Isovaleryl CoA dehydrogenase (IVDH) is a flavoprotein that introduce a trans-double bond between C2 and C3 of the isovaleryl CoA substrate, an intermediate in leucine catabolism pathway. Interrogation of the Paracoccus denitrificans Pd1222 genome has identified Pden_3633 gene as a candidate to encode for IVDH. In previous study by Rafid et al (under the publishing), this putative IVDH was expressed in E. coli and purified as N-terminal Strep-tagged protein. In current study, spectral properties of the purified IVDH were conducted and the results showed that the enzyme was obtained as an apoprotein. For this reason, IVDH has been reconstituted by incubation with flavin adenine dinucleotide (FAD) and the experiment showed that the ratio 1:

Fifteen local isolates of Pseudomonas were obtained from several sources such as soil, water and some high-fat foods (Meat, olives, coconuts, etc.). The ability of isolates to produce lipase was measured by the size of clear zone on Tween 20 solid medium and by measuring the enzymatic activity and specific activity. Isolate M3 (as named in this study) was found to be the most efficient for the production of the lipase with enzymatic activity reached 56.6 U/ml and specific activity of 305.94 U/mg. This isolate was identified through genetic analysis of the 16S rRNA gene. and it was shown that the isolate M3 belongs to Pseudomonas aeruginosa with 99% similarity. The DNA of isolate M3 was extracted and lipase gene was amplified through PCR tec

A  local  isolate  Bacillus  subtilis     was used,  which  producing

thennophilic  complex  enzyme having similar  activity  of  endogluganase

enzyme ( Endo-l,4-B-Dglucanase ).

Partially digested  chromosomal  DNA of  Bacillus subtilis by Eco

Rl  restriction  enzyme  randomly cloned  into  Eco Rl  pSU10l   shuttle vector. The  resulted  hybrid  plasmid was  transformed  into  protoplast of

Streptomyces sp.      SH-H.

The  result   revealed &nbsp

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 .

Lipoxygenase was extracted from the cup of Pleurotus ostreatus ( Jaq : Fr ) oyster mushroom for the first time in Iraq, and purified homogeneously through precipitation with 40% saturation of (NH4)2SO4 as a partial purification then loaded on DEAE-Cellulose (Diethyl amino ethyl Cellulose) ion-exchange chromatography column and then the highly active elution parts have been passed through gel filtration column with Sephacryl S-300 as a final purification with 804 (U/mg protein) specific activity, 11.32 fold of purification and 36.54% yield . The molecular weight of the enzyme was estimated to 74 KDa by gel filtration Sephacryl S-300 column and the isoelectric point for enzyme was 5.3. The optimal pH for lipoxygenase activity and stability

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

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