8/7/2019 SATHISH PRASAD
1/46
Presented by:
SATHISH
Chemistry Department.
8/7/2019 SATHISH PRASAD
2/46
INTRODUCTION
IONIC LIQUIDS
COMPOSITION OF IONIC LIQUIDS
Figure 1: structure of ionic liquids[ BMIM]
.
8/7/2019 SATHISH PRASAD
3/46
8/7/2019 SATHISH PRASAD
4/46
APPLICATIONS OF IONIC LIQUIDS
y Ionic liquids as stationary phases in gas chromatography
y Ionic liquids in capillary electrophoresis
y Ionic liquids as background electrolyte additives in non-
aqueous media
y Ionic liquids as electrolyte additives in aqueous media
8/7/2019 SATHISH PRASAD
5/46
Figure 2: Mechanism of polyphenols separation using 1-alkyl-3-methylimidazolium based ionic
liquid
NN
CH4R
NN
R
CH3
NN
RCH3
NN
RCH3
NN
RCH3
O
OH
OH
OH
OH
OH O
NN
CH3 R
EOF
NN
CH3R
NN
R CH4
NN
R CH3
NN
R CH3
NN
R CH3
8/7/2019 SATHISH PRASAD
6/46
APPLICATIONS OF IONIC LIQUIDS CONT.
y Analytical applications of ionic liquids as a micelle-formingsurfactant
y Application of ionic liquids to the electrodeposition ofmetals
y Ionic liquids in spectrometry
y Ionic liquids as extractions
y Extraction of bioactive compounds in natural plant
8/7/2019 SATHISH PRASAD
7/46
IONIC LIQUIDS IN LIQUID CHROMATOGRAPHY
Figure 3: Scheme illustrating potential interactions between methylimidazolium cation and phenyl-basedreversed-phase stationary phase.
Reversed-phaseliquidchromatographicanalysisofionicliquids
8/7/2019 SATHISH PRASAD
8/46
APPLICATIONS OF IONIC LIQUIDS IN NORMAL-
PHASE LIQUID CHROMATOGRAPHY Ionic liquids as mobile-phase additives in liquid
chromatography
Ionic liquids as stationary phases in liquid chromatography
A Surface confined ionic liquids as reversed phase stationaryphases in liquid
Figure 4: Scheme illustrating potential reorientation of bonded imidazolium ligands in response to deprotonationofresidual silanols
8/7/2019 SATHISH PRASAD
9/46
DRAWBACKS FOR INDUSTIAL APPLICATION
Lack of physical parameters such as conductivity, viscosity is
serious drawbacks for industrial application of ionic liquids.
ydrophobic ionic liquids although they are stable and allow
easiest recovery from biphasic processes bur never designed to
dissolve carbohydrate-based macromolecules because their
solubilisation depends on the competitive replacement of
intermolecularhydrogen bonding.
ne of the potential problems with ionic liquids is the possible
pathway into environment through waste water but this problem is
common with
all solvents
8/7/2019 SATHISH PRASAD
10/46
THEORY
ADSORPTION
Adsorption is the process in which matter is
extracted from one phase and concentrated at the
surface of a second phase. (Interface accumulation).
This is a surface phenomenon as opposed toabsorption where matter changes solution phase,
e.g. gas transfer. This is demonstrated in the
following schematic.
8/7/2019 SATHISH PRASAD
11/46
.
8/7/2019 SATHISH PRASAD
12/46
If we have to remove soluble material from the solution phase,
but the material is neither volatile nor biodegradable, we often
employ adsorption processes. Also adsorption has application
elsewhere, as we will discuss later.
Adsorbate: material being adsorbed
Adsorbent: material doing the adsorbing. (examples are
activated carbon or ion exchange resin).
8/7/2019 SATHISH PRASAD
13/46
TYPES OF ADSORPTION
Exchange adsorption (ion exchange)
Electrostatic due to charged sites on the surface. Adsorptiongoes up as ionic charge goes up and as hydrated radius goesdown.
Physical adsorption
Van der Waals attraction between adsorbate and adsorbent. Theattraction is not fixed to a specific site and the adsorbate isrelatively free to move on the surface. This is relatively weak,reversible, adsorption capable of multilayer adsorption
8/7/2019 SATHISH PRASAD
14/46
CHEMICALADSORPTION
Some degree of chemical bonding between adsorbate and
adsorbent ch
aracterized by strong attractiveness. Adsorbedmolecules are not free to move on the surface. There is a high
degree of specificity and typically a monolayer is formed. The
process is seldom reversible.
