ABSTRACT
Sodium dodecyl sulfate, (SDS) is an anionic surfactant that widely utilized in industry and households. Which represent toxic effects to the health and aquatic organisms. The bacterial strains Pseudomonas aeruginosa and Pseudomonas otitidis were isolated from the water samples from waste disposal sites (Taif Governate, Kingdom of Saudi Arabia). So, in the present study, we have made an attempt to improve the biodegradation of SDS by Pseudomonas aeruginosa and Pseudomonas otitidis by different methods such as mutation (Physically and chemically), physically by exposure of bacterial strains to ultraviolet radiation (UV) and chemically by using chemicals such as ethidium bromide (EtBr), also biodegradation rate of SDS can be increased by immobilization technique. The bacterial strains were immobilized in alginate beads, and its SDS degradation efficiency was observed to increase many fold than free strains.
ABSTRACT
Title: Effects of sodium dodecyl sulphate on enhancement of lipoxygenase activity of hemoglobin Authors: Ezebuo, F C Eze, S O O Chilaka, F C Keywords: Hemoglobin Linoleic acid Lipoxygenase Met-hemoglobin Oxodienes Sodium dodecyl sulphate Issue Date: Dec-2012 Publisher: NISCAIR-CSIR, India Abstract: Lipoxygenases comprise a family of non-heme iron-containing enzymes that catalyze the stereospecific dioxygenation of polyunsaturated fatty acids with 1, 4-cis-cis-pentadiene structure. Hemoglobin, a heme iron-containing protein has been reported to have lipoxygenase activity but the assay conditions that could enhance the activity remain obscure. Therefore, establishment of optimum assay conditions for lipoxygenase activity of hemoglobin could allow modeling of hemoglobin as lipoxygenase. Hemoglobin was extracted from blood of an identified individual of genotype AA. The hemoglobin was dialyzed at 4 oC for 24 h against 50 mM Tris-HCl buffers (pH 8.5 and 7.2) and effects of sodium dodecyl sulphate (SDS) and linoleic studied at pH 5.0 and 7.2 with UV–VIS Titration Spectrophotometry. The results show that 3.3, 8.6 and 88.1% concentrations of met-hemoglobin were found in presence of 0.0 mM SDS at pH 5.0 and 7.2, 1.043 mM SDS at pH 7.2 and 0.404 mM SDS at pH 5.0 respectively. Also, the difference spectra of hemoglobin in presence of linoleic acid showed positive peak at 285 nm which suggest the presence of oxodienes–a reaction product of hydroperoxidase activity of lipoxygenase. Formation of met-hemoglobin/met-myoglobin is highly correlated with lipid oxidation. Since highest concentration of met-hemoglobin (88.1%) was observed in presence of 0.404 mM SDS at pH 5.0, lipoxygenase activity of hemoglobin was enhanced in presence of SDS under these conditions.
ABSTRACT
The anionic surfactant sodium dodecyl sulphate (SDS), the core components of detergent and cosmetic product formulations, contributes significantly to the pollution profile of sewage and wastewater of all kinds. In this study, 44 SDS degrading strains were isolated by soil enrichment methods and the utilization efficiency was assessed by methylene blue active substances (MBAS) assay and High performance liquid chromatography (HPLC) method. Isolate S2 which showed maximum degradation was identified as Pseudomonas aeruginosa MTCC 10311 based on phenotypic features and 16 S rDNA typing .The isolate was found to harbor plasmid within the size range of 9-10 kb. The cured derivative of SDS degrading Pseudomonas aeruginosa was obtained at a frequency of 10.7% by incubation with ethidium bromide (500 mg ml-1) at 40oC. 96% of SDS degradation occurred at 1500 ppm level within 48 hr of incubation, whereas higher concentration of SDS (10000 ppm) showed only 20% degradation. The optimum temperature and pH was 30oC and 7.5, respectively.The additional supplementation of carbon and nitrogen source increased the degradation capacity from 93 to 95% and 90 to 96% respectively within 36 hrs of incubation.
ABSTRACT
Objective: Dithiothreitol(DTT) and ?-Mercaptoethanol(2-ME) are important reducing agents for SDS-PAGE.This study is to observe the diffusing effect of DTT and 2-ME during electrophoresis,and to find a way of avoiding this effect.Methods: We placed protein samples containing reducing agents and non-reduced protein samples separately in the sample wells at intervals for SDS-PAGE electrophoresis,and determined whether or not the electrophoretic lanes of the non-reduced samples were interfered by the adjacent lanes.Results: DTT and 2-ME diffused to the neighboring lane,so that the non-reduced samples were reduced partially.The spreading effect was positively correlated with the content of the reducing agent.Conclusion: DTT and 2-ME have a diffusing effect during SDS-PAGE electrophoresis.In separating the reduced and non-reduced proteins in the same gel at the same time,at least a blank lane should be set up in between them in order to avoid the diffusing effect.
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Sodium dodecyl sulphate-polyacrylamide gel electrophoresis of circulating filarial antigen fraction-2 isolated from plasma of microfilaraemic patients with Wuchereria bancrofti infection has shown 21 bands with molecular weights ranging from 12 to 120 kDa. The gel (12 cm) was sliced at an interval of one cm and the eluates of all the gel slices viz., CFA2–1 to CFA2–12 showed the presence of filarial antigen by sandwich enzyme-linked immunosorbent assay. The low molecular weight circulating filarial antigen fractions were found to share a common epitope with Wuchereria bancrofti microfilariae excretory-secretory antigen and urinary filarial antigen. The 3 antigen fractions CFA2-1, CFA2–9 and CFA2–12 showed higher sensitivity in detecting filarial immunoglobulin Μ antibodies than immunoglobulin G antibodies. However CFA2–9 fraction was found useful in serological differentiation of microfilaraemics from those with disease manifestations when filarial immunoglobulin G antibodies were detected. The antigenic epitope of CFA2–1 appears to be a carbohydrate, whereas CFA2–9 appears to be protein in nature.
ABSTRACT
The effect of urea, guanidine hydrochloride and sodium dodecyl sulphate on glycinin, the high molecular weight protein fraction from soybean has been investigated by analytical ultracentrifugation. Urea and guanidine hydrochloride dissociate the protein to a '2S' protein through the intermediary 7S and 4S proteins. However, in sodium dodecyl sulphate the protein directly dissociates to a 2S protein. Analysis of the data by calculation of per cent fraction and S20,w value indicates that dissociation and denaturation of glycinin occur simultaneously in the presence of the above reagents but to different extents.
ABSTRACT
The effect of sodium dodecyl sulphate on mustard and rapeseed 12S protein has been monitored by the techniques of ultracentrifugation, viscosity, difference spectra and fluorescence spectrophotometry. At low concentration of sodium dodecyl sulphate (<3.47 mM) mustard protein undergoes aggregation and at higher concentrations it dissociates to 1.8 S protein, the dissociation being complete at 17.3 mM sodium dodecyl sulphate. The rapeseed protein, on the other hand, undergoes dissociation at all the concentrations of sodium dodecyl sulphate. The reduced viscosity values of mustard protein in the presence of the denaturant are higher than those of rapeseed protein. Similarly in difference spectra change in absorbance values of mustard protein are higher.' The relative fluorescence intensity of the mustard protein increases with sodium dodecyl sulphate concentration, upto 0.87 mM and this is followed by fluorescence quneching at higher denaturant concentrations. However, with the rapeseed protein fluorescence quenching was observed at all concentrations of sodium dodecyl sulphate.