Form Of Chloride Salts Research Articles

Effect of Na, K and Ca Salts on Growth, Physiological Performance, Ion Accumulation and Mineral Nutrition of Mesembryanthemum crystallinum.

Mesembryanthemum crystallinum L. is an obligatory halophyte species showing optimum growth at elevated soil salinity levels, but the ionic requirements for growth stimulation are not known. The aim of the present study was to compare the effects of sodium, potassium and calcium in the form of chloride and nitrate salts on the growth, physiological performance, ion accumulation and mineral nutrition of M. crystallinum plants in controlled conditions. In a paradoxical way, while sodium and potassium had comparable stimulative effect on plant growth, the effect of calcium was strongly negative even at a relatively low concentration, eventually leading to plant death. Moreover, the effect of Ca nitrate was less negative in comparison to that of Ca chloride, but K in the form of nitrate had some negative effects. There were three components of the stimulation of biomass accumulation by NaCl and KCl salinity in M. crsytallinum: the increase in tissue water content, increase in ion accumulation, and growth activation. As optimum growth was in a salinity range from 20 to 100 mM, the increase in the dry biomass of plants at a moderate (200 mM) and high (400 mM) salinity in comparison to control plants was mostly due to ion accumulation. Among physiological indicators, changes in leaf chlorophyll concentration appeared relatively late, but the chlorophyll a fluorescence parameter, Performance Index Total, was the most sensitive to the effect of salts. In conclusion, both sodium and potassium in the form of chloride salts are efficient in promoting the optimum growth of M. crystallinum plants. However, mechanisms leading to the negative effect of calcium on plants need to be assessed further.

Similar Responses of Relatively Salt-Tolerant Plants to Na and K during Chloride Salinity: Comparison of Growth, Water Content and Ion Accumulation.

The aim of the present study was to compare changes in growth, ion accumulation and tissue water content in relatively salt-tolerant plant taxa—Beta vulgaris subsp. maritima, Beta vulgaris subsp. vulgaris var. cicla, Cochlearia officinalis, Mentha aquatica and Plantago maritima—as a result of NaCl and KCl salinity in controlled conditions. Similar growth responses to Na+ and K+ salinity in a form of chloride salts were found for all model plants, including growth stimulation at low concentrations, an increase in water content in leaves, and growth inhibition at high salinity for less salt-resistant taxa. All plant taxa were cultivated in soil except M. aquatica, which was cultivated in hydroponics. While the morphological responses of B. vulgaris subsp. vulgaris var. cicla, B. vulgaris subsp. maritima and P. maritima plants to NaCl and KCl were rather similar, C. officinalis plants tended to perform worse when treated with KCl, but the opposite was evident for M. aquatica. Plants treated with KCl accumulated higher concentrations of K+ in comparison to the accumulation of Na+ in plants treated with equimolar concentrations of NaCl. KCl-treated plants also had higher tissue levels of electrical conductivity than NaCl-treated plants. Based on the results of the present study, it seems that both positive and negative effects of Na+ and K+ on plant growth were due to unspecific ionic effects of monovalent cations or/and the specific effect of Cl−.

The influence of cations on α-lactalbumin amyloid aggregation

There is limited knowledge regarding α-lactalbumin amyloid aggregation and its mechanism. We examined the formation of α-lactalbumin amyloid fibrils (α-LAF) in the presence of cations (Mg2+, Ca2+, Na+, K+, NH4+, and Cs+) in the form of chloride salts at two concentrations. We have shown that studied cations affect the conformation of α-lactalbumin, the kinetics of its amyloid formation, morphology, and secondary structure of α-LAF in a different manner. The higher salts concentration significantly accelerated the aggregation process. Both salt concentrations stabilized α-lactalbumin's secondary structure. However, the presence of divalent cations resulted in shorter fibrils with less β-sheet content. Moreover, strongly hydrated Mg2+ significantly altered α-lactalbumin's tertiary structure, followed by Na+, NH4+, K+, and weakly hydrated Cs+. On the other hand, Ca2+, despite being also strongly hydrated, stabilized the tertiary structure, supposedly due to its high affinity towards α-lactalbumin. Yet, Ca2+ was not able to inhibit α-lactalbumin amyloid aggregation.Graphic abstract