Generally some combination of physical and chemical
adsorption is responsible for activated carbon adsorption in
water and wastewater
8/7/2019 SATHISH PRASAD
15/46
ADSORPTION EQUILIBRIA
If the adsorbent and adsorbate are contacted long enough an
equilibrium will be established between the amount of
adsorbate adsorbed and the amount of adsorbate in solution.
The equilibrium relationship is described by isotherms.
qe = mass of material adsorbed (at equilibrium) per mass of
adsorbent.
e = equilibrium concentration in solution when amountadsorbed equals qe.
qe/ e relationships depend on the type of adsorption that
occurs, multi-layer, chemical, physical adsorption, etc.
8/7/2019 SATHISH PRASAD
16/46
ISOTHERM MODELS
y The figures below show that there are four common models for
isotherms.
8/7/2019 SATHISH PRASAD
17/46
LANGMUIR ISOTHERM
This model assumes monolayer coverage and constant bindingenergy between surface and adsorbate.
The model is:
represents the maximum adsorption capacity (monolayercoverage) (g solute/g adsorbent).
Ce has units of mg/L.
K has units of L/mg
0a e
ee
K Q Cq
1 K C
!
0
aQ
8/7/2019 SATHISH PRASAD
18/46
BET (BRUNAUER,EMMETT AND TELLER)
ISOTHERM
y This is a more general, multi-layer model. It assumes that a
Langmuir isotherm applies to each layer and that no transmigration
occurs between layers. It also assumes that there is equal energy of
adsorption for each layer except for the first layer.
S
=saturation (solubility limit) concentration of the solute. (mg/liter)
KB = a parameter related to the binding intensity for all layers.
Note: when e > 1 and K = KB/ s BET isotherm
approaches Langmuir isotherm.
)}/)(1K(1){(
QKq
SeBeS
0
aeB
e
!
8/7/2019 SATHISH PRASAD
19/46
FREUNDLICH ISOTHERM
y For the special case of heterogeneous surface energies
(particularly good for mixed wastes) in which the energy term,
KF
, varies as a function of surface coverage we use the
Freundlich model.
yy nn andand KKFF areare systemsystem specificspecific constantsconstants..
n
eFeK!
8/7/2019 SATHISH PRASAD
20/46
RESEARCH OBJECTIVE
y The objective is to use ionic liquids as mobile phasesalong with acetic acid and methanol to study their effect asmobile phase additives in reversed phase liquid
chromatography.
ere tryptophan was used as solute and an aqueoussolution of methanol along with ionic liquid was used asmobile phase.
Study involved comparision of calibration curves, profile,calibbration data, adsorption behaviour and peak shapeswith two different columns (prevail, Xterra)
8/7/2019 SATHISH PRASAD
21/46
Experimentaly Commercially available tryptophan was purchased from
Spectrum (Gardena, CA 9 2 8 and Newburnswick, NJ,
89 1).
Thio urea was purchased from Sigma Aldrich.
Methanol, water and acetic acid used are all PLC grade and
were purchased from Fischer Scientific FairLaw, NJ.
8/7/2019 SATHISH PRASAD
22/46
APPARATUS
Apparatus used is Shimadzu liquid chromatography, PLC-model 2 A, which is equipped with auto sampler (SIL-
2 A/2 AC) and online degasser (DGU-2 A3/ DGU-2 A5)was used.
UV-VIS (SPD-2 A/SPD-2 AV) was used as a detector.
XTERRA-C18 (15 mm .6mm, Particle size-5) was used as a
stationary phase that was supplied from (Waters, 2 Libertyway, Franklin, MA 2 38).
PREVAIL-C18(25 mm .6mm, Particle size-5) was used as astationary phase.
