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°

Prodigiosin is a ‘natural red pigment produced by Serratia marcescens which exhibits immunosuppressive and anticancer properties in addition to antimicrobial activities. This work presents an attempt to maximize the production of prodigiosin by two different strategies: one factor at time (OFAT) and statistical optimization. The result of OFAT revealed that sucrose and peptone were the best carbon and nitrogen sources for pigment production with concentration of prodigiosin of about 135 mg/ L. This value was increased to 331.6mg/ L with an optimized ratio of C/N (60:40) and reached 356.8 with pH 6 and 2% inoculum size at end of classical optimization. Statistical experimental design based on Response surface methodology was co

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.

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

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.

Forty one isolates of genus Proteus were collected from 140 clinical specimens such as urine, stool, wound, burn, and ear swabs from patients of both sex. These isolates were identified to three Proteus spp. P. mirabilis, P. vulgaris and P. penneri .The ability of these bacteria to produce L-asparaginase II by using semi quantitative and quantitative methods was determined. P. vulgaris Pv.U.92 was distinguished for high level of L-asparaginase II production with specific activity 1.97 U/mg. Optimum conditions for enzyme production were determined; D medium with 0.3% of L-asparagine at pH 7.5 with temperature degree 35°C for incubation. Ultrasonication was used to destroy the P. vulgaris Pv.U.92 cells then ASNase II was extracted and pu

The bacteria Azotobacter Vinelandii  was taken from a central research in Baghdad, The purification of alginic acid which produced from the bacteria by several steps starting with precipitation with isopropanol (3:1) v/v , Washing by ppt with 100ml of isopropanol       : distilled water (3:1) v/v , then the ppt was dissolved in warm distilled water and dialysis against distilled water from 24 h/s . To Complete the purification , gel filtration chromatography was conducted on sephacryl s-100 column followed by ion – exchange chromatography . Using DEAE cellulose column . The molecular Weight of purified al ginic acid was higher than that of blue dextran 2000,It was more than (2) millions Dalton .<

     Keratin is a fibrous, insoluble structural protein that is highly cross-linked with hydrophobic, hydrogen, and disulfide bonds. Keratinases are enzymes that belong to the category of serine hydrolases that are capable of breaking down keratin. The results of the determination of the better fermentation system showed that the production of keratinase from local A.terreus A13 isolate by submerged fermentation (SmF) system was the best system to give the highest specific activity (113.4 U/mg) of keratinase compared with solid-state fermentation (SSF). The optimum conditions for keratinase production by SmF, were determined via cultivation conditions, including carbon source, nitrogen source, temperature, pH of the medium,