n H is model dependent and the values of n H determined
using volumetric data and comp ressibility data are slightly different[33].

IV.DISCUSS ION

The volumetric behavior of solute at infinite dilution represented by Vφ 0 (see table 1) are positive and increases
fro m glycine to leucine at a particu lar temperature and concentration. This may be attributed to the increased
hydrophobic / non polar character of the side chain of these amino acids causing a reduction in elect rostriction at the
terminal charged groups , suggesting the presence of strong solute – solvent interactions in the system [34]. The increase
in the values of Vφ 0 with temperature may be attributed to the release of some solvent mo lecules fro m the loose solvation
layers of the solutes in solution [20]. The Vφ 0 values of amino acids in aqueous xylose solution at particular temperature
and concentration following the order glycine < alanine<valine< leucine.

Table 2 Partial molal volume (Vφ 0 ) of α – amino acids in aqueous xylose solutions at different temperatures.
Vφ 0 * 106 / m3 mo l-1 at various ms / mo l kg -1
Amino
0.00 (Water)
Acid
Present Work Literature 0.05 0.10 0.15 0.20
T = 298.15 K
Glycine 43.003 (0.095) 43.14a, 43.16b 37.958(0.099) 38.564(0.100) 39.053(0.100) 39.400(0.099)
Alanine 60.280(0.099) 60.41b , 60.12c 56.429(0.099) 56.810(0.099) 57.252(0.099) 57.994(0.098)
Valine 90.581(0.100) 90.65a, 90.39d 87.787(0.097) 88.205(0.098) 88.425(0.098) 89.304(0.099)
Leucine 108.166(0.042) 107.75b , 107.76e 105.315(0.098) 105.817(0.099) 105.975(0.098) 106.526(0.098)
T = 303.15 K
Glycine 43.523(0.095) 43.59a 39.074(0.100) 39.658(0.099) 40.188(0.099) 40.732(0.098)
Alanine 60.614(0.099) 60.63a 57.110(0.099) 57.674(0.099) 58.198(0.098) 58.895(0.098)
Valine 90.718(0.099) 90.98a 88.437(0.098) 88.873(0.100) 89.079(0.099) 89.886(0.098)
Leucine 108.255(0.064) 106.253(0.099) 106.654(0.095) 106.833(0.099) 107.297(0.099)
T = 308.15 K
Glycine 44.007(0.097) 43.90 f, 44.26g 40.185(0.099) 40.824(0.100) 41.305(0.100) 41.839(0.097)
Alanine 61.540(0.100) 61.41g 58.296(0.098) 58.777(0.097) 59.353(0.098) 60.154(0.098)
Valine 91.356(0.099) 91.42 f 89.454(0.098) 89.686(0.100) 90.017(0.099) 90.678(0.098)
Leucine 108.681(0.075) 108.40 f 107.053(0.088) 107.336(0.099) 107.682(0.097) 108.002(0.097)
T = 313.15 K
Glycine 44.538(0.097) 44.52 f 41.656(0.099) 42.291(0.099) 42.819(0.100) 43.401(0.097)
Alanine 62.617(0.100) 62.90 f 60.009(0.097) 60.675(0.098) 61.085(0.098) 61.820(0.098)
Valine 91.673(0.099) 91.58 f 89.912(0.099) 90.164(0.099) 90.521(0.098) 91.089(0.098)
Leucine 109.148(0.074) 109.00 f 107.813(0.074) 108.024(0.099) 108.386(0.098) 108.654(0.098)
a
Ref 28, b Ref29, c Ref30, d Ref31, e Ref32, fRef33, g Ref34

The transfer volume values of ΔVφ 0 (see table 2) will indicate only the solute solvent interactions. In the present case ,
these values for all the four amino acids are negative and increase monotonically with the mass fractions of xy lose in
aqueous xylose solutions indicating the presence of strong solute solvent interactions in the solutions.. These results can

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be explained by the cosphere overlap model, as developed by Fried man and Krishnan [43]. The types of interactions
existing between homologous amino acid mo lecules and xylose mo lecules are