8/7/2019 SATHISH PRASAD
23/46
y ORIGIN
SR6 Origin 7.5, Origin Lab Corporation, One round house
plaza, North
ampton, MA 1 6 USA, 1991-2 6 was used
y Preparation of mobile phase
yAqueous solutions 1 % methanol, 1%acetic acid Without ILs
SOFTWARE PROGRAMS
8/7/2019 SATHISH PRASAD
24/46
Aqueoussolutionsof1%aceticacid, NomethanolWith ILs
5Mm Ionic liquid with No methanol and 1% acetic acid
Preparation of .1 g/L, 1g/L, 1 g/L of tryptophan
1 Mm Ionic liquid 1% acetic acid, No methanolPreparation of .1 g/L, 1g/L, 1 g/L of tryptophan
Aqueoussolutionsof1%aceticacid, 10% methanolWith Ils
5Mm Ionic liquid with 1 % methanol and 1% acetic acid
Preparation of .1 g/L, 1g/L, 1 g/L of tryptophan
Mm Ionic liquid with 1 % methanol and 1% acetic acid
Preparation of .1 g/L, 1g/L, 1 g/L of tryptophan
8/7/2019 SATHISH PRASAD
25/46
MECHANISM
Interactionof[BMIM]BF4 onmodifiedsilicasurface.
8/7/2019 SATHISH PRASAD
26/46
RESULTS AND DISCUSSION
2 6 8
2
2
6
8
(A
A (mau)
t (min)
N O
E O
N O I L
A C T R
T O
A N
g/L
5 5
2
6
8
(B)t (min)
A
(mau)
NO
EO
N O I L
A C TR! "
TO"
A N #
$
/L
10 12 14
%
&
% %
2% %
3% %
' % %
5% %
6% %
B(
I(
5( (
N O(
E O)
0 1
)
A C T R2 3
T O3 )
A N0 4
/L
t (min)
A
(mau)
(c)0 2 4 6 8 10 12 14 16
0
200
400
600
800
1000
B(
I(
5( (
NO(
EO)
0 1
)
A C TR2
TO3 )
A N0 5 4
/L
A6
7
(mau)
t (min) (D)
10 12 140
100
200
300
400
500
600
Abs (mau)
t (min)
BMIM 10MM NO MEOH 1% HAC TRYTOPHAN 1G/L
(E)
0 4 8 12 160
150
300
450
600
750
900
1050
Abs (mau)
t (time) (F)
BMIM 10MM NO MEOH 1% HAC TRYTOPHAN 10G/L
Figure 5: Effect of the concentration of BMIM in mobile phase on breakthrough curves of tryptophan A-B: No MeOHNO IL;C-D: No
MeOH, 5 mM BMIM;E-F: No MeOH, 1 mM BMIM; left 1 g/LTryptophan and right 1 g/LTryptophan. Column: C18 X-terra, Flowrate:
1. ml/min, Wavelength: 3 5 and 31 for tryptophan 1 g and1 g/L respectively.
8/7/2019 SATHISH PRASAD
27/46
0 2 4 6 8 10
0
200
400
600
Abs (mau)
t (min)(A)
NO MEOH NO IL 1% HAC TRYPTOPHAN 1G/L
0 2 4 6 8 10 12 1 4 160
100
200
300
400
500
Abs (mau)
t (min) (C)
BMIM 5MM NO MEOH 1% HAC TRYPTOPHAN 1G/L
0 2 4 6 8 10 12 14 160
100
200
300
400
500
600
Abs (mau)
t (min) (D)
BMIM 5MM NO MEOH 1% HAC TRYTOPHAN 10G/L
0 2 4 6 8 10 120
100
200
300
400
500
Abs (mau)
t (time) (E)
BMIM 10MM NO MEOH 1% HAC TRYPTOPHAN 1G/L
0 3 6 9 12
0
200
400
Abs (mau)
t (time)(F)
BMIM 10MM NO MEOH 1% HAC TRYPTOPHAN 10G/L
Figure 6: The effect of concentration of BMIM in mobile phase on the overloaded band profiles of tryptophan A-B: No MeOHNo IL;C-
D: No MeOH, 5 mM BMIM;E-F: No MeOH, 1 mM BMIM; left 1g/LTryptophan and right 1 g/LTryptophan.Column: C18 X-terra,
Flow rate: 1. ml/min, Wavelength: 3 5 and 31 for tryptophan 1g and 1 g/L respectively
8/7/2019 SATHISH PRASAD
28/46
CALIBRATION GRAPHS
Mobile phase C(g/L) Parameters of polynomifit : y=a+bx+cx2+dx3
a b cd
No IL No MeOH1%HAC
1 TRYP0.02225 0.00103 8.28317
10 TRYP 0.06058 0.00347 4.94741
5 mM BMIM 1%HACNo MeOH
1 TRYP 0.00616 0.001 8.98003
10 TRYP 0.06884 0.00357 4.68651*
10 mM BMIM 1%HACNo MeOH
1 TRYP 0.01923 9.3561310-4 9.1786
10 TRYP -0.09964 0.00652 5.019
Table 4: Parameters of the polynomial fit for the different
concentrations of BMIM in the mobile phase.
