fourier transform infrared spectroscopy (ftir ) spectral ... · and, ftir spectral analysis of the...

Research Journal of Chemical

Vol. 6(2), 29-36, February (201

International Science Community Association

Fourier Transform Infrared Spectroscopy

Nanoparticles (BSA NPs) and Egg Albumin Nanoparticles (EA NPs)

Amity Institute of Biotechnology, Amity

Available online at: Received 28th January

Abstract

Advance protein based nanobiotechnology are now, known for its advanced approach to synthesize various nanomaterials

using various newly developed chemical and green technologies to carry out their applications in various fields of life

sciences. Now these days, Bovine serum albumin nanoparticles (BSA NPs) are very popular as non

vehicle systems for drug delivery used in number of therapeutic strategies to be considered in combating cancers, tumors,

hormone associated and neurodegenerative disease. The albumin nanoparticles e.g. bovine serum albumin nanoparticles

(BSA NPs) and egg albumin nanopartic

desolvation process to get desired particle size at nanosacle e.g. range between 100 to 300 nm with minimal size distribution

The size controlled BSA and egg albumin nanoparticles ca

and non-viral biocompatible nanodevice and nanovehicle carrier for loading of desired drug/ biological active ingredients/

hormones molecules/ chimeric-DNA with efficient target delivery sys

using emulsified and desolvation method are done via glutaraldehyde coupling for loading of

found to be better eco-friendly and cost

Sometimes, the metalonanoparticles or nanomaterials are found to be very costly and toxic because of their slow natural

degradation in host and their chemically driven synthesis. Hence, the synthesis of bio

might be used for their further consideration for their safe and non

technology, biomedical approaches and pharmaceutical industry for the treatment of various diseases. Hence, this d

Fourier Transform Infrared Spectroscopy

albumin nanoparticles (BSA NPs) and egg albumin nanoparticles (EA NPs) and their active functional groups and chemical

interactions for loading desired biological components or drugs that can might be further considered to increase their safe

and cost effective therapeutic viability.

Keywords: Bovine serum albumin nanoparticles, Egg albumin nanoparticles, BSA NPs, EA NPs,

Emulsification method, Cicer arietinum amylase, Drug delivery, FTIR.

Introduction

Fine particles are considered to be known which are sized inbetween 100 and 2,500 nanometers and ultrafine particles are purely called nanoparticles which were found to be in the range of 1-100 nanometers in size

1,2. These days, protein based

nanotechnology are very much considered to the research and

technological developments at atomic, molecular and macromolecular scales to prepare synthetic polymers together with the absorbability and low toxicity of the degradation end

products3,4

. Silver-poly(methylmethacrylate) (Ag/PMMA) nanocomposites were prepared via in-situ polymerization technique using N,N’-dimethylformamide (DMF) and

characterized by Fourier transform infrared spectroscopy (FTIR)

to know the details of active functional groups present in the synthesized PMMA

5. FTIR spectra of silver nanoparticles was

also found to be observed to have exhibited prominent peaks at

2,927, 1,631, and 1,383 cm−1

which showed sharp and strong absorption band at 1,631 cm

−1 assigned to the stretching

Chemical Sciences _______________________________________

(2016)

Association

Fourier Transform Infrared Spectroscopy (FTIR) Spectral Analysis of BSA


Kirti Rani Amity Institute of Biotechnology, Amity University Uttar Pradesh, Noida, Sec-125, Noida-201303,

[email protected]

Available online at: www.isca.in, www.isca.me, www.isca.me January 2016, revised 2nd February 2016, accepted 16th February 201

Advance protein based nanobiotechnology are now, known for its advanced approach to synthesize various nanomaterials

using various newly developed chemical and green technologies to carry out their applications in various fields of life

sciences. Now these days, Bovine serum albumin nanoparticles (BSA NPs) are very popular as non

r drug delivery used in number of therapeutic strategies to be considered in combating cancers, tumors,


(BSA NPs) and egg albumin nanoparticles (EA NPs) are easily prepared by number of established emulsified and

desolvation process to get desired particle size at nanosacle e.g. range between 100 to 300 nm with minimal size distribution

The size controlled BSA and egg albumin nanoparticles can be used as the standard cost effective, non

viral biocompatible nanodevice and nanovehicle carrier for loading of desired drug/ biological active ingredients/

DNA with efficient target delivery system. As well as, fabrication of BSA NPs and EA NPs by

using emulsified and desolvation method are done via glutaraldehyde coupling for loading of Cicer arietinum

friendly and cost-effective choice as compared to synthesis of other metal based nanoparticles.


degradation in host and their chemically driven synthesis. Hence, the synthesis of bio-compatible

might be used for their further consideration for their safe and non-toxic therapeutic applications in fields of biosensor

technology, biomedical approaches and pharmaceutical industry for the treatment of various diseases. Hence, this d

Fourier Transform Infrared Spectroscopy (FTIR) analysis was used to determine the purity of the prepared bovine serum


s for loading desired biological components or drugs that can might be further considered to increase their safe

Bovine serum albumin nanoparticles, Egg albumin nanoparticles, BSA NPs, EA NPs,

amylase, Drug delivery, FTIR.