Neutron capture cross section of Mn53 from irradiation with cold and reactor neutrons

The neutron capture cross section of $^{53}\mathrm{Mn}$ was measured with cold and reactor neutrons by the activation method, relative to the well-known cross section of $^{59}\mathrm{Co}$. Three targets containing a total of $\ensuremath{\approx}{10}^{18}$ atoms $^{53}\mathrm{Mn}$ in the form of chloride salt were prepared using a stock solution obtained from activated accelerator waste in the course of the ERAWAST initiative at Paul Scherrer Institute, Switzerland (PSI). Natural cobalt salt was added to the sample material as an internal neutron flux monitor. The total numbers of $^{53}\mathrm{Mn}$ and $^{59}\mathrm{Co}$ atoms in the target were deduced via mass spectrometric measurements at PSI. Cold-neutron activation was carried out at the ICON beamline at PSI. Reactor activation was performed at the LVR-15 research reactor of Research Centre \ifmmode \check{R}\else \v{R}\fi{}e\ifmmode \check{z}\else \v{z}\fi{} in a well-moderated neutron field of an outer reactor channel. The thermal-neutron capture cross section and the resonance integral were determined by the cadmium ratio method. The induced activities of $^{54}\mathrm{Mn}$ and $^{60}\mathrm{Co}$ were quantified by high-resolution $\ensuremath{\gamma}$-ray spectrometry. The obtained thermal-neutron capture cross section of $76.5\ifmmode\pm\else\textpm\fi{}1.4\phantom{\rule{0.222222em}{0ex}}\mathrm{b}$ agrees well with previously reported results. The uncertainty of this value could be reduced by almost an order of magnitude with respect to older measurements and is on a level comparable to stable nuclides. The resonance integral of $43.1\ifmmode\pm\else\textpm\fi{}1.2\phantom{\rule{0.222222em}{0ex}}\mathrm{b}$ was obtained for the real reactor spectrum with epithermal-spectrum shape factor $\ensuremath{\alpha}=0.025$.

Хроматографический метод определения хлорорганических соединений в нефти

На основании испытаний модельных и реальных образцов нефтей, содержащих ХОС в различных концентрациях, были определены показатели прецизионности разработанного метода. Также было проведено сравнение показателей точности разработанного метода с существующими стандартными методами определения ХОС. Как видно из полученных данных, разработанный метод имеет более низкий предел обнаружения и лучшие показатели прецизионности, чем существующие методы, что дает возможность определения более низких концентраций с высокой точностью.

Microbatch under-oil salt screening of organic cations: single-crystal growth of active pharmaceutical ingredients.

Multicomponent solid forms of active pharmaceutical ingredients represent a modern method of tuning their physicochemical properties. Typically, salts are the most commonly used multicomponent solid form in the pharmaceutical industry. More than 38% are formulated as organic cations. Salt screening is an essential but demanding step when identifying the most appropriate formulation. The microbatch under-oil crystallization technique of proteins has been combined with the previously developed high-throughput vapour-diffusion screening for use as a novel method of primary salt screening of organic cations. The procedure allows the set up of about 100 crystallization experiments per 30 min. This requires between 17 and 564 mg of screened cationic active pharmaceutical ingredients, which were of moderate to very high water solublity. Five distinct organic salts, three of them diverse active pharmaceutical compounds or the other enantiomer thereof, in the form of chloride salts were tested. The screening was extremely successful; at least two new single-crystal structures could be obtained for each particular compound and many more salts as single crystals were formed compared with our previous vapour-diffusion method.

Liquid phase assisted grain growth in Cu2ZnSnS4 nanoparticle thin films by alkali element incorporation.

The effect of adding LiCl, NaCl, and KCl to Cu2ZnSnS4 (CZTS) nanoparticle thin-film samples annealed in a nitrogen and sulfur atmosphere is reported. We demonstrate that the organic ligand-free nanoparticles previously developed can be used to produce an absorber layer of high quality. The films were Zn-rich and Cu-poor, and no secondary phases except ZnS could be detected within the detection limit of the characterization tools used. Potassium was the most effective alkali metal to enhance grain growth, and resulted in films with a high photoluminescence signal and an optical band gap of 1.43 eV. The alkali metals were introduced in the form of chloride salts, and a significant amount of Cl was detected in the final films, but could be removed in a quick water rinse.