8/7/2019 SATHISH PRASAD
29/46
0 100 200 300 400 500 600 700
0.0
0.2
0.4
0.6
0.8
1.0
C (g/L)
Abs (mau)
NO MEOH NO IL 1% HAC TRYPTOPHAN 1G/L
0 200 400 600 800 1000 1200
0
2
4
6
8
10
C (g/L)
Abs (mau) (B)
NO MEOH NO IL 1% HAC TRYPTOPHAN 10G/L
0 100 200 300 400 500 600 700
0.0
0.2
0.4
0.6
0.8
1.0
C (g/L)
Abs (mau) (C)
BMIM 5MM NO MEOH 1% HAC TRYPTOPHAN 1G/L
0 200 400 600 800 1000 1200
0
2
4
6
8
10
C (g/L)
Abs (mau) (D)
BMIM 5MM NO MEOH 1% HAC TRYPTOPHAN 10G/L
0 100 200 300 400 500 600 700
0.0
0.2
0.4
0.6
0.8
1.0
Abs (mau)
C (g/L)
BMIM 10MM NO MEOH 1% HAC TRYPTOPHAN 1G/L
(E)
0 200 400 600 800 1000 1200
0
2
4
6
8
10
C (g/L)
Abs (mau) (F)
BMIM 10MM NO MEOH 1% HAC TRYPTOPHAN 10G/L
Figure 7: Calibration curves of tryptophan determined by FA with different concentrations of BMIM on C18 X-terra column. tryptophanA-
B: No MeOHNo IL;C-D: No MeOH, 5mM BMIM;E-F: No MeOH, 1 mM BMIM; left 1g/LTryptophan and right 1 g/LTryptophan. Flow
rate 1. mL/ min; Wavelength 3 5 nm and room temperature. Mobile phases: aqueous mixture containing 1% HAC and NOmethanol and
BMIM
8/7/2019 SATHISH PRASAD
30/46
0 2 4 6 8 10
0
20
40
60
80
q(g/L)
C(g/L)
NO MEOH NO IL 1% HAC TRYPTOPHAN
(A)
0 2 4 6 8 10
0
40
80
q(g/L)
c(g/L)(B)
BMIM 5MM NO MEOH 1% HAC TRYPTOPHAN
0 2 4 6 8 10
0
20
40
60
80
100
q (g/L)
C (g/L)
BMIM 10MM NO MEOH 1% HAC TRYPTOPHAN
(C)
0 2 4 6 8 10
0
40
80
Tryptophan, No MeOH 1%HAC
black sqaures:10 mM BMIMBF4
red triangles: 5 mM BMIMBF4
q(g/L)
c(g/L)
Figure 8: Experimental isotherm data with different concentrations of BMIM on X-TerraColumn. Flow rate 1. mL/ min; Wavelength 3 5
nm and Room temperature. Mobile phases: -1 % (v/v) mixtures of No methanol, acetic acid andHPLC water
8/7/2019 SATHISH PRASAD
31/46
[BMIM] Model5 mM Langmuir
TRYPTOPHAN
IM
10g/L
1 g/L
AVG
FA
195.7
220
207.8
220.95
0.09252
0.0817
0.17422
0.0817
10 mM Langmuir
TRYPTOPHAN
IM
10g/L
1g/L
AVG
162.3
158.5
160.4
0.1111
0.1074
0.10975
FA 218.02096 0.08614
Theparametersofisothermalcurvefortryptophan withdifferent
concentrations ILsinmobilephaseon C1 Xterracolumn.
