Seven [35%] and five [25%] Serratia marcescens  isolates were obtained out of 20 samples of lettuce and 20 samples of spinach, respectively, taken from different locations in a farm in Baghdad city. The isolate that produced chitinase in higher level was chosen to purify chitinase through several stages of purification including: ammonium sulfate precipitation, DEAE- sephadex ion exchange chromatograpgy and sephadex G-200 gel filtration with 89.5- fold purification and 30% recovery.       The purified chitinase was characterized and the molecular weight of enzyme was 59000 daltons by using gel filtration chromatography. The optimum pH and temperature of the purified chitinase were 6.0 and 50°

Lipoxygenase was extracted from the cup of Pleurotus ostreatus ( Jaq : Fr ) oyster mushroom for the first time in Iraq, and purified homogeneously through precipitation with 40% saturation of (NH4)2SO4 as a partial purification then loaded on DEAE-Cellulose (Diethyl amino ethyl Cellulose) ion-exchange chromatography column and then the highly active elution parts have been passed through gel filtration column with Sephacryl S-300 as a final purification with 804 (U/mg protein) specific activity, 11.32 fold of purification and 36.54% yield . The molecular weight of the enzyme was estimated to 74 KDa by gel filtration Sephacryl S-300 column and the isoelectric point for enzyme was 5.3. The optimal pH for lipoxygenase activity and stability

Catalase (EC 1.11.1.6) is a well known enzyme which exists in almost all living creatures exposing to oxygen (such as plants, bacteria, and animals). It is a very necessary enzyme to protect the cell from oxidative detriment by reactive oxygen species (ROS). The aim of this study is the partial purification and characterization of Catalase enzyme from Banana peels. In this study, fresh banana peels are treated with 70 % ethanol ,further separated with chloroform ,water and ethyl acetate respectively .The supernatant of the enzymatic sample which is treated with chloroform is loaded into gel filtration column with Sephadex G-100 (1.0 x 90 cm) equilibrated with pH7 buffer media (phosphate buffer 0.1 M). Kinetic studies of the purified en

The 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

Three strain of Bacillus cereus were obtained from soil sours Laboratories of Biology Department/ College of Science/ University of Baghdad. The bacteria secreted extracellular xylanase in liquid cultur the test ability of xylanase production from these isolates was studied semi quantitative and quantitative screening appeared that Bacillus cereus X3 was the highest xylanase producer. The enzyme was partial purification 191 fold from cultur by reached step by 4 U/mg proteins by ammonium sulfat precipitation 80%, Ion exchang DEAE-cellulos chromatography Characterization study of the partial purifation enzyme revealed that the enzyme had a optimum activity pH8 and activity was stable in the pH rang (8-10) for 30min. maximal activity was attai

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.

The aim of the current study was to optimize different cultural and environmental conditions for production the antibacterial bioactive metabolites by Streptomyces rochei M78 isolated from agriculture soil, in Baghdad, Iraq. The effect of various parameters such as, culture media, incubation time, pH, carbon and nitrogen sources, C: N ratios and inducers on antibacterial metabolite production was studied by varying single parameter at a time. It was found from the results that higher metabolite production by isolate observed using starch casein broth (SCB) as the best production medium, at initial pH 7.0.Starch andcasein +yeast extract + peptone appeared to be the best carbon and nitrogen sources respectively and C: N ratio of 4: 1 after

The activity of peroxidase (POD) in cabbage was evaluated using
spectrophotometric method. The enzyme was extracted from the cabbage leaves
with 0.1 M phosphate buffer solution pH 7. 0 . POD activity was determined using
(O-dianisidine) as a substrate. The effects of the amounts of enzyme extract,
substrate concentration, pH and temperature were investigated. The highest activity
of POD was recored at 2 mg/ml. The highest activity of POD was optimized with
16 mM O-dianisidine, The optimum pH was 7.0 for POD , The optimum
temperature was 30°C for POD. These optimum conditions were used to
determined the enzyme activities in cabbage sample. Acetone fractionated
peroxidase from crude extract of Brassica oleracea

Ninety five samples were collected from different samples (urine, ear and wounds swaps), from hospitals in Baghdad city. The results of cultural, microscopic , biochemical tests indicated that in urine samples E.coli have high occurrence frequency 19 (47.5%) followed by Proteus mirabilis 18(45%) and Klebsiella species 1 (2.5%), while in wounds samples each of Pseudomonas spp. and Proteus mirabilis 10 (25%) , then followed by E.coli with 5 (12.5%) and Klebsiella species 3 (7.5%). Ear swaps samples revealed that Pseudomonas aeruginosa 7 (46%) was the major bacterium followed by Proteus mirabilis 4(26.6).Sensitivity test against eleven antimicrobial agents was done for all of the Proteus mirabilis isolates (32 isolates). The results display

Soil samples from fields cultivated with barley and wheat in addition to samples
from spoiled orange and apple fruits and carrot roots were collected with the aim to
isolate cellulase producing bacterial strains. Bacterial isolates obtained from these
samples were grown on a selective medium containing carboxymethyl cellulose
(CMC) as a sole source for carbon and energy. Results showed that nine isolates out
of fifty were able to produce cellulase.The specific activity of cellulase in culture
filtrate of the most efficient isolate was 1.601 u/mg protein.This isolate was
identified according to its morphological characteristics and biochemical tests, and
then by using Api 20-E and VITEK-II identification systems an