Table 3 :Partial molar volume of transfer (ΔVφ 0 ) of α – amino acids in aqueous xylose solutions at different
temperatures.
ΔVφ 0 * 106 / m3 mo l-1 at various ms / mol kg -1
Amino
0.05 0.10 0.15 0.20
acids
T = 298.15 K
Glycine -5.045 -4.439 -3.950 -3.603
Alanine -3.851 -3.470 -3.028 -2.286
Valine -2.794 -2.376 -2.156 -1.277
Leucine -2.851 -2.349 -2.191 -1.640
T = 303.15 K
Glycine -4.449 -3.865 -3.335 -2.791
Alanine -3.504 -2.94 -2.416 -1.719
Valine -2.281 -1.845 -1.639 -0.832
Leucine -2.002 -1.601 -1.422 -0.958
T = 308.15 K
Glycine -3.822 -3.183 -2.702 -2.168
Alanine -3.244 -2.763 -2.187 -1.386
Valine -1.902 -1.67 -1.339 -0.678
Leucine -1.628 -1.345 -0.999 -0.679
T = 313.15 K
Glycine -2.882 -2.247 -1.719 -1.137
Alanine -2.608 -1.942 -1.532 -0.797
Valine -1.761 -1.509 -1.152 -0.584
Leucine -1.335 -1.124 -0.762 -0.494

(1) Hydrophilic– ionic group interactions between the OH groups of xylose and the zwitterionic center of the amino acid.
(2) Hydrophilic–hydrophilic group interactions between the OH groups of xylose and the OH groups of the amino acid
med iated through the hydrogen bonding.
(3) Hydrophilic–hydrophobic group interactions between the OH groups of xy lose and the non-polar (-CH2 ) groups of
the amino acid.
(4) Hydrophobic–hydrophobic group interactions between the (-CH2 ) groups of xylose and the non-polar (-CH2 ) groups
of the amino acid.
The interactions of types (1) and (2) make positive contributions to the transfer volu me, whereas the
contributions of type (3) and (4) are opposite. It may be in ferred that the negative transfer volume in the ternary solution,
indicate that hydrophilic– hydrophobic and hydrophobic–hydrophobic interactions are not compensated by ion–
hydrophilic and hydrophilic–hydrophilic interactions [16,44,45]. With the increase of saccharide concentrations, the
interactions between the –OH group of the saccharide and the zwitterionic centre of the glycine also increase gradually
which are not compensated by the interactions between the –OH group of the saccharide and non-polar group of the
amino acids.

Table 4 : Hepler’s constant of α – amino acids in aqueous xylose solutions at different temperatures
Amino ∂2 Vφ 0 /∂T2 /(m6 . mol-2 . k-2 ) at various ms / mo l kg -1
acids 0.05 0.10 0.15 0.20
Glycine 0.0036 0.0037 0.0038 0.0023
Analine 0.0103 0.0103 0.0079 0.0077
Valine -0.0019 -0.0019 -0.0015 -0.0017
Leucine -0.0018 -0.0015 -0.0015 -0.0012

The positive values of (∂2 Vφ 0 /∂T2 ) for glycine and alanine (see table 3) indicate[46] that these two amino acids
act as structure-maker and negative(∂2 Vφ 0 /∂T2 ) values for valine and leucine supports the structure breaking ability of
these amino acids in aqueous -xylose solutions.

The evaluated hydration number n H values using volumetric data (see table 4) show a decreasing trend with increase in
temperature and concentration which indicates hydrophilic-hydrophobic group interactions are higher and as a result,
greater electrostriction of solvent water is produced leading to higher values of n H at lower concentration.

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Table 5: Hydration Number (nH) of α – amino acids in water and in aqueous xylose solutions from volumetric data at
different temperatures.
n H at various ms / mo l kg -1
Fro m volu me Fro m volu me Fro m volu me Fro m volu me Fro m volu me
Amino Acid 0 0.05 0.10 0.15 0.20
T = 298.15 K
Glycine 2.14 3.40 3.25 3.13 3.04
Alanine 2.46 3.43 3.33 3.22 3.04
Valine 3.64 4.34 4.24 4.18 3.96
Leucine 3.36 4.07 3.95 3.91 3.77
T = 303.15 K
Glycine 2.01 3.13 2.98 2.85 2.71
Alanine 2.38 3.26 3.12 2.99 2.81
Valine 3.61 4.18 4.07 4.02 3.82
Leucine 3.34 3.84 3.74 3.69 3.58
T = 308.15 K
Glycine 1.89 2.85 2.69 2.57 2.43
Alanine 2.15 2.96 2.84 2.7 2.50
Valine 3.45 3.93 3.87 3.79 3.62
Leucine 3.23 3.64 3.57 3.48 3.40
T = 313.15 K
Glycine 1.76 2.48 2.32 2.19 2.04
Alanine 1.88 2.53 2.37 2.26 2.08
Valine 3.37 3.81 3.75 3.66 3.52
Leucine 3.12 3.45 3.40 3.31 3.24