8/7/2019 SATHISH PRASAD
32/46
PREVAIL COLUMN
89
@
8
@
9A 8
8
@
8 8
A 8 8
B 8 8
C 8 8
A D E F G H I P
Q R Q S T eU
V
AW
PREVAIL NO ILX Y
ACa
Rb
Pa
OP
ANc
d
X e f
L
gh
i
g
i
hp g p
h
g
p g g
q g g
r g g
As
t
u
v w x
y
e
PREVAIL NO IL
AC
R
P
OP
AN
L
A
R T
U
j
Cj
PREVAIL NO IL k l m
AC n Ro
Pn OPm
AN k
L
Figure 9: Effect of concentration of BMIM in mobile phase on breakthrough curves ofTryptophan A-C: No OMIM;D-F: 1 % MeOH, 5 mM
BMIM;Column: C18Prevail, Flow rate: 1. ml/min, Wavelength: 3 5 and 31 for tryptophan 1 g and 1 g/L respectively.
8/7/2019 SATHISH PRASAD
33/46
8/7/2019 SATHISH PRASAD
34/46
0 5 10 15 20 25 300
20
40
60
80
100
120
140
160
180 NO MEOH NO IL 1% HAC TRYPTOPHAN 0.1G/L
Abs (mau)
t (time) (A)
0 2 0 0 4 00 60 0 8 00 1 0 0 0 1 2 00 1 40 0 1 60 0
0
1
2
3
4
5
6 NO MEOH NO IL 1% HAC TRYTOPHAN 1G/L
Abs (mau)
t (time) (B)
0 5 10 15 20 25 300
1 00
2 00
30 0
4 00
50 0
6 00
A b s ( m a u )
t ( t im e) (C )
N O I L N O M E O H 1 % H A C T R Y P T O P H A N 1 0 G /L
Figure 11: The effect of concentration of BMIM in mobile phase on the overloaded band profilesof tryptophanA-C: No BMIM;Column:
C18 Prevail, Flow rate: 1. ml/min, Wavelength: 3 5 and 31 for tryptophan 1 gand 1 g/L respectively
8/7/2019 SATHISH PRASAD
35/46
0 5 10 15 20 25 300
50100
150
200
250
300
Abs (mau)
t (time)
BMIM 5MM 10% MEOH 1% HAC TRYPTOPHAN 0.1G/L
(A)
0 5 1 0 1 5 2 0 2 5 3 0 3 5 400
100
200
300
400
Abs (mau)
t ( t ime)
B M I M 5 M M 1 0 % M E O H 1 % H A C T R Y P T O P H A N 1 G / L
(B )
0 10 20 30 40 500
10
20
30
40
50
60
70BMIM 5MM NO MEOH 1% HAC TRYPTOPHAN 0.1G/L
Abs (mau)
t (time) (C)
0 10 20 30 400
50
100
150
200
250
300BMIM 5MM NO MEOH 1% HAC TRYPTOPHAN 1G/L
Abs (mau)
t (time) (D)
0 1 2 3 4 50
50 0
1 0 0 0
1 5 0 0
2 0 0 0
2 5 0 0
3 0 0 0
3 5 0 0
A b s ( m a u )
t ( t ime)
B M I M 5 M M N O M E O H 1 % H A C T R Y P T O P H A N 1 0 G / L
(E )
0 10 20 30 40 5 00
20
40
60
80
100B M I M 1 0 M M 1 O % M E O H 1 % H A C T R Y P T O P H A N 0 .1 G / L
A b s ( m a u )
t ( t ime) (F)
0 5 1 0 1 5 2 0 2 5 3 00
1 0 0
2 0 0
3 0 0
40 0
5 0 0
A b s ( m a u )
t ( t i m e )
B M I M 1 0 M M 1 0 % M E O H 1 % H A C T R Y P T O P H A N 1 G /L
(G )
0 5 1 0 1 5 2 0 2 50
1 0 0
2 0 0
3 0 0
40 0
5 0 0
6 0 0 B M I M 1 0 M M 1 0 % M E O H 1 % H A C T R Y P T O P H A N 1 0 G / L
A b s ( m a u )
t ( t im e ) (H )
0 10 20 30 40 500
10
20
30
40
50
60BMIM 10MM NO MEOH 1% HAC TRY PTOPHAN 0.1G/L
Abs (mau)
t (time) (I)
0 10 20 30 40 50
0
50
100
150
200
250BMIM 10MM NO MEOH 1% HAC TRYPTOPHAN 1G/L
Abs (mau)
t (time) (J)
0 10 20 30 40
