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

In this study, detection of uricase production from Pseudomonas aeruginosa
isolates was done by applying colorimetric method, Uricase was purified from the
most potent isolate by precipitation using ammonium sulphate (80% saturation) then
purification was achieved using DEAE –Cellulose ion exchange and Sepharose 6B
gel filtration chromatography column, 16.4% of total enzyme was recovered with
specific activity 2337.5U/mg and 22.21folds of purification. Characterization of
uricase involved detection of optimal conditions for uricase activity, the maximal
activity was obtained at temperature 45ºC,while uricase appeared to be stable at
40ºC. Uricase showed optimal activity at pH 9 while pH stability was in the

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.

This study was conducted to isolate and identify killer yeast Hanseniaspora uvarum from dates vinegar and measurement the ability of this yeast to produce killer toxin. The antimicrobial activity of the concentrated supernatant containing partially purified concentrated killer toxin was also detected against several pathogenic bacteria and yeast species, which includes two types of yeast Rhodotorula mucilaginosa and Candida tropicalis and four human pathogenic bacteria Staphylococcus aureus, Escherichia coli, Klebsiella pneumoniae and Pseudomonas aeurginosa. In addition, the antagonistic activity of examined yeast have been studied toward four types of fungi, where two are pathogenic

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

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

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