Biochemical and Biophysical Research Communications
Regular ArticleFTIR Study of Horseradish Peroxidase in Reverse Micelles
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Cited by (17)
Comparison of structures of walnut protein fractions obtained through reverse micelles and alkaline extraction with isoelectric precipitation
2019, International Journal of Biological MacromoleculesCitation Excerpt :Reverse micelles can simultaneously separate the oil and protein from oil-containing materials, and allow easy scale-up [14]. Several papers have been reported the effect of reverse micelles on protein structure [15,16]. Hu et al. [17] also found that the reverse micelles could change the functional properties and surface structure of walnut proteins.
FTIR spectroscopic characterization of soy proteins obtained through AOT reverse micelles
2013, Food HydrocolloidsCitation Excerpt :But the intensity of peaks in reverse micelles increased. The result indicated that the secondary structures of soy proteins might be partly destroyed in the AOT reverse micelles (Chen et al., 2001). The quantity of peak area and contents of the corresponding protein secondary structure were given in Table 2.
Infrared spectroscopy of proteins in reverse micelles
2013, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :Huang et al. found that the degree to which bovine pancreatic RNAse A underwent conformational change was greater at low values w0 (study performed in H2O) [24]. Chen et al. examined the effect of surfactant type on the amide I′ spectrum of horseradish peroxidase and found that AOT preserved protein structure better than CTAB and SDS [6]. Further studies of α-chymotrypsin in CATB reverse micelles were performed by Celej et al., who found that encapsulation increased α-helix content, and decreased β-sheet content — correlating with increased enzymatic activity [4].
Investigation of structural effects and behaviour of Pseudomonas aeruginosa amidase encapsulated in reversed micelles
2012, Process BiochemistryCitation Excerpt :Therefore, specific activity of amidase is lower in the conventional buffer medium due to the high water content which favors the amidase hydrolysis reaction as opposed to the acetohydroxamic acid synthesis [2]. Nevertheless, the microenvironment in which the enzyme is solubilized in reverse micelles has physico-chemical properties distinct from a bulk aqueous solution which can alter protein structure and therefore with the biocatalytic activity [16,24–26]. Structure–function relationships of the enzyme in both media were further evaluated in order to fully understand these results.
Kinetics of reactions catalyzed by enzymes in solutions of surfactants
2008, Advances in Colloid and Interface ScienceCitation Excerpt :On the other hand, it has been shown that the presence of nonionic surfactants relieves protein denaturation caused by electrostatic interactions [64,65]. The secondary structure of horseradish peroxidase (HRP) in AOT RM, and in CTAB and SDS media, has been determined [57] utilising FTIR spectroscopy. The structure of HRP in AOT RM was the closest one to that in aqueous solution while, in CTAB and SDS systems, the spectra were much different, indicating that the enzyme structure has been partly destroyed by the microenvironment provided by the surfactants.
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