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

Lipase enzyme has attracted a lot of attention in recent years because of its diverse biotechnological applications. The present study was conducted to screen germinated seeds of four crops, namely sunflower (Helianthus annuus), flaxor linseed (Linum usitatissimum ), peanut (Arachis hypogaea  ) and castor bean (Ricinus communis), for the activity of their lipases. to the study also included the extraction and purification of lipase from the seeds of  the most promising crop using different solvents. The results indicated that the maximum enzymatic activity (0.669 U/ml) was  obtained when 0.1 M Tris-HCl buffer extract was used after 3 days of seed germination of all the tested species, as compared to the other test solvents

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

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

: Partial purification of phosphoenolpyruvate carboxykinase (PEPCK) from type 2 diabetic patients sera take place using some purification steps such as participation with ammonium sulphate (55-80%) and filtered through dialysis, then ion exchange chromatography by DEAE sepharose anion column, gel filtration chromatography by sephadex G-100 column. In ion exchange step, there are four peak are obtained, the highest enzyme activity obtained by (0.4 M Nacl) with purification fold (2.18), yield (44.3) of enzyme and specific activity (13.5) mg/ng, which obtained a single peak by gel filtration chromatography, the degree of purification (5.34) fold, yield of enzyme (20%) with specific activity (33.109mg/ng). The purified enzyme had an optimum tem

The study aimed to purification of acid phosphatase (ACP) from sera of obesetype 2 diabetes mellitus patients, this study included from thirty T2DM patients and thirty control, purification process was done with several steps included precipitation with inorganic salt (NH4 ) 2SO4 30%-80%, dialysis, ion exchange chromatography by DEAE sepharose anion column and size exclusion chromatography by Sepharose 6B.ACP, BMI, FBS, HbA1c, Lipid profile, Urea, Creatinie, Insuline, Homa-IR were determined. Results showed the precipitate and concentrated protein appeared four peaks in ion exchange column. ACP located in the first and second peak with purification fold (21.1), (37.2) yield of enzyme and specific activity (173.3) IU/ml, which obtained a si

From 211 urine samples, Gram negative bacteria were isolated from only 61 urine samples with isolation percentage 28.9%. Escherichia coli were isolated percentage 70.49% while Klebsiella pneumoniae and Psendomonas aeruginosa were 8.19% and 6.55%, respectively.Proteus spp. Were isolated from 9 (14.75%), P. mirablis and P. vulgaris were isolates percentage 11.47% and 3.27%, respectively. Uroepithelial Cell Adhesin (UCA) fimbriae expression by P.mirabilis isolates was detected by the high capacity to adhesion to human uroepithetial cells, the isolate p.mirabilis U7 was adhesion to human uroepithelial cells mean no.30.2 bacteria/cell when grown on luria broth at 37C for 24h, but then grown it’s on luria agar at 37C for 24h the adhesion

        Peroxidase is a class of oxidation-reduction reaction enzyme that is useful for accelerating many oxidative reactions that protect cells from the harmful effects of free radicals. Peroxidase is found in many common sources like plants, animals and microbes and have extensive uses in numerous industries such as industrial, medical and food processing. In this study, P. aeruginosa was harvested to utilize and study its peroxidases. P. aeruginosa was isolated from a burn patient, and the isolate was verified as P. aeruginosa using staining techniques, biochemical assay, morphological, and a sensitivity test. The gram stain and biochemical test result show rod pink gram-ne

This study includes adescription of Human serum Albumin by amodified using ion- exchange chromatography with manipulated comparison with cold ethanol precipitation method , It has been nticed that this procedure is superior orer the classical method . The Final yield by the new method 69.32% with purity of 83.42% compared with cohn which yield 60.30 % with purity of 80.7 % . The new method prored that it suitable for the pusi Fication of such material because it yield no precipitation material and it increases the Final yield of albumin solutions . • Human serum Albumin . • Albumin purification . • Ion – exchange chromatography . • Human plasma . • Albumin extraction .