Utilization of bacterial activity for decolorization of coloured products is one the most promising industrial strategy, as an eco-sustainable and cost-competitive alter-native to physicochemical methods. Laccase production from Bacillus sp. was stud-ied for its decolorization influences on different dyes (Indian ink, Brilliant green, Bromothymol blue, Crystal violet, Safranin, Bromophenol blue, Methelen blue, Giemsa stain, Nigrosin, Toluidin blue, Neutral red, Phenol red, Hanna, Blood, Ben-gal rose B, Bromkresol green, 4-Bromoaniline, Aniline blue, 2,6-Dichlorophenol in-vophenol, Curcumin, Acridine orange, Indigo carmine, Xylene cynol FF,10G, Aliza-rine yellow GG and Kongorose). After 5 days of incubation of the spore-bound lac-case with different dyes, the maximum decolorization have seen in toluidin blue (89%), neutral red (84%), and indigo carmine (83%), brilliant green (82%) and acri-dine orange (82%), while the final percentage of degradation of other dyes were less than 65%. However, no additional redox mediator was added to the reaction, which suggests that this enzyme could be used in industries for effluents treatment. In addi-tion, our results indicate that the percentage of decolonization have decreased as the dyes concentrations were increased.
The current study aims to produce cellulase enzyme from Streptomyces spp. isolates and study the effect of some cultural conditions on cellulase production; biofuel production from cellulotic waste through enzymatic and acids hydrolysis. Out of 74 isolates of Streptomyces sp. were screened for cellulse production in solid and liquid media. Results showed higher capability of isolate Streptomyces sp. B 167 for cellulase production and bioconversion of cellulose, therefore selected for further studies. The results of optimization revealed that the cellulase enzyme productivity by the selected isolate reached 2.1 and 2.28 U/ml after 48 h of incubation time and pH 7 respectively. Cellulase productions in tested isolate improved (2.57 U/ml) b
... Show MoreThe current study aims to produce cellulase enzyme from Streptomyces spp. isolates and study the effect of some cultural conditions on cellulase production; biofuel production from cellulotic waste through enzymatic and acids hydrolysis. Out of 74 isolates of Streptomyces sp. were screened for cellulse production in solid and liquid media. Results showed higher capability of isolate Streptomyces sp. B 167 for cellulase production and bioconversion of cellulose, therefore selected for further studies. The results of optimization revealed that the cellulase enzyme productivity by the selected isolate reached 2.1 and 2.28 U/ml after 48 h of incubation time and pH 7 respectively. Cellulase productions in tested isolate improved (2.57 U/ml) b
... Show MoreThe objective of this study was to isolate and identify the asparaginase-producing bacteria, then purify and characterize the enzyme in order to investigate their properties in the future. Fifteen local bacterial isolates were isolated from various sites in the city of Baghdad, identified by conventional morphological and biochemical procedures, and confirmed using vitek 2 methods, and submitted to primary screening processes for asparaginase production. For secondary screening, eight isolates with the greatest yellow zone ability on a specific solid medium were chosen. Bacillus sp. was reported to have the highest enzyme production (7.5 U/mg proteins). After 24 hours of incubation, submerged fermentation yielded optimal conditi
... Show MoreThe reactive yellow azo dye (λmax = 420 nm) is widely utilized for textile coloring due to its low-cost stability and tolerance properties. Treatment of dye-containing wastewater by traditional methods is usually inadequate because of its resistance to biological and chemical degradation. From this research, the continuous reactor of an advanced oxidation method supported the use of H2O2/TiO2/UV to remove the coloration of the reactive yellow dye from the discharge. At constant best conditions obtained from the batch reactor tests pH=7, H2O2 dosage = 400 mg/l and TiO2=25mg/l , the aqueous solutions were tested in the continuous reactor at different dye concentration and d
... Show MoreIn this study three reactive dyes (blue B, red R and yellow Y) in single , binary and ternary solution were adsorbed by activated carbon AC in equilibrium and kinetic experiments. Surface area, Bulk and real density, and porosity were carried out for the activated carbon.
Batch Experiments of pH (2.5-8.5) and initial concentration (5-100) mg/l were carried out for single solution for each dye. Experiments of adsorbent dosage effect (0.1-1)g per 100 ml were studied as a variable to evaluate uptake% and adsorption capacity for single dyes(5, 10) ppm, binary and ternary (10) ppm of mixture solutions solution of dyes. Langmuir, and Freundlich, models were used as Equilibrium isotherm models for single solution. Extended Langmuir and Freun
Imidacloprid is systemic insecticide (1-[(6-chloro-3-pyridinyl) methyl]-N-nitro-2-imidazolidinimine) and the world’s most widely used has significant efficacy against a broad variety of pests and a unique mode of action by using it spreader and irrigation. The persistence of this pesticide in the soil means that it causes environmental damage that must be cleaned up. In this study collected and identified the best bacteria isolate that breakdown imidacloprid from the Plant Protection Director in Baghdad, which has been using neonicotinoid pesticides for years in their own greenhouse for pest control. Using high-performance liquid chromatography HPLC to measuring the residual concentrations of imidacloprid in MSM media at a concentration o
... Show MorePesticide biodegradation can be accomplished by the technique of bioremediation, which makes use of microorganisms’ ability to degrade pesticide residues. This study aimed to separate and identify imidacloprid-biodegradable from botanical fields soil of greenhouses in the Plant Protection Directorate /Ministry of Agriculture in Baghdad, which has been using imidacloprid pesticides for many years. Using high-performance liquid chromatography, residual imidacloprid concentrations in MSM medium at a concentration of 25 mg/L after 21 days were measured to identify the best degrading bacterial isolates. Isolate No.37 the best bacterial isolate was able to degrade 63% of imidacloprid. was
The bacteria Azotobacter Vinelandii was taken from a central research in Baghdad, The purification of alginic acid which produced from the bacteria by several steps starting with precipitation with isopropanol (3:1) v/v , Washing by ppt with 100ml of isopropanol : distilled water (3:1) v/v , then the ppt was dissolved in warm distilled water and dialysis against distilled water from 24 h/s . To Complete the purification , gel filtration chromatography was conducted on sephacryl s-100 column followed by ion – exchange chromatography . Using DEAE cellulose column . The molecular Weight of purified al ginic acid was higher than that of blue dextran 2000,It was more than (2) millions Dalton .<
... Show MoreTwenty isolates of Serratia marcescens were isolated from inflammation of the urinary tract (UTI)., These isolates were found to produce hemolysin as indicated by blood agar plates in which the hemolysis of red blood cell indicate a positive result. Isolates were selected according to their hemolysis activity by measuring absorbance of hemoglobin at 405 nm that released from red blood cell. Hemolysin was completely purified using 50-75% saturation of ammonium sulphate followed by ion exchange chromatography with DEAE-cellulose then gel filtration chromatography by sepharose 4B. Accordingly molecular weight for the purified toxin was estimated as 45 KD.
Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.