Kinetic study of the colloidal and enzymatic stability of β-galactosidase,for designing its encapsulation route through sol–gel route assisted by Triton X-100 surfactant

The kinetic study of the colloidal and enzymatic stability for the β-galactosidase of Bacillus circulans was carried out in function of the presence of Triton X-100 surfactant, under orbital agitation and varying the pH and temperature. The correlation between the Dynamic Light Scattering and enzyme assay data, supported by z-potential and Differential Scanning Calorimetry analyses, gave insights about the mechanism of the protective role of the surfactant against the enzyme deactivation during its incubation. The best conditions for preserving the enzymatic activity, under orbital agitation, were: presence of 1 × 10⁻³M Triton X-100, at pH 6.0 and 25 °C or 40 °C during less than 24 h, even in the presence of 0.1 M sodium cations or 4% ethanol. As these conditions also affect the polycondensation of the siliceous species and the enzyme-silica interactions, these could be considered as primary information for designing and optimizing an encapsulation route of β-galactosidase in silica, by a sol–gel process assisted by surfactant.     

A green and efficient procedure for the preconcentration and determination of cadmium,nickel and zinc from freshwater,hemodialysis solutions and tuna fish samples by cloud point extraction and flame atomic absorption spectrometry

Cloud point extraction (CPE) was used to simultaneously preconcentrate trace-level cadmium, nickel and zinc for determination by flame atomic absorption spectrometry (FAAS). 1-(2-Pyridilazo)-2-naphthol (PAN) was used as a complexing agent, and the metal complexes were extracted from the aqueous phase by the surfactant Triton X-114 ((1,1,3,3-tetramethylbutyl)phenyl-polyethylene glycol). Under optimized complexation and extraction conditions, the limits of detection were 0.37 μg L⁻¹ (Cd), 2.6 μg L⁻¹ (Ni) and 2.3 μg L⁻¹ (Zn). This extraction was quantitative with a preconcentration factor of 30 and enrichment factor estimated to be 42, 40 and 43, respectively. The method was applied to different complex samples, and the accuracy was evaluated by analyzing a water standard reference material (NIST SRM 1643e), yielding results in agreement with the certified values.     

Purification and biochemical characterization of angiotensin I-converting enzyme (ACE) from ostrich lung: The effect of 2,2,2-trifluoroethanol on ACE conformation and activity

This work reports the purification and biochemical characterization of angiotensin I-converting enzyme (ACE) from ostrich (Struthio camelus) lung. The molecular weight of the purified enzyme was approximately evaluated to be 200 kDa and the maximum enzyme activity was observed at pH 7.5. The enzyme activity was increased by detergents of Triton X-100 (0.01%), cetyltrimethylammonium bromide (CTAB) (0.1 and 1 mM) and sodium dodecyl sulfate (SDS) (0.1 mM), while decreased by Triton X-100 (1% and 10%) and SDS (1 mM and 10 mM). The secondary and tertiary structure and activity of ACE in the absence and presence of trifluoroethanol (TFE) were investigated using circular dichroism, fluorescence quenching and UV–visible spectroscopy, respectively. Our results revealed that TFE stabilizes ACE at low concentrations, while acts as a denaturant at higher concentration (20%). The K_m, K_cat and K_cat/K_m values of ostrich ACE towards FAPGG were 0.8 × 10^?4 M, 59,240 min^?1 and 74 × 10⁷ min^?1 M^?1, respectively. The values of IC₅₀ and K_i for captopril were determined to be 36.5 nM and 16.6 nM, respectively. In conclusion, ostrich lung ACE is a new enzyme which could be employed as a candidate for studying ACE structure and its natural or synthetic inhibitors.     

