scholarly journals DEGRADATION OF REACTIVE DYES USING IMMOBILIZED PEROXIDASE PURIFIED FROM NIGELLA SATIVA

2021 ◽  
Vol 52 (6) ◽  
pp. 1365-1374
Author(s):  
G. M. Aziz ◽  
S. I. Hussein ◽  
S. D. Abbass ◽  
A. L. Ibrahim ◽  
D. K. Abbas
Keyword(s):  
Removal Efficiency ◽  
Immobilized Enzyme ◽  
Specific Activity ◽  
Nigella Sativa ◽  
Gel Filtration ◽  
Textile Dyes ◽  
Sodium Acetate Buffer ◽  
Optimum Conditions ◽  
Maximum Removal ◽  
Final Purification

 The present study was aimed to exploit the free and immobilized peroxidase from Nigella sativa seeds to degradation of textile dyes polluting the environment and water. The optimum conditions for extracting the enzyme from the Nigella seeds were determined and the highest specific activity of the enzyme was obtained 1750 units / mg protein when extracting the enzyme from the ground seeds at a ratio of 1:20 (w: v) with sodium acetate buffer at 0.2 M and pH 5.0 for 15 minutes. The enzyme was purified using two steps including the concentration by sucrose and gel filtration by using Sephadex G-150. The results shown an increase in final purification folds 2.8 time with an enzyme yield of 35%. The immobilization of peroxidase were done by entrapment method using Ca- alginate and the immobilization ratio was reached to 49%. The removal efficiency of dyes by crude enzyme (free, immobilized) and partial purified peroxidase were studied with textile dyes such as yellow, red, black and blue dyes at optimum conditions pH 5, temperature 37oC after 3 hr. Maximum removal efficiency of dyes observed with crude peroxidase and reached (76.9, 88.7, 91 and 88) % respectively. These results were close to the efficiency of the purified enzyme in removing the four dyes, while the efficiency of the crude immobilized enzyme in removing the dyes was about (70, 81, 72 and 56.4)%, respectively.

scholarly journals DETERMINATION OF THE OPTIMUM CONDITIONS FOR UREASE INHIBITTION EXTRACTED FROM SOME LOCAL PLANTS

2021 ◽  
Vol 52 (4) ◽  
pp. 802-809
Author(s):  
Hussein & et al.
Keyword(s):  
Specific Activity ◽  
Extraction Ratio ◽  
Inhibition Activity ◽  
Sodium Acetate Buffer ◽  
Optimum Conditions ◽  
Extraction Buffer ◽  
Urease Enzyme ◽  
Local Plants ◽  
Optimum Extraction

In the current study, four types of plants commonly used namely Soybean, chickpea, bean, pea were obtained and screened for urease activity, among this plants, chickpea was chosen with maximum enzymatic activity, and it had the highest productivity of urease enzyme (1243 U/mg protein). Also sodium acetate buffer (0.2 M, pH 5.0) was chosen as a best extraction buffer with specific activity 1460 U/mg protein. The optimum extraction ratio represented by 1:8 (w:v) after 15 min, it was given 1988 U/mg protein. As well as four types of plants include garlic, red onion, green onion and cabbage were used to select the optimum plant material that inhibited urease enzyme. Cabbage was chosen, it had the highest inhibition activity of the enzyme (41%). Also tris buffer (0.2 M, pH 9) was selected as a best extraction buffer of plants inhibitor with inhibition activity 80%. The optimum extraction ratio represented by 1:8 (w:v) after 60 min, it was given 86% enzyme inhibition activity.

scholarly journals DEGRADATION EFFICIENCY OF PHENOLIC COMPOUNDS USING IMMOBILIZED PEROXIDASE PURIFIED FROM SOYBEAN

2019 ◽  
Vol 50 (3) ◽  
Author(s):  
Jasim & Aziz
Keyword(s):  
Phenolic Compounds ◽  
Gallic Acid ◽  
Gel Filtration ◽  
Textile Dyes ◽  
Degradation Efficiency ◽  
Agarose Gel ◽  
Covalent Linkage ◽  
Whole Plant ◽  
Peroxidase Enzyme ◽  
Maximum Removal

This study was aimed on purification, immobilization and application of peroxidase enzyme from whole plant of soy bean for the decolorization of textile dyes and degradation of some phenolic compounds. The purification of peroxidase was in two steps include: concentration by sucrose and gel filtration by using sephadex G-150. The purification fold was 4.46 and 2.09 with an enzyme yield of 22.34% and 25.55% for peak 1 and peak 2 respectively. The purified peroxidase enzyme was immobilized by two methods include: covalent linkage immobilization by gluteraldehyde activated chitosan and entrapment by sodium alginate and agarose gel, the immobilization ratio reached to 58.07%, 50% and 11.75% respectively. Crude, purified and immobilized peroxidase were studied with textile dyes (red, blue, yellow and black) after 24 hr, the maximum removal efficiency was with immobilized peroxidase reached to 13.25, 35.12, 14.37 and 26.92 % respectively. Immobilized peroxidase on chitosan was able to degrade some phenolic compounds (tannic acid, naphthalene and gallic acid) during 2 hr, and the degradation efficiency was reached to 95.85%, 79.75% and 33.88% respectively.