PURIFICATION AND CHARACTERIZATION OF THE NEWLY THERMOSTABLE PROTEASE PRODUCED BY Brevibacillus thermoruber LII ISOLATED FROM PADANG CERMIN HOTSPRING, INDONESIA

Thermo stability is among of the vital enzyme characteristics for industrial application. Brevibacillus thermoruber LII was obtained as a potential isolate from the previous researchwhich screened the potential thermostable protease producing bacteria from Indonesian hotspring.The newly thermostable protease produced by thermophilic Brevibacillus thermoruber LII hadbeen purified and characterized. It was predicted that the pure enzyme obtained from Brevibacillusthermoruber LII was homo hexameric, having molecular weight of 36 kDa unit protein and itsnative was 215 kDa. In addition, it was also a neutral metalo serine protease according tobiochemical tests that it was totaly inhibited by PMSF (Phenylmethanesulfonyl fluoride) and EDTA(Ethylenediaminetetraacetic acid). It showed optimum activity at pH of 8 and active in acidic buffer(up to pH of 4). All of metal ion in the form of chloride salt (2.5 mM) which were tested on theenzyme enhanced the enzyme activity but Li2+. Ca2+ion increased the activity and the stability ofenzyme against thermal. The enzyme also showed the stability against solvent. The protease LIIhad optimum temperature at 60oC without CaCl 2and 80 – 85oC with addition of 2.5 mM CaCl 2. TheK Mand V maxvalues for the purified protease LII were 27.2 mg/ml or 0.362 – 0.272 M for substrateHammersteinCasein (MM 75–100 kDa) and 261.1 µg/minute/ml, respectively.

IDENTIFICATION AND PARTIAL CHARACTERIZATION OF CRUDE EXTRACELLULAR ENZYMES FROM BACTERIA ISOLATED FROM SHRIMP WASTE PROCESSING

Attention on chitin degrading enzymes has been growing since their ability to reduce the waste of shrimp/other crustaceans processing industries and converting them into value added products such as biologically active chitin and chitosan oligomer. Previous experiment found that KLU 11.16 isolate was one of the potential bacteria isolated from shrimp waste producing chitinolytic enzymes including chitosanases. A study on the identification of KLU 11.16 extracellularcrude enzyme was carried out by cultivating the bacteria on chitin medium. Due to the wide application of chitosanase, the characterization of the crude chitosanase was carried out after an identification of the enzymes secreted. Based on assessment using zymogram technique, this bacteria secreted a mixed extracellular chitinolytic enzyme and other hydrolytic enzyme. The crudechitinolytic enzyme degraded 85% deacetylated (DA) better than 100% DA chitosan, and slightly degraded glycol chitin, indicating that KLU 11.16 secreted chitosanases and chitinases enzyme. In addition to the chitinolytic enzyme, the bacteria also secreted protein and carbohydrate degrading enzymes when running at SDS-PAGE enriched with casein, soluble starch and CMC substrates.Crude chitosanases enzyme was performed well at pH 6 and temperature of 300C, and the activity can be increased by addition of 1 mM Fe 2+ in form of chloride salt. Addition of detergent, i.e1mM of Triton X-100 and SDS slightly decreased the activity. Future application of the crude chitosanase from KLU 11.16 was on producing chitosan derivative such as chitosan oligomer using substrateof 85% DA chitosan, which is more digestable by other enzymes secreted by KLU 11.16