Activity of hydroperoxide lyase under aqueous and micro-aqueous conditions

Hydroperoxide lyases (HPL E.C. 4.1.2.) are part of the lipoxygenase pathway in plants and catalyze the conversion of fatty acid hydroperoxides into oxo acids and short chain aldehydes. These aldehydes have desirable properties for the food and agricultural industry. HPL activity can be modulated by salts and surfactants, but the mechanisms governing the modulation are not fully understood. Recombinant HPL activity was evaluated by use of factorial experimental design investigating the effects of KCl and Triton X-100 on HPL activity with 13-hydroperoxy-octadecadienoic acid (LA-OOH) and 13-hydroperoxy-octadienoyl sulfate (LS-OOH) as substrates. To investigate solubility issues of the two different substrates, an aqueous and a two-phase micro-aqueous reaction medium was used. The highest HPL activity (8.7 μmol min⁻¹ mg⁻¹) was achieved under aqueous conditions with high salt (1.5 M) and low surfactant (0%, v/v) concentrations and LA-OOH as a substrate. Maximal activity (2.4 μmol min⁻¹ mg⁻¹) under micro-aqueous conditions was achieved with high salt (1.5 M) and high surfactant (0.01%, v/v) concentrations and LS-OOH as a substrate. A significant interaction between salt and surfactant as well as salt and substrate could be identified and a hypothesis for the interaction phenomena is presented.     

Regeneration of denatured polyphenol oxidase in Toona sinensis (A.Juss.) Roam

The regeneration of polyphenol oxidase (PPO) from leaves of Toona sinensis (A.Juss.) Roam (TS), denatured by boiling with 0.4% (w/v) sodium dodecyl sulfate (SDS) and 1% (v/v) β-mercaptoethanol, and was studied with SDS-polyacrylamide gel electrophoresis (PAGE) and the gel-activity-stained assay. The optimal regenerating conditions for the denatured TS-PPO were as follows: extracting with buffer of 150 mM Na-Pi, pH 7.2; regenerating with buffer of 50 mM Tris–HCl, pH 7.2, 2% Triton X-100 for 45 min. In addition, the PPO regeneration was promoted by the addition of Cu²⁺ in the recovery buffer. The regenerating activity of the denatured-PPO was reduced in samples extracted with buffers containing polyvinylpyrrolidone (PVP), polyvinylpolypyrrolidone (PVPP) or Triton X-100.     

Selenium uptake,speciation and stressed response of Nicotiana tabacum L.

The research on the function and mechanism of selenium (Se) is of great significance for the development of Se-enriched agricultural products. In this paper, uptake, speciation distribution, the effects on the flue-cured tobacco growth and antioxidant system of Se at different levels (0–22.2 mg Se kg⁻¹) were studied through a pot experiment, aiming to clarify flue-cured tobacco's response to Se stress and the relationship between Se speciation and antioxidant system. The results showed that the leaf area and number, the biomass and the chlorophyll content reached the maximum at 4.4 mg kg⁻¹ of Se treatment. Selenium at low levels (≤4.4 mg kg⁻¹) stimulated the growth of flue-cured tobacco by elevating the capability of antioxidant stress and reducing the malondialdehyde (MDA) content to 0.6–0.8 times of that of the control. However, high Se levels (≥11.1 mg kg⁻¹) depressed the capability of antioxidant stress and raised the MDA content to 1.5-fold of that of the control, and meanwhile the biomass of the aboveground parts and underground parts declined notably. The Se content in different parts of flue-cured tobacco significantly increased with the growth of Se levels. The range of Se content in roots, leaves and stems at 2.2–22.2 mg kg⁻¹ of Se treatment were 16.7–58.6 mg kg⁻¹, 2.6–37.3 mg kg⁻¹ and 2.2–10.3 mg kg⁻¹, respectively. According to the detection of different Se speciation, only selenocysteine (SeCys) was detectable in leaves at 2.2 mg kg⁻¹ Se treatment; SeCys, selenite [Se(IV)]and selenate [Se(VI)] were detected in flue-cured tobacco leaves at Se treatment (≥4.4 mg kg⁻¹), which accounted for 4.6–10%, 9–18.7% and 71–86% respectively; SeCys, selenomethionine (SeMet) and Se(IV) were detected in roots, and organic selenium(66–84%) was the main Se species at Se ≤ 11.1 mg kg⁻¹ treatment; four Se species [SeCys, SeMet, Se(IV) and Se(VI)] were detected in flue-cured tobacco roots, and the main Se species was inorganic Se (60%) at 22.2 mg kg⁻¹ Se treatment. That was to say, the percentage of organic Se species (SeCys and SeMet in flue-cured tobacco leaves and root) declined, whereas the ratio of inorganic Se species [Se(IV) and Se(VI)] increased with the growth of Se levels. The correlation analysis showed that the superoxide dismutase (SOD) activity as well as the glutathione (GSH) and MDA contents were positively correlated with the Se(IV) and Se(VI) contents at P < 0.01 and excessive inorganic Se might destruct the reactive oxygen species (ROS) balance and enhance the MDA content, thus causing damage to the plant growth. In a word, the present study suggested that the ratio of inorganic Se [Se(IV) and Se(VI)] was closely related with the growth and the antioxidant capacity of flue-cured tobacco and the excessive application of Se led to the higher proportion of inorganic Se and poorer antioxidant capacity, which ultimately inhibited the growth of flue-cured tobacco.     