Fine particles are considered to be known which are sized in-between 100 and 2,500 nanometers and ultrafine particles are purely called nanoparticles which were found to be in the range

. These days, protein based

gy are very much considered to the research and

technological developments at atomic, molecular and macromolecular scales to prepare synthetic polymers together with the absorbability and low toxicity of the degradation end

ethacrylate) (Ag/PMMA) situ polymerization

dimethylformamide (DMF) and

characterized by Fourier transform infrared spectroscopy (FTIR)

to know the details of active functional groups present in the FTIR spectra of silver nanoparticles was

also found to be observed to have exhibited prominent peaks at

which showed sharp and strong assigned to the stretching

vibration of (NH) C=O group; developed band 1,383 for Cand C–N stretching; observed sharp peak at 2,927

assigned to C–H and C–H (methoxy compounds) stretching vibration

6. FTIR spectra was also used for characterization of

ZnO nanoparticles. Infrared studies wer

ascertain the purity and nature of the metal nanoparticles that had observed peak at 3452.30 and 1119.15 cm

present due to O-H stretching and deformation. Other observed peaks at 1634.00 and 620.93 cm

correspond the Zn-O stretching and deformation vibration, respectively

7.

And, FTIR spectral analysis of the iron oxide nanoparticles and microgel magnetic particles were also reported to characteristic

the absorption band of Fe–O bond of bulk Fecm−1 to reduced the size of prepared nanoparticles to nanoscale dimensions

8. The molecular characteristics of the resulting BSA

NPs were also characterized by FTIR to have sharp FTIR peaks at 3385 cm-1 , 3113 cm-1, 1707 cm

___________E-ISSN 2231-606X

Res. J. Chem. Sci.

29

) Spectral Analysis of BSA


201303, UP, India

2016

Advance protein based nanobiotechnology are now, known for its advanced approach to synthesize various nanomaterials by

using various newly developed chemical and green technologies to carry out their applications in various fields of life-

sciences. Now these days, Bovine serum albumin nanoparticles (BSA NPs) are very popular as non-toxic and nonviral

r drug delivery used in number of therapeutic strategies to be considered in combating cancers, tumors,


les (EA NPs) are easily prepared by number of established emulsified and

desolvation process to get desired particle size at nanosacle e.g. range between 100 to 300 nm with minimal size distribution.

n be used as the standard cost effective, non-toxic, non-allergic

viral biocompatible nanodevice and nanovehicle carrier for loading of desired drug/ biological active ingredients/

tem. As well as, fabrication of BSA NPs and EA NPs by

Cicer arietinum amylase that

s of other metal based nanoparticles.


compatible BSA NPs and EA NPs

toxic therapeutic applications in fields of biosensor

technology, biomedical approaches and pharmaceutical industry for the treatment of various diseases. Hence, this designed

(FTIR) analysis was used to determine the purity of the prepared bovine serum


s for loading desired biological components or drugs that can might be further considered to increase their safe

Bovine serum albumin nanoparticles, Egg albumin nanoparticles, BSA NPs, EA NPs, Desolvation method,

C=O group; developed band 1,383 for C–C N stretching; observed sharp peak at 2,927 cm

−1 that

H (methoxy compounds) stretching . FTIR spectra was also used for characterization of

ZnO nanoparticles. Infrared studies were carried out in order to

ascertain the purity and nature of the metal nanoparticles that had observed peak at 3452.30 and 1119.15 cm-1 which may be

H stretching and deformation. Other observed peaks at 1634.00 and 620.93 cm-1 were also reported to

O stretching and deformation vibration,

And, FTIR spectral analysis of the iron oxide nanoparticles and microgel magnetic particles were also reported to characteristic

O bond of bulk Fe3O4 at 570 and 375 −1 to reduced the size of prepared nanoparticles to nanoscale

. The molecular characteristics of the resulting BSA NPs were also characterized by FTIR to have sharp FTIR peaks

1, 1707 cm-1 , 1533 cm-1 and 1242

Research Journal of Chemical Sciences __________________________________________________________E-ISSN 2231-606X

Vol. 6(2), 29-36, February (2016) Res. J. Chem. Sci.

