PURIFICATION AND CHARACTERIZATION OF PROTEASE FROM Pseudomonas aeruginosa ISOLATED FROM SOME WOUND AND BURN INFECTION.
|Journal of University of Anbar for Pure Science|
|Article 12, Volume 3, Issue 3, December 2009, Pages 37-44 PDF (613.73 K)|
|Document Type: Research Paper|
|SAMEER F. SAMAAN* 1; SOUOD R. ALANI2; RANA M. AL-SHWAIKH* 3|
|1Al-Mustansiriya University - College of Science|
|2The Ministry of Science and Technology|
|3University of Baghdad - College of Education Ibn Al-Haytham|
|Twenty Four isolates of Pseudomonas aeruginosa were identified. The isolates were|
8(33%) from wound infections, 16(66%) isolates from burn infections. The sensitivity of Pseudomonas
aeruginosa isolates was been tested against (10) antibiotics showed isolates version resistance with
different percentage against antibiotics. Pseudomonas aeruginosa exhibited (100%) resistance to
Ampicillin. While percentages of resistance to Cefixime and Ceftazidime were (95.8%) and (79%)
respectively. Resistance percentages to Tobramycin, Piperacillin, Norfloxacillin, Ciprofloxacin were
(41.6%), (20.8%), (20.8%) and (4%) respectively. All isolates of Pseudomonas aeruginosa were highly
sensitive (100%) to Aztronam, Imipenem, Cefepime. The optimum conditions for protease production
were in LB medium with a pH (8) after (48) hrs of incubation at (35) Cº. Purification of the protease
was done using ion exchange chromatography DEAE-cellulose and gel filtration with sephadex G-100.
Molecular weight of the purified protease was measured by sephadex G-100 and it was found to be
around (21379) Dalton. The optimum temperature of enzyme activity was (35) Cº. However, the pH (8)
was for activity and stability of this enzyme. Zn++ and Ca++ ions may play a role in the enhancement
and stability of the enzyme. Enzyme activity was not inhibited in the presence of reducing agent such
as Cysteine, but it was inhibited in the presence of EDTA
|Pseudomonas aeruginosa; Protease|
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