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

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

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.

Abstract :In this study, amygdaline in Iraqi plant seeds was extracted and isolated from their seeds matrix using reflux procedure and subsequently identified and determined by high performance liquid chromatography (HPLC) on reversed phase column of LC-18 (150mm x 4.6mm, 5?m )with actonitrile :water ( 50 : 50 ) as mobile phase at flow rate of ( 0.5 mL/min ) and detection at wavelength of 215 nm.The experimental results indicated that the linearity of calibration is in the range of 1.0-30.0 mg L-1amygdaline with the correlation coefficient of 0.9949. The limit of detection (LOD) and limit of quantitation (LOQ) for amygdaline were of 0.88 and 2.93 mg L-1 in standard pure sample. The mean recovery percent is 97.34±0.58 at 95% confidence inte

Biofilm formation is one of the biggest challenges of scientists. Role of heavy metals in forming biofilm is not clear enough. Here, the effect of lead on biofilm formation by Bacillus spp. isolated from soil in terms of biofilm formation and remove was studied. In present study, 10 isolates of Bacillus spp were isolated from soil. The ability of all isolates to form biofilm was evaluated. The effect of lead on biofilm formation was studied by adding lead (pb) before forming biofilm. In another experiment the lead was added after biofilm formation to study the effect of lead on biofilm remove. The current study, showed the ability of all studied isolates to form biofilm. Maximum biofilm formation by Bacillus spp isolate number 8 (B8) follow

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

In Paracoccus denitrificans Pd1222 bacterium, Pden_3633 encoding gene has been nominated to encode for Isovaleryl CoA dehydrogenase (IVDH) [1], the enzyme which involve in leucine catabolism pathway. In this study, this putative IVDH was investigated. IVDH encoding gene from P. denitrificans Pd1222 in addition to desired features for cloning, expression and purification have been designed and synthesized. The synthetic coding sequence was expressed in Escherichia coli. The enzyme was purified as a Strep-Tagged protein with a total protein 220.5 mg. An apparent molecular weight of 42.9 kDa was determined on SDS gel. Amino acid alignment showed a very high similarity (91-96%) with corresponding IVDH from several other Paracoccus species. A

This study was performd on 50 urine specimens of patients with type 2 diabetes, in addition, 50 normal specimens were investigated as control group. The activity rate of maltase in patients (6.40±2.17) I.U/ml and activity rate of maltase in normal (0.44±0.20)I.U/ml. The results of the study reveal that maltase activity of type 2 diabetes patient's urine shows significant increase (P<0.01) compare to normal.

Proteinases (E.C.3.4.21) family are widely distributed in the nature; it was present in animals tissues , plants and microbial cell . Protease was purified from Zahdi seed (Phoenix dactylifera L.) by several steps included ammonium sulphite ppt (75%) saturation and dialyzed against the 80mM sodium phosphate buffer at pH 7.5 . The enzyme specific activity was 407.62 unit/mg protein. The obtained extract was purified by DEAE-Cellulose column followed by gel filtration through Sephacyl S-200 column .The enzyme specific activity ,yield and purification fold were 1873.49 unit/mg protein, 22.99 and 58.42% respectively. The results of protease characterization showed that the molecular weight was 25118 daltons as determined by gel f

An extracellular β-galactosidase from the thermophilic fungus Rhizomucor
Pusillus IB8 has been purified via several steps included precipitation by ammonium
sulphate at 80 % saturation, DEAE- Cellulose Ion exchange chromatography and gel filteration on sepharose CL-6B column. The Final purification folds and the yield of the enzyme were 42.5 and 24.8 % respectively. The purified β-galactosidase has an optimum pH for its activity between 4.5 to 5, while the optimum pH for enzyme stability was between 5 to 5.5. Futhermore, it was found that the optimum temperature for its activity was 60 C°. The purified enzyme retained approximatly 98% of its original activity when incubated at 60 C° for 60 min. However, 25 % of its activity was