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Protease-Based Enzymatic Pretreatment Enhances Biodegradability of Dairy Wastewater Purification and SEC-HPLC Molecular Evidence
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Abstract<p> The large protein clumps in dairy effluent make it harder for microbes to break down the waste, making traditional biological treatment methods less effective. This research generated an extracellular protease from Pseudomonas aeruginosa, partially purified it, and utilized it as an enzymatic pretreatment to improve substrate accessibility for biological processes. The purification method, which included ammonium sulfate precipitation and dialysis, raised the specific activity from 1.21 to 20.26 U mg <sup>−1</sup> . This meant that the active enzyme fraction had been made stronger. Size-exclusion high-performance liquid chromatography (SEC-HPLC) was used to evaluate molecular changes in protein-rich wastewater. Following enzymatic treatment, chromatographic profiles showed a big change from early-eluting high-molecular-weight protein fractions to late-eluting low-molecular-weight peptides. This was clear proof of proteolytic cleavage. This structural transformation significantly altered on the physical and chemical properties of organic nitrogen, but it didn’t change the amount of organic matter. Biodegradability studies showed that samples that had been treated with enzymes used more oxygen in the first stage of decomposition. The high biochemical oxygen demand (BOD) and chemical oxygen demand (COD) levels did not mean that pollution was getting worse instead, they meant that microbial oxidation was happening faster because bacteria could get to soluble substrates more easily. The BOD/COD ratio showed that the speed of biodegradation was getting better. Enzymatic hydrolysis turned slowly biodegradable particulate COD into soluble parts that break down quickly. A mechanistic link exists between protein fragmentation and improved biological treatment effectiveness when enzyme purification, molecular-scale chromatographic analysis, and biodegradation performance evaluation are utilized simultaneously. The findings demonstrate that protease-based pretreatment is a viable and energy-efficient approach for mitigating hydrolysis issues in activated sludge systems. This could be a good way to deal with dairy waste that is high in protein. </p>
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Publication Date
Sun Mar 07 2010
Journal Name
Baghdad Science Journal
Identification and Purification of Cholera Like Toxin from Environmental Isolate of Vibrio cholerae
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The presence and prevalence of V. cholerae were investigated in forty five water samples collected from different locations of Tiger River/ Baghdad city. Twenty one isolates were isolated by adopting a simple isolation techniques. The final identification revealed that only three isolates were confirmed as V. cholerae. They were named 1J, 1R and Dial 131 which are all serogrouped as non-O1. Toxin Coregulated Pili (TCP) and heat labile enterotoxin (LT) were determined in only the environmental isolate 1J while non of the isolates produced heat stabile toxin (ST). The purification scheme was improved, few steps were adopted to include back extraction of ammonium sulfate, saturation between 80-20%, desalting through Sephadex G25, and gel filt

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Publication Date
Sun Mar 01 2009
Journal Name
Baghdad Science Journal
Purification and Characterization &#946; - lactamase produce from local isolate Klebsiella pneumonia
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Beta-lactamase was purified from local isolate Klebsiella pneumonia by several steps included precipitation with ammonium sulphate at 20-40% saturation, DEAE- ion exchange chromatography and gel filtration on Sephacryl S-200 column. The obtained purification fold and recovery were 32.66; 47.04% respectively. The characterization of the purified beta-lactamase showed that the molecular weight was about 4000 daltons as determined by gel filtration.Purified enzyme had an optimal pH of 7 for activity and an optimal stability between pH 6.5-7.5, results shows that the optimal temperature appear to be 35 ? C .During storage the enzyme retained 72% at -20 ? C and retained 25% of the activity at the same period at 4 ? C.

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Publication Date
Mon Aug 14 2017
Journal Name
Oriental Journal Of Chemistry
Leucine Aminopeptidase from Arachis hypogaea L. Seeds Partial Purification and Characterization
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Leucine amino peptidases (LAP; EC 3.4.11.1) constitute a diverse set of exopeptidases that catalyze the hydrolysis of leucine residues from the amino-terminal of protein or peptide substrates, (LAP) are present in animals, plants, and microbes. In this study, leucine amino peptidase was purified partial from Arachis hypogaea seeds by using gel filtration chromatography Sephadex G-100. The enzyme was purified 3.965 fold with a recovery of 29.4%. Its pH and temperature optimum were(8.7) and (37oC), respectively. The results show novel properties of LAP from Arachis hypogaea L. or peanut. The Km value for LAP (77 mM), with V max (1538 m mole min-1). We recommend a separate isoenzymeof the enzyme (LAP) from Arachis hypogaea on L. peanut seeds a