Concurrent purification and antioxidant activity of phycobiliproteins from Lyngbya sp. A09DM: An antioxidant and anti-aging potential of phycoerythrin in Caenorhabditis elegans

The present study probes into the purification of phycobiliproteins, and characterization of their in vitro anti-oxidant activity. Moreover, the study also demonstrates the use of antioxidant virtue of phycoerythrin in moderating the phenomenon of aging in Caenorhabditis elegans. Phycoerythrin, phycocyanin and allophycocyanin were purified successfully from Lyngbya sp. A09DM by ammonium sulfate fractionation appended with Triton X-100 intercession. The success of protocol was examined by a series of biochemical characterization like SDS-PAGE, native-PAGE, UV–visible spectroscopy and fluorescence spectroscopy ensuring purity, integrity and functionality of purified phycoerythrin, phycocyanin and allophycocyanin. Purified phycobiliproteins were evaluated for antioxidant and metal ion chelating activity by various in vitro antioxidant assay systems. Results showed significant and dose-dependent antioxidant as well as metal chelating potential of all phycobiliproteins in decreasing order of phycoerythrin > phycocyanin > allophycocyanin. Expansion in lifespan and improvement in pharyngeal pumping of C. elegans were noticed upon pre-treatment with phycoerythrin (100 μg ml⁻¹). Moreover, phycoerythrin mediated increase in worm survival under oxidative stress revealed that the life expansion effect of phycoerythrin on nematode is in part by an action of its antioxidant virtue. These results collectively added up evidence in favor of the ‘free-radical theory of aging’. The present report, for the first time, describes antioxidant potential of phycoerythrin and its use in extending life-span of C. elegans.     

Surfactant-assisted two phase partitioning bioreactors for laccase-catalyzed degradation of anthracene

The degradation of anthracene by laccase from Trametes versicolor in enzymatic reactors was evaluated. The use of a surfactant (Triton X-100) at concentration above critical micelle concentration (CMC) enhanced anthracene solubility and facilitated its degradation. Moreover, Triton exerted a beneficial effect on the laccase stability and protected it from the oxidative action of the mediator 1-hydroxybenzotriazole (HBT). In a further stage, the combined configuration of a two phase partitioning bioreactor (TPPB) operating with silicone oil as an immiscible solvent and the surfactant achieved the degradation of anthracene at higher conversion rate: 16 μmol/L_Rh. Furthermore, a model for anthracene degradation by laccase-mediator system was developed. The first order kinetic constant (k) and the overall mass transfer coefficient (K_La) were estimated by using the method of least squares. The increased K_La value obtained, 788.1 h^?1, proved that Triton also improved mass transfer. Anthracene concentration in aqueous phase was close to that corresponding to equilibrium state suggesting that mass transfer mechanism did not limit the global process. The kinetic constant, which is expected to depend on the initial concentration of enzyme, resulted in 52.2 h^?1. Enzyme inactivation occurred in two stages and could be modeled by using a three parameter biexponential model. The possibility of reusing silicone oil to dissolve more anthracene was proven in three consequent cycles with high percentages of anthracene removal.     

