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Urate oxidase (uricase) was isolated and purified from Pseudomonas aeruginosa to apparent homogeneity using ammonium sulphate precipitation followed by ion exchange and gel filtration chromatography. The specific activity of the purified uricase enzyme was found to be 636.36 with the use of uric acid as a substrate. The purified uricase enzyme is a monomeric protein with molecular weight of 64 kilodaltons...
An intracellular glutathione transferase was purified to homogenity from the fungus, Mucor mucedo, using DEAE-cellulose ion-exchange and glutathione affinity chromatography. Gel filtration chromatography and SDS-PAGE revealed that the purified GST is a homodimer with approximate native and subunit molecular mass of 53 kDa and 23.4 kDa, respectively. The enzyme has a pI value of 4.8, a pH optimum at...
Two different extracellular lipases were isolated and purified from Pseudomonas aeruginosa Ps-x to apparent homogeneity using ammonium sulfate precipitation followed by ion exchange chromatography on Q- and S-Sepharose column. Both of the purified lipases are monomeric protein with molecular weight of 15.5 and 54.97 KDa respectively. The optimal activities of the enzymes were at 45 and 50°C and pHs...
Cytolytic toxins produced by Aeromonas hydrophila and Aeromonas veronii biotype sobria strains were partially purified from culture filtrates by two steps of purification: ammonium sulfate precipitation and hydrophobic chromatography using Phenyl-Sepharose CL-4B. Hemolytic activity was detected in one or two peaks in elution profile. Purified toxins were also cytotoxic to Vero and CHO cells. Moreover,...
A marine Bacillus strain was isolated from the eastern harbour of Alexandria and identified as Bacillus sp. MIG. Maximum activity of studied proteases was obtained when the bacterium was grown in medium with 1 % wheat bran and 0.5% yeast extract in addition to the mineral salts and incubated for 48 h at 30°C and 120 rpm. Two alkaline proteases (Pro 1 and Pro 2) were purified to homogeneity using cation...
A β-mannosidase was purified from Phlebia radiata grown in a medium containing wheat bran or galactomannan as a carbon source. Maximal activity was observed at pH 5.5 and at 50°C. Highly purified isoforms of β-mannosidase (GM-1, GM-2) isolated from media containing galactomanan and (OT-1) media with wheat bran were obtained by means of column chromatography on Q-Sepharose, SP-Sepharose and chromatofocusing...
Production and purification of α-amylase by probiotic Lactobacillus plantarum MTCC 1407 has been investigated under submerged fennentation using Mann Rogassa Sharpe medium containing (1%) soluble starch in lieu of glucose (2%) as carbon source. Response Surface Methodology was used to evaluate the effect of main variables, i.e. incubation period, pH and temperature on enzyme production. A full factorial...
In this paper production of a cold-active esterase EstA from the Antarctic bacterium Pseudoalteromonas sp. 643A in E. coli expression system was described. The purification and biochemical characteristic of EstA were performed in the presence of urea and then compared with results obtained for the esterase with no addition of urea and isolated from the native source. In both cases the cold-active...
α-1,3-Glucanases (mutanases) are currently of great interest due to their potential use in the field of dental care. These enzymes have been reported in several bacteria, yeasts and fungi, but up to now, characterization of this family of proteins has been relatively poor. In this study, we identify and characterize a mutanase gene from Trichoderma harzianum CCM F-340. Sequence analysis, on the nucleotide...
Apurinic/apyrimidinic (AP) sites in DNA are considered to be highly mutagenic and must be corrected to preserve genetic integrity, especially at high temperatures. The gene encoding a homologue of AP exonuclease was cloned from the thermophilic anaerobic bacterium Thermoanaerobacter tengcongensis and transformed into Escherichia coli. The protein product showed high identity (80%) to human Ape1 nuclease,...
An intracellular aminopeptidase N synthesized by Pseudomonas putida Lup was purified and characterized. The approx. 150-fold purified enzyme showed highest activity against A-β-naphthylamide at pH 7.5 and at temperature 40°C and was 100% thermostable for 240 min at 40°C. P. putida lup aminopeptidase N is a monomer with molecular mass approx. 99 kDa determined by SDS-PAGE and gel permeation chromatography...
Bacteriocin E50-52, a class IIa bacteriocin with a wide antibacterial spectrum, and has a huge potential to be a substitute for conventional antibiotics. In this research, the bacteriocin E50-52 gene was cloned into the expression vector pET SUMO (small ubiquitin-related modifier) and introduced into Escherichia coli BL21 (DE3). The recombinant fusion protein SUMO-bacteriocin E50-52 expressed in a...
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