The mucilage was isolated from mustard seeds and identification by some different methods like, thermo gravimetric, FTlR., X-ray powdered, proton NMR, FTIR spectra of the three gums contain different functional group in the gums, major peaks  bands noticed were belong to OH (3410.15 – 3010.88) group from hydroxyl group, CH aliphatic (2925-2343.51), C-O (1072.42-1060.85) group and C=O 1743.65, Thermo chemical parameters of mucilage was evaluated  and compared with the standard gums, Results indicated the mucilage was decomposed in 392°C and mass loss 55%, The X ray process found the mucilage had single not sharp peak

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 .

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

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

In this study, measuring effectiveness Alauriz in some seeds powder and found that the seeds of-sophistication sex had the highest effective enzymatic reach 353 units / gProtein and Alkabbatah study enzyme extract under different storage conditions and Altaj showed that the enzyme loses Thbatih and whether Mrkbhetwan adding Alklasrin concentration of 10% for the systematic solution

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

Indole acetic acid (IAA) produced from F. oxysporum (F2) was purified by several steps included extraction by cold ethyl acetate ; Column chromatography using silica gel and TLC chromatography . The pure indole acetic acid (IAA) which produce by F. oxysporum (IAA) was tested by ultraviolet spectra at (200-300)nm ; and appear that the maximum absorbance at 229nm , the high performance liquid chromatography (HPLC) used to test the purity of the indole acetic acid and the results showed one peak at appearance time 3.822 min

        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

Introduction: Melanin is a high-molecular weight pigment produced through the oxidative polymerization of phenolic or indolic compounds and plays a perfect role in UV-light shielding, as well as in photoprotection. Among biopolymers, melanin is unique in many aspects. This study is designed to screen Production, extraction and characterizes of an extracellular melanin pigment from clinically isolated P. aeruginosa. Objective: The aim of the current study is isolation and diagnosis of P.aeruginosa using vitek-2 compact system and screening the ability to produce melanin and characterization of extracted melanin by UV-vis, FTIR, XRD and SEM. Materials and methods: the samples swab inoculated on cetrimide agar as selective media and incubated