0
50
100
150
200
250
300
Abs (mau)
t (time)
BMIM 5MM NO MEOH 1% HAC TRYPTOPHAN 10G/L
(K)
Figure 12: The effect of concentration of BMIM in mobile phase on the overloaded band profiles of tryptophan A-B: BMIM 5mM 1 %
MEOH, C-E:BMIM 5mM No MEOH;F-H:BMIM 1 mM 1 % MEOH;I-K:BMIM 1 mM No MEOH;Column: C18 Prevail, Flow
rate: 1. ml/min, Wavelength: 3 5 and 31 for tryptophan 1 gand 1 g/L respectively
8/7/2019 SATHISH PRASAD
36/46
Parameters of the polynomial fit for the different
concentrations of BMIM in the mobile phase
Mobile phase C(g/L) Parameters of polynomifit : y=a+bx+cx2+dx3a b c d
No IL No MeOH
1%HAC
0.1g/L
10 g/L
1 g/L
-5.046* 2.0351* 2.386* -1.618*
-0.0452 0.00661 -6.865* 1.143
-1.521* 1.52101* 1.521 1.22701
BMIM 5 mM 10%MeOH 1%HAC
0.1 g/L
1 g/L
10 g/L
-1.656 4.497 -1.418 2.438
8/7/2019 SATHISH PRASAD
37/46
8/7/2019 SATHISH PRASAD
38/46
0 100 200 300 400
0.00
0.02
0.04
0.06
0.08
0.10
C (g/L)
Abs (mau)
BMIM 5MM 10% MEOH 1% HAC TRYPTOPHAN 0.1G/L
(A)0.0 0.1 0.2 0.3 0.4 0.5
0.0
0.2
0.4
0.6
0.8
1.0
C (g/L)
t (time)
BMIM 5MM 10% MEOH 1% HAC TRYPTOPHAN 1G/L
(B) 0 200 400 600 800 1000
0.0
0.2
0.4
0.6
0.8
C (g/L)
Abs (mau)
BMIM 5MM 10% MEOH 1% HAC TRYPTOPHAN 10G/L
(C)
40 60 80 100 120 140
0.03
0.04
0.05
0.06
0.07
0.08
0.09
C (g/L)
Abs (mau)
BMIM 5MM NO MEOH 1% HAC TRYPTOPHAN 0.1G/L
(D)
200 300 400 500 600 700 8000.2
0.3
0.40.5
0.6
0.7
0.8
0.9
1.0
1.1
C (g/L)
Abs (mau)
BMIM 5MM NO MEOH 1% HAC TRYPTOPHAN 1g/L
(E) 400 500 600 700 800 900 1000110012002
3
4
5
6
7
8
9
10
11
C (g/L)
Abs( mau)
BMIM 5MM NO MEOH 1% HAC TRYPTOPHAN 10G/L
(F)0 20 40 6 0 8 0 100 120 140
0.00
0.02
0.04
0.06
0.08
0.10
C (g/L)
Abs (mau)
BMIM 10MM 10% MEOH 1% HAC TRYPTOPHAN 0.1G/L
(G)
0 100 200 300 400 500 600 700
0.0
0.2
0.4
0.6
0.8
1.0
C (g/L)
Abs (mau)
BMIM 10MM 10% MEOH 1% HAC TRYPTOPHAN 1G/L
(H)
0 200 400 600 800 1000 1200
0
2
4
6
8
10
C (g/L)
Abs (mau)
BMIM 10MM NO MEOH 1% HAC TRYPTOPHAN 10G/L
(L) - 10 0 0 1 00 2 0 0 30 0 40 0 5 00 6 0 0 70 0
0.0
0.2
0.4
0.6
0.8
1.0
C (g/L)
Abs (mau)
BMIM 10MM NO MEOH 1% HAC TRYPTOPHAN 1G/L
(K)
0 20 40 60 80 100 1200.00
0.02
0.04
0.06
0.08
0.10
C (g/L)
Abs (mau)
BMIM 10MM NO MEOH 1% HAC TRYPTOPHAN 0.1G/L
(J)
Figure 1 : Calibration curves of tryptophan determined by FA with different concentrations of
BMIM on C18 Prevail column. TryptophanA-C: BMIM 5 mM 1 % MeOH: D-F: BMIM 5 mM No MeOH; G-I: BMIM 1 mM 1 %
MeOH; J-L: BMIM 1 mM No MeOH; Flow rate 1. mL/ min; Wavelength 3 5 nm and room temperature. Mobile phases: 1 -1 % (v/v)
mixtures of methanol, acetic acid and HPLC water.