Purification and characterization of a nitroreductase from the soil bacterium Streptomyces mirabilis

A NADH-dependent nitroreductase from an efficient nitro-reducing soil bacterium, Streptomyces mirabilis DUT001, was isolated and characterized. The enzyme was purified to near homogeneity using ammonium sulfate precipitation, ion exchange chromatography, and gel filtration chromatography. The native enzyme was estimated by gel filtration to have a molecular weight of 68 kDa, and its subunit molecular weight determined by SDS-PAGE was about 34 kDa, which indicated this enzyme was a dimer. Polycyclic nitroaromatic compounds were preferred substrates for this enzyme. The purified enzyme exhibited maximum activity at pH 7.5 and 40 °C. The addition of various chemicals such as reducing agents, metal ions, and chelating agents, had effects on enzyme activity. Mg²⁺, Ca²⁺, Sr²⁺, and 1% (w/v) Triton X-100 increased activity. However, Hg²⁺, Co²⁺, Ni²⁺, Cu²⁺, and SDS reduced activity. The maximum reaction rate (V_max) was 64 μM min^?1 mg^?1 enzyme and the apparent Michaelis–Menten constants (K_m) for 4-nitro-1,8-naphthalic anhydride and NADH were 276 and 29 μM, respectively. Menadione, bimethylenebis, sodium benzoate, and antimycin A were inhibitors of the purified nitroreductase with apparent inhibition constants (K_is) of 20, 36, 44 and 80 μM, respectively.     

Effects of detergents on the West Nile virus protease activity

Detergents such as Triton X-100 are often used in drug discovery research to weed out small molecule promiscuous and non-specific inhibitors which act by aggregation in solution and undesirable precipitation in aqueous assay buffers. We evaluated the effects of commonly used detergents, Triton X-100, Tween-20, Nonidet-40 (NP-40), Brij-35, and CHAPS, on the enzymatic activity of West Nile virus (WNV) protease. Unexpectedly, Triton X-100, Tween-20, and NP-40 showed an enhancement of in vitro WNV protease activity from 2 to 2.5-fold depending on the detergent and its concentration. On the other hand, Brij-35, at ?0.001% enhanced the protease activity by 1.5-fold and CHAPS had the least enhancing effect. The kinetic analysis showed that the increase in protease activity by Triton X-100 was dose-dependent. Furthermore, at Triton X-100 and Tween-20 concentrations higher than 0.001%, the inhibition of compound B, one of the lead compounds against WNV protease identified in a high throughput screen (IC₅₀ value of 5.7 ± 2.5 μM), was reversed. However, in the presence of CHAPS, compound B still showed good inhibition of WNV protease. Our results, taken together, indicate that nonionic detergents, Triton X-100, Tween, and NP-40 are unsuitable for the purpose of discrimination of true versus promiscuous inhibitors of WNV protease in high throughput assays.     

Amperometric xanthine biosensors based on electrodeposition of platinum on polyvinylferrocenium coated Pt electrode

Novel xanthine biosensors were successfully fabricated by immobilizing xanthine oxidase on polyvinylferrocenium perchlorate matrix (PVF⁺ClO₄⁻) and platinum electrodeposited polyvinylferrocenium perchlorate matrix. PVF⁺ClO₄⁻ film was coated on Pt electrode at +0.7 V vs. Ag/AgCl by electrooxidation of polyvinylferrocene (PVF). Platinum nanoparticles were deposited on PVF⁺ClO₄⁻ electrode by electrochemical deposition in 2.0 mM H₂PtCl₆ solution at −0.2 V. Xanthine oxidase was incorporated into the polymer matrix via ion exchange process by immersing modified Pt electrodes in the enzyme solution. The amperometric responses of the biosensors were measured via monitoring oxidation current of hydrogen peroxide at +0.5 V. Under the optimal conditions, the linear ranges of xanthine detection were determined as 1.73 × 10⁻³–1.74 mM for PVF⁺XO⁻ and 0.43 × 10⁻³–2.84 mM for PVF⁺XO⁻/Pt. The detection limits of xanthine were 5.20 × 10⁻⁴ mM for PVF⁺XO⁻ and 1.30 × 10⁻⁴ mM for PVF⁺XO⁻/Pt. Moreover, the effects of applied potential, electrodeposition potential, H₂PtCl₆ concentration, amount of electrodeposited Pt nanoparticles, thickness of polymeric film, temperature, immobilization time, xanthine and xanthine oxidase concentrations on the response currents of the biosensors were investigated in detail. The effects of interferents, the operational and storage stabilities of biosensors and the applicabilities to drug samples of the biosensors analysis were also evaluated.     