Adsorption of crystal violet dye by a zeolite-montmorillonite nano-adsorbent: modelling, kinetic and equilibrium studies

Clay Minerals ◽  
2019 ◽  
Vol 54 (4) ◽  
pp. 357-368 ◽  
Author(s):  
Malihe Sarabadan ◽  
Hadis Bashiri ◽  
Seyed Mahdi Mousavi
Keyword(s):  
Removal Efficiency ◽  
Crystal Violet ◽  
Freundlich Isotherm ◽  
Optimum Conditions ◽  
Experimental Conditions ◽  
Equilibrium Studies ◽  
Adsorbent Dosage ◽  
Crystal Violet Dye ◽  
Nano Adsorbent ◽  
Maximum Removal

AbstractA zeolite-montmorillonite (zeolite-Mt) nano-adsorbent was prepared by calcination at 600°C. The synthesized nano-adsorbent was tested for removal of a toxic and cationic dye (crystal violet) from water, and it was characterized by various techniques. The effects of variables such as pH, temperature, adsorbent dosage and initial dye concentration on the removal efficiency of the dye were investigated by response surface methodology (RSM). Experimental conditions were optimized by RSM to achieve the maximum dye removal efficiency. Optimum conditions for maximum removal of dye were obtained at pH 9, temperature of 25°C, adsorbent dosage of 2 g L−1 and initial dye concentration of 40 mg L−1. Under these conditions, the maximum removal efficiency obtained was 99.9%. Various isotherms were applied to study adsorption equilibrium, and of these, the Freundlich isotherm provided the best fit. In addition, the fractal-like integrated kinetic Langmuir model was the most appropriate among several kinetic models. The thermodynamic parameters were also determined. The zeolite-Mt prepared under optimum conditions displayed a greater adsorption capacity than activated carbon (manufactured by Merck) and than various other adsorbents.

scholarly journals Removal of malachite green from aqueous solutions by electrocoagulation/peanut shell adsorption coupling in a batch system

2017 ◽  
Vol 75 (8) ◽  
pp. 1830-1838 ◽  
Author(s):  
Xiansheng Wang ◽  
Jiaheng Ni ◽  
Shuo Pang ◽  
Ying Li
Keyword(s):  
Malachite Green ◽  
Removal Efficiency ◽  
Current Density ◽  
Energy Demand ◽  
Operating Time ◽  
Peanut Shell ◽  
Optimum Conditions ◽  
Batch System ◽  
Unit Energy ◽  
Maximum Removal

A electrocoagulation (EC)/peanut shell (PS) adsorption coupling technique was studied for the removal of malachite green (MG) in our present work. The addition of an appropriate PS dosage (5 g/L) resulted in remarkable increase in the removal efficiency of MG at lower current density and shorter operating time compared with the conventional EC process. The effect of current density, pH of MG solution, dosage of PS and initial concentration of MG were also investigated. The maximum removal efficiency of MG was 98% under optimum conditions in 5 min. And it was 23% higher than that in EC process. Furthermore, the unit energy demand (UED) and the unit electrode material demand (UEMD) were calculated and discussed. The results demonstrated that the EC/PS adsorption coupling method achieved a reduction of 94% UED and UEMD compared with EC process.

scholarly journals EFFECIENCY OF IMMOBILIZED POLYPHENOL OXIDASE ON SOME TEXTILE DYES DEGRADATION USING BATCH OPERATION SYSTEM BY PACKED BED BIOREACTOR

2019 ◽  
Vol 50 (3) ◽  
Author(s):  
S. I. Hussein
Keyword(s):  
Solanum Lycopersicum ◽  
Polyphenol Oxidase ◽  
Removal Efficiency ◽  
Gel Filtration ◽  
Packed Bed ◽  
Textile Dyes ◽  
Textile Dye ◽  
Operation System ◽  
Packed Bed Bioreactor ◽  
Batch Operation