8/7/2019 SATHISH PRASAD
39/46
8/7/2019 SATHISH PRASAD
40/46
8/7/2019 SATHISH PRASAD
41/46
0 200 400 600 800 1000-0.1
0.0
0.1
0.2
0.3
0.4
0.5
0.6
0.7
0.8
C (g/L)
t (time)
BMIM 5MM TRYP 0.4 MIN 1g/L
(A)
-200 0 200 400 600 800
0
1
2
3
4
C (g/L)
t (time)
BMIM 5MM TRYP 0.4 MIN 10g/L
(B)0 200 400 600 80010001200140016001800
0.00
0.01
0.02
0.03
0.04
0.05
0.06
0.07
0.08
C (g/L)
t (time)
BMIM 5MM 10% MEOH 0.5 min 0.1g/L
(C)
-500 0 500 1000 1500 2000 2500 3000
-0.01
0.00
0.01
0.02
0.03
0.04
0.05
BMIM 10MM NO MEOH 0.1g/L 0.5 min
C (g/L)
t (time) (D)
600 800 1000
0.00
0.02
0.04
0.06
0.08
C (g/L)
t (time)
BMIM 10MM 10% MEO H 0.1g/L 0.5 min
(F) -500 0 500 1000 1500 2000 2500
0.000
0.005
0.010
0.015
0.020
0.025
0.030
C (g/L)
t (time)
BMIM 5MM NO MEO H 0.5 min 0.1g/L
(G)
-500 0 500 10001500200025003000
0.00
0.05
0.10
0.15
0.20
0.25
0.30
C (g/L)
t (time)
BMIM 10MM NO MEOH 1g/L 0.5 min
(H)
Figure 17 :Experimental (dotted) and the calculated of profiles (solid lines) with different concentrations of Tryptophan and
Phenylalanine on C18 X-terra column. Flow rate 1. mL/ min; Wavelength 3 5 nm and Room temperature. Mobile phases: 1 -1 %
(v/v) mixtures of methanol, acetic acid without methanol.
8/7/2019 SATHISH PRASAD
42/46
CONCLUSION
The adsorption isotherm behavior of tryptophan depends on the composition of
mobile phase and concentration of Ionic liquid used.
Inverse method was used to calculate adsorption parameters. Here it is important
to choose a good isotherm model.
The model can be guessed from the shape of the overloaded band profiles.
This method is useful for purification process and in the industrial field because
the parameters for adsorption isotherm is known in a very short time when
compared to that of Frontal analysis.
Our results indicate that the shape of the profiles, the isotherms, and the retention
of tryptoph
an are affected by the amount of IL added to t
he mobile p
hase.
The amount of analyte adsorbed on the column and the retention factor can be
manipulated by changing the amount of BMIM in the mobile phase.
Mobile phase containing no methanol as modifier and containing only BMIM can
be used as mobile ph
ase to elute tryptoph
an
8/7/2019 SATHISH PRASAD
43/46
REFERENCES:
. D.Rogers, R.Kenneth, A Chem.Soc, 856 (2003) 3-21
J.Matyn, R.Kenneth, Pure Appl.Chem, 72, (2000) 1391-1398A.Berthod, M.J.Ruin-Angel, J.chromatogr. A.1184 (2008) 6-1
Y. Wang, T.Minglei, Int.J.Mol.sci.10, (2009) 2591-2610
L.Anderson, Daniel W.Armstrong,A Chem.Soc (2006) 2893-2902
F.V Rantwijk, Roger, Chem rev, 107 (2007) 2757-2785
M.J Ruiz-Angel, A.Berthod, J.chromatogr, 1189 (2008) 476-482
http://www.directindustry.com/prod/shimadzu-europe/high-performance-liquid-chromatograph- hplc-system-
25210-56987.html
T.L.Greanes, Calamun, Chem, Rev, 108 (2008) 206C.Baudequin, D.Brigon, Tetrahedron: Asymmetry, 16 (2005)3921
C. F.Poole, J . Chromatogr, 1037 (2004) 49-82
R.Gabriele, Jurgen, J.Chemical physics, 128 (2008) 154509-1 154509-7
