sathish prasad

8/7/2019 SATHISH PRASAD

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Presented by:

SATHISH

Chemistry Department.


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INTRODUCTION

IONIC LIQUIDS

COMPOSITION OF IONIC LIQUIDS

Figure 1: structure of ionic liquids[ BMIM]

.


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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


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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


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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


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IONIC LIQUIDS IN LIQUID CHROMATOGRAPHY

Figure 3: Scheme illustrating potential interactions between methylimidazolium cation and phenyl-basedreversed-phase stationary phase.

Reversed-phaseliquidchromatographicanalysisofionicliquids


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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


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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


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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.


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.


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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).


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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


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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


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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.


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ISOTHERM MODELS

y The figures below show that there are four common models for

isotherms.


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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


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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

!


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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!


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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)


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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.


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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.


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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


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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


Mm Ionic liquid with 1 % methanol and 1% acetic acid



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MECHANISM

Interactionof[BMIM]BF4 onmodifiedsilicasurface.


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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)


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.


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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)


0 2 4 6 8 10 120

100

200

300

400

500

Abs (mau)

t (time) (E)


0 3 6 9 12

0

200

400

Abs (mau)

t (time)(F)


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


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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.


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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)


0 200 400 600 800 1000 1200

0

2

4

6

8

10

C (g/L)

Abs (mau) (B)


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)


0 200 400 600 800 1000 1200

0

2

4

6

8

10

C (g/L)

Abs (mau) (D)


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)


(E)

0 200 400 600 800 1000 1200

0

2

4

6

8

10

C (g/L)

Abs (mau) (F)


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


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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


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[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.


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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.


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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


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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)


(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


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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


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0 100 200 300 400

0.00

0.02

0.04

0.06

0.08

0.10

C (g/L)

Abs (mau)


(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)


(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)


(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)


(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)


(H)

0 200 400 600 800 1000 1200

0

2

4

6

8

10

C (g/L)

Abs (mau)


(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)


(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.


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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.


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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


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. 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

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sathish prasad

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