International Science Community Association 30

cm-1 that are assigned to the stretching vibration of OH, amide A (mainly NH stretching vibration), amide I (mainly C=O

stretching vibrations), amide II (the coupling out phase of

bending vibration of N-H and stretching vibration of C-N

bands) and amide III (is in the phase combination of N-H in plane bending and C-N stretching)

9. Revioulsy, various

techniques e.g. desolvation, emulsification, thermal gelation, nanospary drying, nab-technology and self-assembly techniques

were used for the preparation of albumin nanoparticles which do

not require high temperature and therefore may be useful when

heat-sensitive bioactive compounds are designed to be

immobilized into fabricated albumin nanoparticles10

.

Hence, protein nanoparticles are observed to be an attractive

biomolecule which have their unique characteristic including

biodegradability, nontoxicity, metabolized in vivo to produce

innocuous degradation products, water solubility, simplicity in

purification and nonimmunogenic nature that allow their ease of controlled and targeted delivery as an ideal nanopreparation

11.

And, desolvation methods are found to be reported more advantageous over emulsification method to prepare albumin nanoparticles due to avoidance of organic solvents to remove the used oily residues and surfactants which are required for the emulsion stabilization. Desolvation technique was found to be more cost effective to prepare more small sized, thermo-stabilized, storage-stabilized nanoparticles with their reported significant alkaline protease mediated controlled biodegradation and increased shelf life period over upto 12-14 months

11,12.

Previously, the enzyme immobilization was also reported into those prepared BSA NPs

13 and EA NPs

14,15 nanoparticles which

were more cost effective, eco-friendly biocompatible, non-toxic, non-allergic and non-corrosive enzyme loading carrier by using desolvation method

11 and emulsification method

12 to make them

more industrially viable11-15

. Hence, this concrete Fourier Transform Infrared Spectroscopy (FTIR) spectral analysis was used for the interpretation of prepared purity of the prepared bovine serum albumin nanoparticles (BSA NPs)

11 and egg albumin nanoparticles (EA

NPs) by desolvation method13

; bovine serum nanoparticles (BSA NPs)

12 and egg albumin nanoparticles (EA NPs) by

emulsification method14.

As well as, their active functional groups and molecular interactions were also assigned to get to

know the altered chemical interactions in prepared BSA NPs11,12

and EA NPs13-15

before and after the glutaraldehyde activation

that were further used for desired Cicer arietinum amylase immobilization to be used for their controlled alkaline protease mediated bioproteolysis and effective washing study. So, FTIR analysis was used to carried for the functional chemical interactions of prepared BSA NPs and EA NPs which can might

be exploited for their further inevitable use to load the desired drug/ biological active ingredients/ hormones molecules/

chimeric-DNA with efficient target delivery system as cost effective, non-toxic, non-allergic and non-viral biocompatible nanodevice and nanovehicle carriers. That may become a

landmark in non-toxic therapeutic applications especially in fields of biosensor technology, biomedical approaches and

pharmaceutical industry for the treatment of various diseases (cancer, tumors, hormone-associated and neurodegenerative

disorders) as green clinical therapeutic technology.

Materials and Methods

Preparation of BSA NPs and Cicer arietinum amylase loaded

BSA nanoparticle (Amylase-BSA NPs) by Deslovation

method: BSA NPs and Amyalse-BSA NPs were prepared by

desolvation method by using n-butanol given 2012 and Rani K

& Chauhan C, 201511

.

Preparation of BSA NPs and Cicer arietinum amylase loaded

BSA nanoparticle (Amylase-BSA NPs) by Emulsification

method: BSA NPs and Amyalse-BSA NPs were prepared by

Emulsification method by using coconut oil as natural

occurring emulsifier given Rani K & Chauhan C, 201512

.

Preparation of EA NPs and Cicer arietinum amylase loaded

Egg Albumin nanoparticle (Amylase-BSA NPs) by

Deslovation method: EA NPs and Amyalse-EA NPs were

prepared by desolvation method by using toluene given by Rani

K, 201515

.

Preparation of EA NPs and Cicer arietinum amylase loaded

Egg Albumin nanoparticle (Amylase-BSA NPs) by

Emulsification method: EA NPs and Amyalse-EA NPs were

prepared by emulsification method by using using coconut oil as

natural occurring emulsifier with toluene and n-butanol, given

by 2012 and Rani K, 201513

.