Removal of Zn(II) ions from aqueous solution using Moringa oleifera Lam. (horseradish tree) biomass

The removal of Zn(II) ions from aqueous solution using pure and chemically pretreated biomass of Moringa oleifera was investigated at 30 ± 1 °C in this study. The experimental results explored that the maximum pH (pH_max) for efficient sorption of Zn(II) was 7 ± 0.1 at which evaluated biosorbent dosage and biosorbent particle size, were 0.5 g/L, <0.255 mm, respectively. The cellular Zn(II) concentration increased with the concentrations of Zn(II) in solution. Pretreatment of M. oleifera biomass affected the sorption process and the uptake capacity (mg/g) of biomass for Zn(II) uptake was in following order: NaOH (45.76) > H₂SO₄ (45.00) > CTAB (42.80) > Ca(OH)₂ (42.60) > Triton X-100 (42.06) > H₃PO₄ (41.22) > Al(OH)₃ (41.06) > SDS (40.41) > HCl (37.00) > non-treated biomass (36.07). There was significant increase in uptake capacity of M. oleifera biomass, which suggested that affinity between metal and sorbent can be increased after some sort of pretreatment. Both Langmuir and Freundlich isotherm model fitted well to data of Zn(II) biosorption as represented by high value of their correlation coefficient (i.e. R² ≈ 1). Kinetic studies revealed that Zn(II) uptake was fast with 90% or more of uptake occurring with in 40 min of contact time and the equilibrium was reached in 50 min of contact time. The sorption rates were better described by a second order expression than by a more commonly applied Lagergren equation. Finally it was concluded that pretreatment of M. oleifera biomass can achieve superior Zn(II) uptake capacity in comparison to non-pretreated biomass.     

Reactivation of the alternative oxidase of Yarrowia lipolytica by nucleoside monophosphates

The study of the effect of nucleoside phosphates on the activity of cyanide-resistant oxidase in the mitochondria and submitochondrial particles of Yarrowia lipolytica showed that adenosine monophosphate (5′-AMP, AMP) did not stimulate the respiration of intact mitochondria. The incubation of mitochondria at room temperature (25 °C) for 3–5 h or their treatment with ultrasound, phospholipase A, and the detergent Triton X-100 at a low temperature inactivated the cyanide-resistant alternative oxidase. The inactivated alternative oxidase could be reactivated with AMP. The reactivating effect of AMP was enhanced by azolectin. Some other nucleoside phosphates also showed reactivating ability in the following descending order: AMP = GMP > GDP > GTP > XMP > IMP. The apparent K_m values for AMP in reactivation of the alternative oxidase of submitochondrial particles or mitochondria treated with Triton X-100 and incubated at 25 °C were calculated. Physiological aspects of activation of the alternative oxidase are discussed in connection with the impairment of electron transfer through the cytochrome pathway.     

Biochemical and structural characterization of a detergent-stable serine alkaline protease from seawater haloalkaliphilic bacteria

An extracellular protease from a newly isolated seawater haloalkaliphilic bacterium, haloalkaliphilic bacteria Ve₂-20-9₁ [HM047794], was purified and characterized. The enzyme is a monomer with a 37.2 kDa estimated molecular weight. It catalyzed reactions in the pH range 8–11 and performed optimally at pH 10. While maximal activity occurred at 50 °C, the temperature profile shifted from 50 to 80 °C in 1–3 M NaCl. The enzyme's thermal stability was probed using circular dichroism (CD) spectroscopy with NaCl at 50 and 70 °C. The changes in the enzyme's secondary structure were also analyzed using Fourier transform infrared spectroscopy (FTIR). The N-terminal amino acid sequence GKDGPPGLCGFFGCI exhibited low homology with other bacterial proteases, which highlights the enzyme's novelty. The enzyme was labile in anionic surfactant (1% w/v SDS) but showed stability in non-ionic surfactants (Tween 20, Tween 80 and Triton X-100 all 1% v/v), commercial detergents, and oxidizing and reducing agents. The enzyme's excellent stability in commercial detergents highlights its potential as a detergent additive.     