SCREENING AND CHARACTERIZATION OF L-GLUTAMINASE PRODUCED BY BACTERIA ISOLATED FROM SANGIHE TALAUD SEA

L-glutaminase (L-glutamine amidohydrolase, EC 3.5.1.2) is a very important enzyme due to its role as flavor enhancer and antileukemic agent. Salt-tolerant L-glutaminase produced bymarine bacteria is favorable in food industries. This study describes the screening of L- glutaminase producing marine bacteria from Sangihe-Talaud Sea, North Sulawesi, Indonesia.Screening of L-glutaminase was performed using a liquid medium and identification of selected isolate was performed using molecular-based 16S rDNA. Results showed that there were 7 isolates produced positive results of L-glutaminase, and one of them (II.1 isolate) produced the highest activity, i.e 147.99 U/L, equivalent to the specific activity of 62.32 U/mg. The isolate then selected for further study. Bacterial identification based on 16S rRNA sequencing has revealed that the isolate was 96% similar to Pseudomonas aeruginosa strain CG-T8. Characterization of extracellular L-glutaminase from the II.1 isolate showed that the enzyme worked optimally at temperature of 37-45 °C and pH 7. The enzyme was stable when NaCl solution was added up to 8% and began to decrease on addition of NaCl solution of 16% and 20% with relative activity of 79% and 74%, respectively. The effect of metal ions, e.g Mn2+, Mg2+, and Co2+ in the form of chloride salt, were able to increase enzyme activity, whereas the addition of other metal ions (Zn2+, Fe3+, and Ca2+) decreased the activity. The molecular weights of L-glutaminase was estimated around42 kDa and 145 kDa.

Pt recovery using Cyphos IL-101 immobilized in biopolymer capsules

Cyphos ® IL-101, a tetraalkylphosphonium chloride salt (ionic liquid, IL) has been immobilized in capsules prepared by ionotropic gelation in calcium chloride solutions. The IL content was varied in the resin between 0.29 and 1.28 mmol IL g −1. These resins have been tested for Pt recovery from HCl solutions. The equilibrium was very slightly affected by the concentration of HCl and chloride ions. The sorption isotherms were modeled using the Langmuir equation: the maximum sorption capacity was influenced by the drying of the resin but remained close to 177 mg Pt g −1 for wet resin (i.e. 0.9 mmol Pt g −1, dry weight basis, or 0.7 mol Pt mol −1 Cyphos) and 142 mg Pt g −1 for dry resin (i.e. 0.73 mmol Pt g −1, or 0.57 mol Pt mol −1 Cyphos). The presence of nitrates, nickel or copper ions (added under the form of chloride salts) did not significantly decrease sorption capacity even at concentrations as high as 5 g L −1. Conversely, zinc at the concentration of 5 g L −1, significantly decreased Pt sorption, probably due to the competition effect of chloro-anionic Zn species. This is another evidence of the ion exchange mechanism involved in the binding of hexachloroplatinate species. The kinetics are weakly affected by the agitation speed (in the range 150–350 rpm) indicating that the resistance to film diffusion is not the limiting step. The kinetics are affected by the IL content, metal concentration and more specifically the drying of the resin: intraparticle diffusion sounds to be the controlling kinetic step: the intraparticle diffusion coefficient varied between 2 × 10 −12 and 18 × 10 −11 m 2 min −1, depending on experimental conditions. Platinum can be desorbed from loaded resin using either nitric acid (5 M) or thiourea (0.1 M in 0.1 M HCl acid solution). The resin was efficiently used for three sorption/desorption cycles using nitric acid: a decrease in sorption capacity and desorption efficiency was observed beginning with the third cycle, probably due to a progressive degradation of the resin.

Enterohepatic circulation of 64Cu, 52Mn and 203Hg in rats.

The intestinal absorption of 64CuCl2, 52MnCl2 and 203HgCl2 was compared with those of biliary excreted radiometals in rats during 24 h after intraduodenal administration. Biliary excreted metals were obtained from rats (donors) given previously intravenously 64CuCl2, 52MnCl2 and 203HgCl2. The metals in form of chloride salts as well as the metals excreted via bile were given to control or acceptor rats in the same dose intraduodenally. In manganese, given as 52MnCl2 15.04±8.48%, whereas given biliary excreted 52Mn 35.45±5.72% was absorbed. Biliary excreted manganese is probably in the bile in form suitable for intestinal absorption. In both other metals the intestinal absorption was higher when metal in form of chloride salt was administered (in 64Cu 46.45±11.46% respectively 16.74±8.53%; in 203Hg 40.9±8.52% respectively 21.08±10.7%).