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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Jaouadi, Bassem Zaraî Jaouadi, Nadia Rekik, Hatem Naili, Belgacem Beji, Abdelhamid Dhouib, Abdelhafidh Bejar, Samir |
| Description | Country affiliation: Tunisia Author Affiliation: Jaouadi B ( Laboratory of Microorganisms and Biomolecules, Centre of Biotechnology of Sfax, University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, Sfax 3018, Tunisia. bassem.jaouadi@yahoo.fr) |
| Abstract | An extracellular alkaline elastase was produced from Pseudomonas aeruginosa CTM50182. It was chromatographically purified using HPLC and Mono Q Sepharose column. Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that the purified enzyme (called AMPP) was a monomer with a molecular mass of 33,015.18 Da. The N-terminal 29 amino acid sequence of AMPP showed high homology with those of Pseudomonas elastases. It showed optimal activity at pH 12 and 80 °C and was stable at a pH range of 9-12 after 120 h of incubation. Its thermoactivity and thermostability were upgraded in the presence of 5 mM Co(2+). Its half-life times at 70 and 80 °C were 16 and 10 h, respectively. It was completely inhibited by ethylene glycol-bis (ß-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA), and 1,10-phenanthroline, suggesting that it belongs to the metalloprotease family. AMPP also exhibited high catalytic efficiency, organic solvent-tolerance, and hydrolysis. The lasB gene encoding AMPP was cloned, sequenced, and expressed in Escherichia coli. The biochemical properties of the extracellular purified recombinant enzyme (rAMPP) were similar to those of native AMPP. This organic solvent-stable protease could be considered a potential candidate for application as a biocatalyst in the synthesis of enzymatic peptides. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 60 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2013-09-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Pancreatic Elastase Chemistry Metabolism Pseudomonas Aeruginosa Enzymology Solvents Amino Acid Sequence Base Sequence Cloning, Molecular Enzyme Activation Enzyme Stability Gene Expression Hydrogen-ion Concentration Hydrolysis Ions Kinetics Metals Molecular Sequence Data Antagonists & Inhibitors Genetics Isolation & Purification Phylogeny Proteolysis Classification Rna, Ribosomal, 16s Sequence Alignment Substrate Specificity Temperature Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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