C. Chiappe and Daniela, J.Physical Chemistry, 18 (2005) 275-297
M.H Abraham,; W.E Acree, Green Chem., 8 (2006) 906
HL. Ngo, K. Le Compte, Therochim.Acta357 (2000) 97-102
.Okoturo, TJ. Vandernoot, J.Electroanal.Chem 105 (2001) 4603-4610
G. Law, Watson PR.Langmuir, J.Chromatogra 17(2001)6138-6141M.Deetlefs, M.shara, ACS, Washington DC, 901(2005)219-223
R.P Swatloski, J.D.Holbrey, Green chem., 5(2003)361
Simon M.Mwongela, Abdulqawi Numan, Anal chem. 75(2003)6089-6096
Merike Vaher, Maria Borissova, Proc.EstonianAcad.Chem, 56(2007)187-198
Yuanhong Xu, Erkang Wang, J.of chromatography A, 1216(2009)4817-4823
8/7/2019 SATHISH PRASAD
44/46
Yanes, E. G., Gratz, S.R., Baldwin, M.J., Robinsos, S.E., Anal.chem. 73(2001)3838
Schnee, V.P, Baker, Electrophoresis, 27(2006)4141-4234
Andrew P.Abbott and Katy, Phys chem8 (2006)4265-4279
Siddhartha pandey, Analytica chimica Acta (2005)1-8
Dandan Han and kyung, Molecules 15(2010) 1420-3045Stepnowski,P.,Nichthauser,J.,Mrozik,w.,Buszewski,B.,Anal.Bioanal.Chem.,385(2006)148
P.Stepnowski, Int.J.Mol.sci.7 (2006)497-509
Yulia Polyakova, Yoon Mo, biotechnology and bioprocess engineering, 11(2006)1-6
Wang, Q., Baker, G.A., Baker, S.N., and Colon, L.A., Analyst, 131(2006)1000-1005
Shu Juan LIU, Feng ZHOU, Chinese chemical letters vol.15 (2004)1060-1062
Hisham Hashem, Thomas Jira J.of chromatography A, 1133(2006)69-75
Hagiwara, R.; Ito, Y. J. Fluorine Chem.105 (2000)221-227
Mosel, Principles of adsorption and reaction on solid surfaces, Wiley, New York, 1996.F. Gritti, W. Piatkowski and G. Guiochon, J Chromatogr A. 978 (2002) 81.
A. Cavazzini, G. Bardin, K. Kaczmarski, P. Szabelski, M. Al-Bokari and G.Guiochon, J Chromatogr A. 957 (2002)
111.
W. Piatkowski, D. Antos, F. Gritti and G. Guiochon, J Chromatogr A. 1003 (2003)
A. Felinger, A. Cavazzini and G. Guiochon J Chromatogr A. 986 (2003) 207.
G. Zhong, P. Sajonz and G. Guiochon, Ind Eng Chem (Res.) 36 (1997) 506.
B.J. Stanley, P. Szabelski, Y.B. Chen, B. Sellergren and G. Guiochon, Langmuir 19(2003)772.
G. Schay and G. Szekely, Acta Chim Hung, 5 (1954) 167.A. Cavazzini, A. Felinger and G. Guiochon, J Chromatogr A. 1012 (2003) 139
8/7/2019 SATHISH PRASAD
45/46
J.D. Andrade, Surface and Interfacial Aspects of Biomedical Polymers, Plenum Press, New York, NY, 1985.F. Gritti, G. Guiochon, J. Chromatogr. A. 1028 (2004) 105.
C.H. Jin, Y.M. Koo, D. Choi and K.H. Row, Biotechnol. Bioprocess Eng. 12 (2007)525
S.S. Adams, J Clin Pharmacol. 32 (4) (1992) 31723.
F. Gritti and G. Guiochon, J. Chromatogr. A. 1099 (2005) 142.
F. Gritti and G. Guiochon, J. Chromatogr. A. 1041 (2004) 6375.
F. Gritti and G. Guiochon, J. Chromatogr. A. 1028 (2004) 197210.
F. Gritti and G. Guiochon, J. Chromatogr. A. 1033 (2004) 5769.
T. Ahmad and G. Guiochon, J. Chromatogr. A. 1114 (2006) 111122
T. Minglei, L. Junyu and Kyung Ho Row, Molecules, 14, (2009) 2127-2134
V. Antonio, J. Hernandez, A. Miguel, Anal Bioanal Chem, 392 (2008) 1439-1446
8/7/2019 SATHISH PRASAD
46/46
THANK YOU
Top Related