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.

Twenty isolates of Serratia marcescens were isolated from inflammation of the urinary tract (UTI)., These isolates were found to produce hemolysin as indicated by blood agar plates in which the hemolysis of red blood cell indicate a positive result. Isolates were selected according to their hemolysis activity by measuring absorbance of hemoglobin at 405 nm that released from red blood cell. Hemolysin was completely purified using 50-75% saturation of ammonium sulphate followed by ion exchange chromatography with DEAE-cellulose then gel filtration chromatography by sepharose 4B. Accordingly molecular weight for the purified toxin was estimated as 45 KD.

This study aims to test ceramic waste's capacity to remove nickel from aqueous solutions through adsorption. Ceramic wastes were collected from the Refractories Manufacturing Plant in Ramadi. Through a series of lab tests, the reaction time (5, 10, 15, 20, 25, 30, 35, 40, 45, and 50 minutes, and Ni concentrations (20, 40, 60, and 80) were tested using ceramic wastes with a solid to liquid ratio of 2g/30ml. At a temperature of 30ºC, the pH, total dissolved solids (TDS), and electrical conductivity (EC) were all measured. The equilibrium time was set at 30 min. Thereafter, the sorption (%) somewhat increased positively with the Ni concentration. Freundlich's equation showed that the adsorption intensity is 1.1827 and the Freundlich c

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.

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

يهدف البحث الحالي إلى الاستفادة من القهوة المستهلكة , كمادة وسيطة حيث تعد القهوة المستهلكة من المخلفات المضرة للبيئة الاستخراج الكافيين الطبيعي والذي يعد مادة ذات نشاط حيوي واهمية, وتحديد العوامل الفعالة في كفاءة عملية الاستخلاص من حيث تركيز الكافيين. تضمنت المتغيرات الرئيسية المدروسة وقت الاستخلاص  0-150 دقيقة  ، ودرجة الحرارة  25-55 درجة مئوية  ، وسرعة الخلط  180-450 دورة في الدقيقة  ،   ودرجة الحموضة العالق

The presence and prevalence of V. cholerae were investigated in forty five water samples collected from different locations of Tiger River/ Baghdad city. Twenty one isolates were isolated by adopting a simple isolation techniques. The final identification revealed that only three isolates were confirmed as V. cholerae. They were named 1J, 1R and Dial 131 which are all serogrouped as non-O1. Toxin Coregulated Pili (TCP) and heat labile enterotoxin (LT) were determined in only the environmental isolate 1J while non of the isolates produced heat stabile toxin (ST). The purification scheme was improved, few steps were adopted to include back extraction of ammonium sulfate, saturation between 80-20%, desalting through Sephadex G25, and gel filt

Proteinases (E.C.3.4.21) family are widely distributed in the nature; it was present in animals tissues , plants and microbial cell . Protease was purified from Zahdi seed (Phoenix dactylifera L.) by several steps included ammonium sulphite ppt (75%) saturation and dialyzed against the 80mM sodium phosphate buffer at pH 7.5 . The enzyme specific activity was 407.62 unit/mg protein. The obtained extract was purified by DEAE-Cellulose column followed by gel filtration through Sephacyl S-200 column .The enzyme specific activity ,yield and purification fold were 1873.49 unit/mg protein, 22.99 and 58.42% respectively. The results of protease characterization showed that the molecular weight was 25118 daltons as determined by gel f