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Publication Date
Sat Sep 30 2023
Journal Name
Iraqi Geological Journal
Purification of Aqueous Solutions from Nickel Using Ceramic Waste
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This study aims to test ceramic waste's capacity to remove nickel from aqueous solutions through adsorption. Ceramic wastes were collected from the Refractories Manufacturing Plant in Ramadi. Through a series of lab tests, the reaction time (5, 10, 15, 20, 25, 30, 35, 40, 45, and 50 minutes, and Ni concentrations (20, 40, 60, and 80) were tested using ceramic wastes with a solid to liquid ratio of 2g/30ml. At a temperature of 30ºC, the pH, total dissolved solids (TDS), and electrical conductivity (EC) were all measured. The equilibrium time was set at 30 min. Thereafter, the sorption (%) somewhat increased positively with the Ni concentration. Freundlich's equation showed that the adsorption intensity is 1.1827 and the Freundlich c

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Publication Date
Sun Dec 07 2008
Journal Name
Baghdad Science Journal
Optium Conditions for the Production of Neutral Protease from local strain Aspergillus niger var cabonarius
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The optimum conditions for the production of neutral protease from local strain Aspergillus niger var carbonarius by solid – state fermentation system (Wheat bran) moisted with 0.2 M phosphate buffer (PH7.0) . the hydration ratio was 1:5 (V:W) . the concentration of inoculum was 1×106 spores per 10 gram of solid materials , initial P H 6.5 and 96 hours of incubation period at 30? C .the enzyme activity was 1300 unit / ml and specific activity was 1550 unit / mg protein .

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Publication Date
Sat Nov 01 2025
Journal Name
Russian Journal Of General Chemistry
Synthesis, Antibacterial Activity, and Molecular Docking Study of Some New Azo Derivatives Based on 2(4-Aminophenyl)-5-Substituted 1,3,4-Oxadiazole
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Publication Date
Mon Jan 01 2024
Journal Name
Open Life Sciences
Evaluation of the role of some non-enzymatic antioxidants among Iraqi patients with non-alcoholic fatty liver disease
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Abstract<p>Non-alcoholic fatty liver disease (NAFLD), characterized by hepatic fat accumulation in individuals consuming little or no alcohol, has become highly prevalent globally. Oxidative stress plays a central role in instigating inflammation and cell death pathways driving NAFLD progression. This case–control study aimed to elucidate the association between circulating levels of the pivotal non-enzymatic antioxidants – coenzyme Q10 and vitamins E and C – and liver injury parameters among 60 Iraqi NAFLD patients versus 30 healthy controls. NAFLD diagnosis entailed over 5% hepatic steatosis on ultrasound excluding other etiologies. Patients spanned three age groups: 20–29, 30–39, an</p> ... Show More
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Publication Date
Sun Dec 01 2019
Journal Name
Baghdad Science Journal
Extraction, Purification and Characterization of Peroxidase from Pseudomonas aeruginosa and Utility as Antioxidant and Anticancer
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        Peroxidase is a class of oxidation-reduction reaction enzyme that is useful for accelerating many oxidative reactions that protect cells from the harmful effects of free radicals. Peroxidase is found in many common sources like plants, animals and microbes and have extensive uses in numerous industries such as industrial, medical and food processing. In this study, P. aeruginosa was harvested to utilize and study its peroxidases. P. aeruginosa was isolated from a burn patient, and the isolate was verified as P. aeruginosa using staining techniques, biochemical assay, morphological, and a sensitivity test. The gram stain and biochemical test result show rod pink gram-ne

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Publication Date
Tue Feb 01 2022
Journal Name
Baghdad Science Journal
New Tetra-dentate Schiff Base Ligand N2O2 and Its Complexes with Some of Metal Ions: Preparation, Identification, and Studying Their Enzymatic and Biological Activities
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In present work, new tetra-dentate ligand, titled 3,5-bis ((E)-5-Bromo-2-hydroxy benzylidene amino) benzoic acid (H3L), was prepared via an acid-catalyzed condensation process. New four metallic ligand complexes with Co(II), Ni(II), Cu(II) and Zn(II) ions, were also prepared from the refluxing of equivalent moles. Ligand's structure and its complexes; were confirmed by numerous characterization methods, including Ultraviolet-Visible, Infrared, Mass Spectrometer, 1H and 13C Nuclear Magnetic Resonance spectra, atomic absorption, magnetic moments, and molar conductivity measurements. The results of the spectroscopic analyzes proved that the prepared ligand acts as tetradentate bi-ionic ligand and it was bond

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Publication Date
Sun Mar 02 2008
Journal Name
Baghdad Science Journal
Extraction and Purification of Indole aectic acid from locale isolate Fusarium oxysporum(F2)
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Indole acetic acid (IAA) produced from F. oxysporum (F2) was purified by several steps included extraction by cold ethyl acetate ; Column chromatography using silica gel and TLC chromatography . The pure indole acetic acid (IAA) which produce by F. oxysporum (IAA) was tested by ultraviolet spectra at (200-300)nm ; and appear that the maximum absorbance at 229nm , the high performance liquid chromatography (HPLC) used to test the purity of the indole acetic acid and the results showed one peak at appearance time 3.822 min

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