Alkaline Protease Mediated Bioproteolysis of Prepared

Amylase-BSA NPs and Amylase-EA NPs11-15

: Amylase loaded

BSA NPs and EA NPs were also subjected to proteolysis with

standardized 35 U of alkaline protease to confirmed loading of

desired amylase into prepared active BSA NPs and EA NPs.

Characterization: Fourier Transform Infrared

Spectroscopy (FTIR) analysis of prepared BSA NPs and EA

NPs: The prepared BSA NPs and EA NPs; Amylase-BSA NPs

and Amylase-EA NPs were subjected for characterization to

Fourier Transform Infrared Spectroscopy (FTIR) analysis to

determine the purity of fabricated BSA NPs and EA NPs before

and after the immobilization done by glutaraldehyde coupling.

Designed FTIR spectroscopy was carried out to be scanned at

the range of 500-4000cm-19,16

.

Results and Discussion

Previously reported data of DLS and SEM for confirmed

BSA NPs and EA NPs by Rani K & Chauhan C, 2015; Rani, K, 2015

11-14:

Dynamic Light scattering (DLS) and Scanning

Electron Microscopy (SEM) of prepared BSA NPs and

Amylase-BSA NPs by desolvation method and emulsification

method were already reported by Rani K & Chauhan C, 2015, to

confirm the size of nanoparticles in the approximate range of




2nm to 11nm and 56nm to 107.4nm respectively11,12

. Dynamic

Light scattering (DLS) and Scanning Electron Microscopy

(SEM) results of prepared EA NPs and Amylase-EA NPs by

desolvation method and emulsification method were observed

by Rani K, 2015, to confirm the size of nanoparticles in the

approximate range of 5nm to upto 100nm and 101.2nm to

209nm respectively13,14

. The observed size of BSA NPs and

Amylase-NPs were found to be less than of EA NPs and

Amylase-EA NPs11-14

Those observation were also comparable

similar to other previous reports9,16-18

.

Fourier Transform Infrared Spectroscopy (FTIR) analysis

of prepared BSA NPs and Amylase-BSA NPs & EA NPs and Amylase-EA NPs: FTIR spectroscopy was used to determine

the purity of fabricated BSA NPs and EA NPs before and after

the immobilization of desired enzyme done by glutaraldehyde

coupling11-15

. It was scanned at the range, 500-4000 cm-1

9,16.


of prepared BSA NPs and Amylase-BSA NPs: The FTIR

peaks of prepared BSA NPs by using desolvation method11

before immobilization of amylase were observed at 3381 cm-1

that assigned to the stretching vibration of OH [amide A, mainly

NH stretching vibration]; at 2958 cm-1, at 2932 cm-1 and at

2873 cm-1 that approximate assigned C–H and C–H (methoxy

compounds) stretching vibration; at 1642 cm-1 and at 1292 cm-

1 that assigned to having approximate vibration of (NH) C=O

group and for C–C and C–N stretching respectively (Figure-1).

The FTIR peaks of BSA NPs after immobilization of amylase

were observed at 3388 cm-1 that assigned to the stretching

vibration of OH [amide A, mainly NH stretching vibration]; at

1649 cm-1 that assigned approximate the stretching vibration of

(NH) C=O group (Figure-2). Observed FTIR peaks at 2958 cm-

1, at 2932 cm-1 and at 2873 cm-1 were only observed in BSA

NPs before immobilization only (Figure-1) which confirmed

that immobilization of enzyme was done at these assigned

activated functional groups (Figure-2). These observations were

found to be comparably similar with previous FTIR analysis of

nanoparticles6,9,16-19

.

The FTIR peaks of BSA NPs by using emulsification method12

before immobilization of desired enzyme were observed at 3478

cm-1 that assigned to approximate stretching vibration of OH

[amide A, mainly NH stretching vibration]; at 2923 cm-1 and at

2854 cm-1 that assigned approximate C–H and C–H (methoxy

compounds) stretching vibration; at 1697 cm-1 that assigned to

having approximate vibration of (NH) C=O group and for C–C

and C–N stretching respectively (Figure-3). The FTIR peaks of

BSA NPs after immobilization of amylase were observed at

3566 cm-1 that assigned to have approximate possible stretching

vibration of OH [amide A, mainly NH stretching vibration]; at

1647 cm-1 that assigned approximate the stretching vibration of

(NH) C=O group; at 1369 cm-1 tha assigned to have possible

C–C and C–N stretching (Figure-4). Observed FTIR peaks at

2958 cm-1 and at 2854 cm-1 were only observed in BSA NPs

before immobilization only (Figure-3) which confirmed that

immobilization of enzyme was done at these assigned activated

functional groups (Figure-4). These reported were found to be

comparably similar with previous FTIR interpretation of

nanoparticles6,9,16,20

.

