Sixty four local isolated of Klebsiella spp. have been isolated from environment samples (soil and water). These isolates were identified and diagnosis according to phenotype and biochemical tests. These isolates were subjected to primary and secondary screening, to select the isolate with the highest laccase activity. Fifteen isolates chosen from primary screening for screening their enzyme activity in secondary screening. It has been found the Klebsiella(K7) has the highest productivity of the enzyme (12 Unit/ml).Klebsiella(K7) isolate was diagnosis by Vitak 2 system, it was identified asK. pneumonia. The laccase purified was characterization, the experiments showed that: The molecular weight of laccase was 120KD and the optimum pH for the purified laccase activity was 4.5 and forstability was 6.5. the optimum temperature for enzyme activity was 40oC,the enzyme showed that laccase lost 22, 23 and 20% of its initial activity at 20, 25 and 35°C, respectively.
Specific microorganisms can produce bacterial nanocellulose (BNC), with acetic acid bacteria (AAB) being the most active producer. The family Acetobacteraceae includes the obligate aerobic, motile acetic acid bacteria. The BNC has attracted a lot of interest across a wide range of industries, including pharmaceuticals, due to its flexible characteristics, properties, and advantages. The present study was conducted to purify and characterize BNC produced from AAB isolated from apple vinegar. Bacterial nanocellulose was synthesized using a natural date palm liquid medium at pH 6 at 30°C for 8–10 days. The bacterial cellulose produced was then purified using a technique involving 0.1 M sodium hydroxide. To ascertain the surface mor
... Show MoreBackground: Pumpkin seeds are a valuable source of high-quality protein and can be utilized as functional food ingredients due to their properties, such as solubility, foam formation, and stability. This study aims to produce protein isolate and its enzymatic hydrolysates from local pumpkin seeds to study their properties. Methodology: Preparing defatted pumpkin seeds for protein extraction, followed by the enzymes’ hydrolysis using Trypsin and Pepsin enzymes separately and together in two methods. The determination of amino acids and the degree of hydrolysis was conducted; moreover, protein properties were studied, including solubility, emulsifying activity, stability index, foaming capacity, and stability. Results: A protein sample was
... Show MoreThis research was aimed to the purification and characterization of cytosine deaminase as a medically important enzyme from locally isolated Escherichia coli; then studying its cytotoxic anticancer effects against colon cancer cell line. Cytosine deaminase was subjected to three purification steps including precipitation with 90% ammonium sulfate saturation, ion exchange chromatography on DEAE-cellulose column, and gel filtration chromatography throughout Sephadex G-200 column. Specific activity of the purified enzyme was increased up to 9 U/mg with 12.85 folds of purification and 30.85% enzyme recovery. Characterization study of purified enzyme revealed that the molecular weight of cytosine deaminase produced by E. coli was about 48 KDa,
... Show MoreThe ability of four local fungal isolates for extracellular laccase production has been tested with five grams 1:1(w/v) humidified sawdust as substrate in mineral salt medium. After 21 day of incubation at 25±1 ? C and using one mycelial plug (5mm), higher level of laccase activity (0.15U/ml) and specific activity (15U/mg) were observed by Pleurotus ostreatus in comparison with other fungal isolates. The results of optimum conditions for laccase production from selected isolate showed that, the maximum laccase activity (0.55U/ml) and specific activity (55U/mg) were obtained at moisture ratio 1:3 (w/v), using 3 mycelial plugs (5 mm), after 15 days incubation period at 25±1 ? C. The results of phenol degradation by crud laccase revealed th
... Show MorePolycyclicacetal was prepared from the reaction of PEG with aldehyde derived from Erythro-ascorbic acid (pentulosono-ɣ-lactone-2,3-enedianisoate).All these compounds were characterized by Thin Layer Chromatography (TLC) and FTIR spectra and aldehyde was also characterized by (U.V-Vis), 1HNMR, 13CNMR, and mass spectra.The inhibitory effect of prepared polymer on the activity of human serum AcetylCholinesterase has been studied in vitro. The polymer showed a remarkable activity at low concentration (4.7x10-3 – 4.7x10-8M).
This work describes the enhancement of phenol red decolorization through immobilizing of laccase in chitosan and enzyme recycling. Commercial laccase from white rot fungus, Trametesversicolor (Tvlac), was immobilizedin to freshly prepared chitosan beads by using glutaraldehyde as a cross linker. Characterization of prepared chitosan was confirmed by FTIR and scanning electron microscope (SEM). Tvlac (46.2 U/mL) immobilized into chitosan beads at 0.8 % glutaraldehyde (v/v) within 24 hrs. Synthetic (HBT) and natural (vanillin) mediators were used to enhance dye decolorizoation. It was found that 89 % of phenol red was decolorized by chitosan beads within 180 min. in the absence of enzyme and mediator, while decolorization percenta
... Show MoreNowadays, there is increased interest in the biosynthesis of microbial melanin related to their numerous biological functions and applications in many fields, especially in medical fields, including immune-modulating, antimicrobial antibiotic, antiviral antivenin, anticancer, antitumor activity, and anti-biofilm activity. Pyomelanin is a hydrophobic macromolecule that is typically dark brown or black in color, formed by the oxidative polymerization of phenolic or indolic compounds. Pyomelanin is reported to be safe for consumption, thus providing a crucial strategy for biocontrol of biofilm. Furthermore, natural pyomelanin is known as a potent antioxidant, photoprotective, and free radical scavenging. Objective: This study focuses on the
... Show MoreSome of the characters of the Staphylolysin A and D enzymes purified from Pseudomonas aeruginosa P16 and P5 respectively were studied, the molecular weights of Staphylolysin A and D were 20.417 kilo dalton and 23.988 kilo Dalton respectively by SDS- polyacryl amide gel electrophoresis. The optimum pH for staphylolysin A activity was found to be 8 which gives higher activity reaches 150 unit/ml, and for enzyme stability was 7.5-8.5 in which the enzyme nearly retained its full activity, while it was 9.5 for staphylolysin D that gives higher activity of 16 unit/ml,and 8.5-9.5 for enzyme stability in which the enzyme nearly retained its full activity, Maximum activity of two enzymes was obtained at 40C in which the specific activity for st
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