Table 6: Partial Molar Compressibility (Kφ0 ), of α – ami no acids in in water and in aqueous xylose solutions at
different temperatures.
Kφ0 * 1015 / m3 mo l-1 Pa-1 at Various ms / mo l kg-1
Amino
0.00 (Water)
Acid
Present Work Literature 0.05 0.10 0.15 0.20
T = 298.15 K
Glycine -26.62 -26.60h -28.64 -27.56 -26.35 -25.13
Alanine -24.74 -24.70h -26.69 -25.46 -24.24 -22.98
Valine -30.09 -30.00i -32.47 -30.87 -29.23 -27.52
Leucine -31.24 -31.30j -34.26 -32.18 -30.24 -28.16
T = 303.15 K
Glycine -24.60 -26.57 -25.34 -24.54 -23.11
Alanine -23.77 -25.56 -24.33 -23.07 -21.85
Valine -26.21 -28.32 -26.70 -25.08 -23.51
Leucine -27.62 -30.38 -28.35 -26.30 -24.38
T = 308.15 K
Glycine -23.35 -23.15g -24.89 -23.78 -22.67 -21.74
Alanine -22.92 -21.00g -24.38 -23.13 -21.86 -20.68
Valine -23.61 -23.56e -25.50 -24.00 -22.27 -20.60
Leucine -24.20 -26.66 -24.50 -22.55 -20.62
T = 313.15 K
Glycine -22.83 -22.40j -24.26 -23.06 -21.94 -20.75
Alanine -21.87 -21.00j -22.85 -21.70 -20.52 -19.24
Valine -20.87 -22.60 -20.93 -19.29 -17.66
Leucine -22.63 -24.57 -22.73 -20.69 -18.75
g h i j
Ref 34, Ref 35, Ref36, Ref37

Fro m table 5, partial mo lar co mpressibility values are negativ e indicat ing the presence of strong solute-solvent
interactions, thereby complementing the volu metric results. The negative partial mo lar co mpressibility values are
attributed to the presence of hydrophobic-hydrophobic and hydrophilic-hydrophobic interactions. The partial mo lar
compressibility values increase with temperature and concentration further substantiate the hydrophobic –hydrophobic
interactions are not compensated by hydrophilic – hydrophilic interactions between the cosolutes.

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Table 7 : Hydration Number (nH) of α – Amino acids in Water and in aqueous xylose solution from velocity at
different temperatures
n H at various ms / mo l kg -1
Fro m velocity Fro m velocity Fro m velocity Fro m velocity Fro m velocity
Amino Acid 0 0.05 0.10 0.15 0.20
T = 298.15 K
Glycine 3.29 3.54 3.40 3.25 3.10
Alanine 3.05 3.30 3.14 2.99 2.84
Valine 3.71 4.01 3.81 3.61 3.40
Leucine 3.86 4.23 3.97 3.73 3.48
T = 303.15 K
Glycine 3.04 3.28 3.13 3.03 2.85
Alanine 2.93 3.16 3.00 2.85 2.70
Valine 3.24 3.50 3.30 3.10 2.90
Leucine 3.41 3.75 3.50 3.25 3.01
T = 308.15 K
Glycine 2.88 3.07 2.94 2.80 2.68
Alanine 2.83 3.01 2.86 2.70 2.55
Valine 2.91 3.15 2.96 2.75 2.54
Leucine 2.99 3.29 3.02 2.78 2.55
T = 313.15 K
Glycine 2.82 3.00 2.85 2.71 2.56
Alanine 2.7 2.82 2.68 2.53 2.38
Valine 2.58 2.79 2.58 2.38 2.18
Leucine 2.79 3.03 2.81 2.55 2.31

The values of hydration numbers nH calculated based on compressibility data show a similar t rend as that of volumetric
data. This may be attributed to the dehydration effect of xylose on amino acids.

V. CONCLUS ION

In the present work, the volu metric and co mpressibility properties of so me ho mologous amino acids in aqueous
xy lose solutions are reported at four different temperatures. The values of partial molar volu mes and part ial mo lar
compressibility indicate the presence of strong solute-solvent interactions in the solution. Our study further concludes the
existence of hydrophilic–hydrophobic and hydrophobic–hydrophobic group interactions are over the ion–hydrophilic and
hydrophilic–hydrophilic group interactions between solute and cosolutes in aqueous ternary solution. Fro m the temperature
dependence of partial molar volu metric data, it is found that glycine and alanine act as structure maker while valine and
leucine as structure breaker in aqueous xylose solutions.

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