Extraction of bovine serum albumin using nanoparticulate reverse micelles

Hebbar, H. Umesh; Raghavarao, K.S.M.S.

doi:10.1016/j.procbio.2007.08.010

Cited by 50 publications

(26 citation statements)

References 31 publications

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“…This result was due to that the water uptake by reverse micelles was affected by the surfactants. The forward extraction efficiency was governed primarily by electrostatic interactions between the charged protein and polar head of surfactant (Leser and Luisi 1989) and was also affected by hydrophobic interactions between the non-polar region of the protein and surfactant tail (Rajib and Bidyut 2005;Umesh Hebbar and Raghavarao 2007). It indicated that reverse micelles could affect the extraction efficiency of proteins from soybean flour.…”

Section: Effect Of Surfactants On Protein Structure In Reverse Micellesmentioning

confidence: 99%

“…The reason might be contributed to the environment changes of soy protein. Firstly, the unusual properties of water localized in the interior of reverse micelles could bring about stronger interaction with the charged groups of protein, and influence conformation of the soy protein (Rajib and Bidyut 2005;Umesh Hebbar and Raghavarao 2007). Secondly, the interaction of surfactant and soy protein could change not only the protein structures, but also the band frequency of CD spectra.…”

Section: Effect Of Surfactants On Protein Structure In Reverse Micellesmentioning

confidence: 99%

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Conformation Analysis of Soybean Protein in Reverse Micelles by Circular Dichroism Spectroscopy

Zhao

et al. 2010

Food Anal. Methods

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Far-UV circular dichroism (CD) spectroscopy was used to study the conformation of protein from soybean flour under the influence of various reverse micelle environments and salt treatments, as compared with the protein using aqueous buffer extraction. These proteins exhibited characteristic CD spectra that reflected a considerable amount of residual secondary structures. The CD analysis showed that the protein modification by reverse micellar system was related to loss of α-helix and β-structure and increase of random coil. The ellipticity of protein in bis (2-ethylhexyl) sodium sulfosuccinate (AOT) and sodium dodecyl sulfate (SDS) reverse micelles was higher than in hexadecyl trimethyl ammonium bromide (CTAB) and TrionX-100. The CD spectra in reverse micelles except for SDS at 210 nm had lower intensity than in aqueous solution. Salts could influence the ellipticity of protein at near 194 nm in an order of NaCl>KNO 3 >>KCl>NaNO 3 >Na 2 SO 4 in monovalent salts and in MgCl 2 >BaCl 2 >CaCl 2 divalent ones. Besides, the ellipticity was totally higher in monovalent salts than in divalent ones.

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Section: Effect Of Surfactants On Protein Structure In Reverse Micellesmentioning

confidence: 99%

Section: Effect Of Surfactants On Protein Structure In Reverse Micellesmentioning

confidence: 99%

Conformation Analysis of Soybean Protein in Reverse Micelles by Circular Dichroism Spectroscopy

Zhao

et al. 2010

Food Anal. Methods

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“…To date, the reverse micelle (RM) technique has been used in the manufacture of numerous devices and applications. Typical examples include carbon monoxide detection [29], purification [30], extraction systems [31], pharmaceutical [32] and electronic devices [33].…”

Section: Introductionmentioning

confidence: 99%

Fine-tuning of catalytic tin nanoparticles by the reverse micelle method for direct deposition of silicon nanowires by a plasma-enhanced chemical vapour technique

Poinern

Fawcett

2010

Journal of Colloid and Interface Science

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. AbstractThe reverse micelle method was used for the reduction of a tin (Sn) salt solution to produce metallic Sn nanoparticles ranging from 85 nm to 140 nm in diameter. The reverse micellar system used in this process was hexane-butanol-cetyl trimethylammonium bromide (CTAB). The diameters of the Sn nanoparticles were proportional to the concentration of the aqueous Sn salt solution. Thus, the size of the Sn nanoparticles can easily be controlled, enabling a simple, reproducible mechanism for the growth of silicon nanowires, (SiNWs) using plasma-enhanced chemical vapour deposition (PECVD). Both the Sn nanoparticles and silicon nanowires were characterised using field-emission scanning electron microscopy (FE-SEM). Further characterisations of the SiNW's were made using transmission electron microscopy (TEM), atomic force microscopy, (AFM) and Raman spectroscopy. In addition, dynamic light scattering (DLS) was used to investigate particle size distributions. This procedure demonstrates an economical route for 2 manufacturing reproducible silicon nanowires using fine-tuned Sn nanoparticles for possible solar cell applications.

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“…Reverse micelles provide mild separation conditions for enzyme recovery in an active form [8][9][10][11][12][13]. By appropriate manipulation of process parameters such as solution pH, ionic strength, and phase volume ratio, it is possible to obtain the purification and concentration of the desired enzyme in a single step [14].…”

Section: Introductionmentioning

confidence: 99%

Reverse Micellar Extraction of β-Galactosidase from Barley (Hordeum vulgare)

Hemavathi

Hebbar

Raghavarao

2008

Appl Biochem Biotechnol

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The reverse micellar system of sodium bis(2-ethylhexyl)sulfosuccinate (AOT)/isooctane was used for the extraction and primary purification of beta-galactosidase (EC 3.2.1.23) from the aqueous extract of barley (Hordeum vulgare) for the first time. The process parameters such as the concentration of the surfactant, the volume of the sample injected, and its protein concentration, pH, and ionic strength of the initial aqueous phase for forward extraction, buffer pH, and salt concentration for back extraction are varied to optimize the extraction efficiency. Studies carried out with both phase transfer and injection mode of reverse micellar extraction confirmed the injection mode to be more suitable for beta-galactosidase extraction. The extent of reverse micellar solubilization of proteins increased with an increase in protein concentration of the feed sample. However, back extraction efficiency remained almost constant (13-14.4%), which indicates the selectivity of AOT reverse micelles for a particular protein under given experimental conditions. beta-Galactosidase was extracted with an activity recovery of 98.74% and a degree of purification of 7.2-fold.

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Extraction of bovine serum albumin using nanoparticulate reverse micelles

Cited by 50 publications

References 31 publications

Conformation Analysis of Soybean Protein in Reverse Micelles by Circular Dichroism Spectroscopy

Conformation Analysis of Soybean Protein in Reverse Micelles by Circular Dichroism Spectroscopy

Fine-tuning of catalytic tin nanoparticles by the reverse micelle method for direct deposition of silicon nanowires by a plasma-enhanced chemical vapour technique

Reverse Micellar Extraction of β-Galactosidase from Barley (Hordeum vulgare)

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