In the current study, three types of common plants, namely Tomato (Solanum lycopersicum), Cucumber (Cucumis sativus) and Orange (Citrus sinensis) were obtained and screened for their polyphenol oxidase (PPO) activity, Among the three plants, Solanum lycopersicum was chosen with maximum enzymatic activity, it had the highest productivity of the enzyme (23733 U/mg protein).The PPO from Solanum lycopersicum was purified using two steps: concentration by sucrose and gel filtration by using Sephacryl S-200. The results showed an increase in the final purification folds by 2.4 times with an enzyme yield of 32.6%. The immobilization studies showed that PPO was more stable when immobilized on chitosan by covalent linkage with immobilization ratio of 62%, in comparison with agar-agar by entrapment method (36%). The removal efficiency of crude and partial purified PPO was studied with textile dyes, including yellow, red, black and blue dyes at optimum conditions: pH 5, temperature 40oC after 3 hrs. Maximum removal efficiency of dyes observed with crude PPO were 53.9, 81.4, 86.5 and 79.6% respectively. However, purified PPO displayed removal efficiency reached 60.3, 84.3, 84.6 and 77.5% respectively. The potential of immobilized PPO on chitosan was evaluated by decolorization of black textile dye in packed bed bioreactor in batch operation. The results indicated that immobilized PPO in batch operation has the ability to remove 99% of the dye after 2 hrs, and the results showed a positive relationship between the degradation rate and incubation time in batch operation.

scholarly journals Decolorization of textile dyes by partially purified Pleurotus ostreatus laccase

2014 ◽  
Vol 8 (3) ◽  
pp. 64-69
Author(s):  
Shamam saady Abdulredha ◽  
Abdulkareem jasim Hashim ◽  
Abduljabar Abas Ali ◽  
Batool Imran Dheeb
Keyword(s):  
Solid State ◽  
Pleurotus Ostreatus ◽  
Specific Activity ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Textile Dyes ◽  
Optimum Temperature ◽  
Optimum Conditions ◽  
Optimum Ph ◽  
Ph Range

Pleurotus ostreatus produced 2.93 U/mg of laccase in solid state fermentation (SSF) using barley bran as substrate under optimum conditions. The optimum SSF conditions were: pH 6.5; temperature, 25Cº; inoculums size 3.5 mm and moisture content, 1:1.5 w/v. Laccase was partially purified 8.29 fold with specific activity 17.5 U/mg by ion exchange chromatography after curd enzyme concentrated by dialysis against the solid sucrose. Partially purified laccase had an optimum pH of 6.5 and was stable in the pH range from 6.5 to 7.5. The optimum temperature was 45 Cº and it displayed considerable stability within the range 15 to 45 Cº with 1h incubation as well as The ability of partial purified laccase to decolorize of textile dyes showed that the blue H3R dye was completely decolorized in all concentrations within first min while yellow FG and red 3B dyes were decolorized in different percentage.

scholarly journals Purification and properties of sheep liver phosphofructokinase

1969 ◽  
Vol 113 (2) ◽  
pp. 235-242 ◽  
Author(s):  
D. J. H. Brock
Keyword(s):  
Ammonium Sulphate ◽  
Specific Activity ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Optimum Conditions ◽  
Sheep Liver ◽  
A Value ◽  
Purification And Properties ◽  
Ammonium Sulphate Fractionation ◽  
Citrate Inhibition

1. The activity of phosphofructokinase in sheep liver was found to be dependent on the composition and molarity of the buffer used in extraction. Under optimum conditions a value of 4–7μmoles/min./g. wet wt. of tissue was obtained. 2. The enzyme was purified 480-fold by a combination of ammonium sulphate fractionation, heat treatment in the presence of ethanol, DEAE-cellulose chromatography and Sephadex G-200 gel filtration. The final specific activity was 18·5μmoles/min./mg. of protein. 3. The purified enzyme was inhibited by ATP and citrate, the degree of inhibition depending on the concentration of fructose 6-phosphate, magnesium chloride and ammonium sulphate, as well as on the pH. ATP and citrate inhibition was overcome by AMP and fructose 1,6-diphosphate. 4. The enzyme was also inhibited by NADH and NADPH in a manner largely independent of other components of the assay medium. AMP and fructose 1,6-diphosphate were not able to overcome this type of inhibition. 5. Octanoate was not an inhibitor of phosphofructokinase. 6. Differences between these results and those of other workers are discussed.

scholarly journals Evaluation of the performance of titanium and zirconium salts as coagulants in industrial wastewater treatment: pollutant removal, sludge production, and sludge characteristics

2021 ◽  
Vol 11 (4) ◽  
Author(s):  
Ayla Uysal ◽  
Eda Boyacioglu
Keyword(s):  
Wastewater Treatment ◽  
Removal Efficiency ◽  
Industrial Wastewater ◽  
Pollutant Removal ◽  
Volume Index ◽  
Optimum Conditions ◽  
Industrial Wastewater Treatment ◽  
Residual Sludge ◽  
Removal Efficiencies ◽  
Maximum Removal