Figure-1

FTIR spectra of prepared activated BSA NPs by desolvation method before the immobilization of Cicer arietinum amylase




Figure-2

FTIR spectra of prepared activated BSA NPs by desolvation method after the immobilization having loaded Cicer arietinum

amylase (immobilization done by glutaraldehyde coupling)

Figure-3

FTIR spectra of prepared activated BSA NPs by emulsification method before the immobilization of Cicer arietinum

amylase




Figure-4

FTIR spectra of prepared activated BSA NPs by emulsification method after the immobilization having loaded Cicer

arietinum amylase (immobilization done by glutaraldehyde coupling)


of prepared EA NPs and Amylase-EA NPs: The FTIR peaks

of prepared EA NPs by using desolvation method13,15

before

immobilization of amylase were observed at 3364 cm-1 that

assigned to the possible stretching vibration of OH [amide A,

mainly NH stretching vibration]; at 2920 cm-1 that approximate

assigned C–H and C–H (methoxy compounds) stretching

vibration; at 1643 cm-1 that assigned to having approximate

vibration of (NH) C=O group (Figure-5). The FTIR peaks of EA

NPs after immobilization of amylase were observed at 1747 cm-

1 that assigned amide I (mainly C=O stretching vibrations)

(Figure-6). Observed FTIR peaks at 3364 cm-1, at 2920 cm-1

and at 1643 cm-1 were only observed in EA NPs before

immobilization only (Figure-5) which confirmed that

immobilization of amylase was done at those assigned activated

functional groups (Figure-6). These observations were found to

be very close to with previous observed FTIR analysis of

nanoparticles6,9,16,17-20

.

The FTIR peaks of EA NPs by using emulsification method13,14

before immobilization of amylase were observed at 3313 cm-1

that assigned to approximate stretching vibration of OH [amide

A, mainly NH stretching vibration]; at 1635 cm-1 that assigned

to having approximate vibration of (NH) C=O group; 1541 cm-

1 that assigned approximate possible amide II (the coupling out

phase of bending vibration of N-H and stretching vibration of C-

N bands) (Figure-7). The FTIR peaks of EA NPs after

immobilization of amylase were observed at 3309 cm-1 that

assigned to have approximate possible stretching vibration of

OH [amide A, mainly NH stretching vibration]; at 1635 cm-1

that assigned to having approximate vibration of (NH) C=O

group (Figure-8). Observed FTIR peak at 1541 cm-1 was only

observed in EA NPs before immobilization only (Figure-7)

which confirmed that immobilization of amylase was done at

those assigned activated functional group (Figure-8). And, these

observed FTIR finding were found to be comparable with that

of previous FTIR spectral observations of nanoparticles6,9,16-19

.

Conclusion

Hence, from this brief FTIR spectral analysis, it was concluded

that BSA NPs and EA NPs were successfully fabricated very

well by using process of desolvation as compared to

emulsification method. As well as, loading of Cicer arietinum

amylase into activated BSA NPs and EA NPs was also carried

out with the best ease of activated functional groups into BSA

NPS and EA NPs by desolvation method as compared to

emulsification method. So, present work may be helpful to

possible designing the used modified fabricated formulations for

the preparation of albumin nanoparticles and make it more

feasible for the effective immobilization and loading of

biological components such as enzyme, drug, antibody, peptide

and hormone molecules etc. And, these advanced fabricated

BSA NPs and EA NPs can be used for cost effective and

biocompatible nonviral nanovehicle as a rational nontoxic and

eco-friendly colloidal carrier for targeted delivery green method

that can be used in safe therapeutic approaches.




Figure-5

FTIR spectra of prepared activated EA NPs by desolvation method before the immobilization of Cicer arietinum amylase

Figure-6

FTIR spectra of prepared activated EA NPs by desolvation method after the immobilization having loaded Cicer arietinum

amylase (immobilization done by glutaraldehyde coupling)




Figure-7

FTIR spectra of prepared activated EA NPs by emulsification method before the immobilization of Cicer arietinum amylase

Figure-8

FTIR spectra of prepared activated EA NPs by emulsification method after the immobilization having loaded Cicer

arietinum amylase (immobilization done by glutaraldehyde coupling)




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