Comparison of two type IV hyperthermophilic adenylyl cyclases characterizations from the archaeon Pyrococcus furiosus

In this paper, two genes that encoded two soluble type IV adenylyl cyclases (AC) from the hyperthermophilic archaeon Pyrococcus furiosus (PFAC I and PFAC II) were cloned and expressed in Escherichia coli (E. coli) BL21 (DE3). Amino acid sequence analysis of the two enzymes showed 29% homology. PFAC I and PFAC II were both Mn²⁺ activated enzyme. They were purified by His-trap chromatography and had a specific activity of 3.1 × 10³ U/mg at pH 10.0, 95 °C (PFAC I) and 2.0 × 10³ U/mg at pH 11.0, 95 °C (PFAC II), respectively. The K_m and k_cat of PFAC I was 1.38 mM and 1.11 s⁻¹. The K_m and k_cat of PFAC II was 1.44 mM and 0.80 s⁻¹. The thermostability of PFAC I and PFAC II were higher than the soluble type IV adenylyl cyclases from Yersinia pestis (YpAC-IV). All of the properties suggested that these two adenylyl cyclases may be useful for the industrial producing of cyclic adenosine 3′,5′-monophosphate (cAMP).     

Fungal surface protein mediated one-pot synthesis of stable and hemocompatible gold nanoparticles

Despite their large secretome and wide applications in bioprocesses, fungi remain underexplored in metal nanoparticles (MNP) biosynthesis. Previous studies have shown that cell surface proteins of Rhizopus oryzae play a crucial role in biomineralization of Au(III) to produce gold nanoparticles (AuNPs). Therefore, it is hypothesized that purified cell surface protein may produce in vitro AuNPs with narrow size distribution for biomedical and biocatalytic applications. However, different protein extraction methods might affect protein stability and the AuNP biosynthesis process. Herein, we have explored the extraction of cell surface proteins from R. oryzae using common detergents and reducing agent (sodium dodecyl sulfate (SDS) Triton X-100, and 1,4-dithiothreitol (DTT)) and their effect on the size and shape of the biosynthetic AuNPs. The surface proteins extracted with reducing agent (DTT) and non-ionic detergent (Triton X-100) produce spherical AuNPs with a mean particle size of 16 ± 7 nm, and 19 ± 4 nm, respectively, while the AuNPs produced by the surface protein extracted by ionic detergent (SDS) are flower-like AuNPs with broader size distribution of 43 ± 19 nm. This synthetic approach does not require use of any harsh chemicals, multistep preparation and separation process, favouring environmental sustainability. The biosynthetic AuNPs thus formed, are stable in different physiological buffers and hemocompatible, making them suitable for biomedical applications.     

Treatment of dye (Remazol Blue) and heavy metals using yeast cells with the purpose of managing polluted textile wastewaters

The bioaccumulation of chromium(VI), nickel(II), copper(II), and reactive dye by the yeast Rhodotorula mucilaginosa has been investigated in media containing molasses as a carbon and energy source. Optimal pH values for the yeast cells to remove the pollutants were pH 4 for copper(II) and dye, pH 6 for chromium(VI) and dye, and pH 5 for nickel(II) and dye in media containing 50 mg l^?1 heavy metal and 50 mg l^?1 Remazol Blue. The maximum dye bioaccumulation was observed within 4–6 days and uptake yields varied from 93% to 97%. The highest copper(II) removal yields measured were 30.6% for 45.4 mg l^?1 and 32.4% for 95.9 mg l^?1 initial copper(II) concentrations. The nickel(II) removal yield was 45.5% for 22.3 mg l^?1, 38.0% for 34.7 mg l^?1, and 30.3% for 62.2 mg l^?1. Higher chromium(VI) removal yields were obtained, such as 94.5% for 49.2 mg l^?1 and 87.7% for 129.2 mg l^?1 initial chromium(VI) concentration. The maximum dye and heavy metal bioaccumulation yield was investigated in media with a constant dye (approximately 50 mg l^?1) and increasing heavy metal concentration. In the medium with 48.9–98.8 mg l^?1 copper(II) and constant dye concentration, the maximum copper(II) bioaccumulation was 27.7% and 27.9% whereas the maximum dye bioaccumulation was 96.1% and 95.3%. The maximum chromium(VI) bioaccumulation in the medium with dye was 95.2% and 80.3% at 48.2 and 102.2 mg l^?1 chromium(VI) concentrations. In these media dye bioaccumulation was 76.1% and 35.1%, respectively. The highest nickel(II) removal was 6.1%, 20.3% and 16.0% in the medium with 23.8 mg l^?1 nickel(II) + 37.8 mg l^?1 dye, 38.1 mg l^?1 nickel(II) + 33.4 mg l^?1 dye and 59.0 mg l^?1 nickel(II) + 39.2 mg l^?1 dye, respectively. The maximum dye bioaccumulation yield in the media with nickel(II) was 94.1%, 78.0% and 58.7%, respectively.     

