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

Imidacloprid is systemic insecticide (1-[(6-chloro-3-pyridinyl) methyl]-N-nitro-2-imidazolidinimine) and the world’s most widely used has significant efficacy against a broad variety of pests and a unique mode of action by using it spreader and irrigation. The persistence of this pesticide in the soil means that it causes environmental damage that must be cleaned up. In this study collected and identified the best bacteria isolate that breakdown imidacloprid from the Plant Protection Director in Baghdad, which has been using neonicotinoid pesticides for years in their own greenhouse for pest control. Using high-performance liquid chromatography HPLC to measuring the residual concentrations of imidacloprid in MSM media at a concentration o

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 .<

Background: 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

Biological activity of the carotenoids which are produced fromchemically-mutaed local isolate of Rhodotorula mucilaginosawas studied. The results showed variation of inhibition activity of caritenoids against different types of pathogenic bacteria include, Staph aureus, E. coli, B. subtilis and Salmo. typh., the number declined from 2×107cell/ml to 2×104, 5×104, 2×105, 9×105 cell/ml respectively after 24hour. The produced carotenoids from alocal mutant Rhodotorula mucilaginosa revealed an antioxidant activity as free radical removal of 85.6%. Carotinoides revealed a highest stability in petroleum ether solvent for 30 days at room temperature. It found that the pigment was more stability in sesame oil compared with sun flower and coc

    Lipase was extracted by Sodium acetate buffer (pH=6; 0.05M) Containing 0.1M NaCl. Enzyme content of crude extract was concentrated by gradual addition of ammonium sulfate at 30-60% saturation. The dialyzed extract was purified on ion-exchange chromatography through DEAE–Cellulose and gel-filtration chromatography through sephacryl S-200 column. The specific activity, enzyme yield and fold purification were 54.06 unit/mg, 42.6% and 10.88 respectively. The molecular weight of the Lipase was 43.651 KDa as determined by gel-filtration chromatography through sephacryl S-200 column. Partial purified lipase used for the improvement of the flavor of butter fat after 12 hours for storage.