AbstractIn this study, titanium tetrachloride (TiCl4), zirconium tetrachloride (ZrCl4), and zirconium oxychloride (ZrOCl2·8H2O) were evaluated using jar test experiments as coagulants and compared with traditional aluminum sulfate (Al2(SO4)3·18H2O) and ferric chloride (FeCl3) for industrial wastewater treatment. The effects of the initial pH of 4–10 and initial coagulant doses of 10–100 mg/L on chemical oxygen demand (COD) and total suspended solids (TSS) removal were investigated. The performances of the five coagulants were also assessed in terms of the settled sludge volume, the sludge volume index (SVI), and removal efficiencies of metals, color, and total phosphorus (TP) under optimum conditions. In addition, the contents of the residual sludge produced for all five tested coagulants under optimum conditions were determined. The results showed that the maximum removal efficiency of COD (69.33%) was achieved using 100 mg/L TiCl4 at pH 8. The maximum removal efficiency of TSS (98.32%) was achieved using 50 mg/L Al2(SO4)3·18H2O at both pH 8 and 10. The settled sludge volume and SVI generated by TiCl4 were lower than that for the other four tested coagulants. ZrCl4, ZrOCl2·8H2O, FeCl3, and Al2(SO4)3·18H2O resulted in 128.13, 92.39, 72.26, and 69.66 mL/g SVI, while that using TiCl4 was 48.84 mL/g. Ti- and Zr-based coagulants achieved better removal efficiencies of TP, Zn, and Cu than FeCl3 and Al(SO4)3·18H2O. The residual sludge from using Ti and Zr coagulants had a very high TP content. The results indicated that Ti- and Zr-based coagulants could be used as alternatives to traditional coagulants for industrial wastewater treatment.

On the Preparation of Bovine α-Thrombin

1978 ◽  
Vol 39 (01) ◽  
pp. 193-200 ◽  
Author(s):  
Erwin F Workman ◽  
Roger L Lundblad
Keyword(s):  
Immobilized Enzyme ◽  
Catalytic Properties ◽  
Specific Activity ◽  
Guanidine Hydrochloride ◽  
Low Molecular Weight ◽  
Reversible Process ◽  
Gel Beads ◽  
Tissue Thromboplastin ◽  
C 50 ◽  
Hydrolysis Of

SummaryAn improved method for the preparation of bovine α-thrombin is described. The procedure involves the activation of partially purified prothrombin with tissue thromboplastin followed by chromatography on Sulfopropyl-Sephadex C-50. The purified enzyme is homogeneous on polyacrylamide discontinuous gel electrophoresis and has a specific activity toward fibrinogen of 2,200–2,700 N.I.H. U/mg. Its stability on storage in liquid media is dependent on both ionic strenght and temperature. Increasing ionic strength and decreasing temperature result in optimal stability. The denaturation of α-thrombin by guanidine hydrochloride was found to be a partially reversible process with the renatured species possessing properties similar to “aged” thrombin. In addition, the catalytic properties of a-thrombin covalently attached to agarose gel beads were also examined. The activity of the immobilized enzyme toward fibrinogen was affected to a much greater extent than was the hydrolysis of low molecular weight, synthetic substrates.

Isolation and Characterization of Plasminogen Activator from Pig Leucocytes

1974 ◽  
Vol 31 (01) ◽  
pp. 072-085 ◽  
Author(s):  
M Kopitar ◽  
M Stegnar ◽  
B Accetto ◽  
D Lebez
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Ph Optimum ◽  
Isolation And Characterization ◽  
Ph Range ◽  
Inhibition Studies ◽  
Final Purification

SummaryPlasminogen activator was isolated from disrupted pig leucocytes by the aid of DEAE chromatography, gel filtration on Sephadex G-100 and final purification on CM cellulose, or by preparative gel electrophoresis.Isolated plasminogen activator corresponds No. 3 band of the starting sample of leucocyte cells (that is composed from 10 gel electrophoretic bands).pH optimum was found to be in pH range 8.0–8.5 and the highest pH stability is between pH range 5.0–8.0.Inhibition studies of isolated plasminogen activator were performed with EACA, AMCHA, PAMBA and Trasylol, using Anson and Astrup method. By Astrup method 100% inhibition was found with EACA and Trasylol and 30% with AMCHA. PAMBA gave 60% inhibition already at concentration 10–3 M/ml. Molecular weight of plasminogen activator was determined by gel filtration on Sephadex G-100. The value obtained from 4 different samples was found to be 28000–30500.

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