Novel antioxidant bromophenols with acetylcholinesterase,butyrylcholinesterase and carbonic anhydrase inhibitory actions

In this study, a series of novel bromophenols were synthesized from benzoic acids and methoxylated bromophenols. The synthesized compounds were evaluated by using different bioanalytical antioxidant assays including 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS⁺) radical scavenging assays. Also, reducing power of novel bromophenols were evaluated by Cu²⁺-Cu⁺ reducing, Fe³⁺-Fe²⁺ reducing and [Fe³⁺-(TPTZ)₂]³⁺-[Fe²⁺-(TPTZ)₂]₂+ reducing and ferrous ions (Fe²⁺) chelating abilities. The compounds demonstrate powerful antioxidant activities when compared to standard antioxidant molecules of α-tocopherol, trolox, butylated hydroxyanisole (BHA), and butylated hydroxytoluene (BHT). Also in the last part of this studies novel bromophenols were tested against some metabolic enzymes including acetylcholinesterase (AChE), butyrylcholinesterase (BChE) enzymes and carbonic anhydrase I, and II (hCA I and hCA II) isoenzymes. The newly synthesized bromophenols showed Ki values in a range of 6.78 ± 0.68 to 126.07 ± 35.6 nM against hCA I, 4.32 ± 0.23 to 72.25 ± 12.94 nM against hCA II, 4.60 ± 1.15 to 38.13 ± 5.91 nM against AChE and 7.36 ± 1.31 to 29.38 ± 3.68 nM against BChE.     

Cloud point extraction-flame atomic absorption spectrometry for pre-concentration and determination of trace amounts of silver ions in water samples

A cloud point extraction (CPE) method was used as a pre-concentration strategy prior to the determination of trace levels of silver in water by flame atomic absorption spectrometry (FAAS) The pre-concentration is based on the clouding phenomena of non-ionic surfactant, triton X-114, with Ag (I)/diethyldithiocarbamate (DDTC) complexes in which the latter is soluble in a micellar phase composed by the former. When the temperature increases above its cloud point, the Ag (I)/DDTC complexes are extracted into the surfactant-rich phase. The factors affecting the extraction efficiency including pH of the aqueous solution, concentration of the DDTC, amount of the surfactant, incubation temperature and time were investigated and optimized. Under the optimal experimental conditions, no interference was observed for the determination of 100 ng·mL⁻¹ Ag⁺ in the presence of various cations below their maximum concentrations allowed in this method, for instance, 50 μg·mL⁻¹ for both Zn²⁺ and Cu²⁺, 80 μg·mL⁻¹ for Pb²⁺, 1000 μg·mL⁻¹ for Mn²⁺, and 100 μg·mL⁻¹ for both Cd²⁺ and Ni²⁺. The calibration curve was linear in the range of 1–500 ng·mL⁻¹ with a limit of detection (LOD) at 0.3 ng·mL⁻¹. The developed method was successfully applied for the determination of trace levels of silver in water samples such as river water and tap water.     

Thermal decomposition studies of cis-bis(1-alkenyl)platinum(II) complexes

Thermal decomposition studies of bis(1-alkenyl)platinum(II) complexes of the type Pt(L₂)R₂ (where L = PPh₃ or L₂ = dppe or dppp; R = 1-alkenyl) are reported. The results revealed interesting organic product distributions depending on the length of the alkenyl chains, the nature of the supporting ligands and the metal centers. It is believed that the major decomposition pathways for the title complexes involve β-hydride elimination and/or reductive elimination as well as alkene isomerization. Mechanisms for the major and minor decomposition pathways are proposed. The amount of isomeric products obtained, i.e., 2-alkenes and 1,(n ? 2)-diene, increases with increasing chain length.