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PURIFICATION AND PROPERTIES OF ASPARTYL PROTEINASE FROM CANDIDA ALBICANS | ||
| IRAQI JOURNAL OF MEDICAL SCIENCES | ||
| Article 1, Volume 5, Issue 1, 2007, Pages 22-28 | ||
| Authors | ||
| Resol Al-Dabbagh; Essam F. AI-Jumaily; Azhar A. lbrahim | ||
| Abstract | ||
| Background: Aspartly proteinase, EC.3.4.23 isolated from leukemic patients with candidermia. Objective: Purification and properties of proteinase from Candida albicans. Methods: The enzyme was purified from Candida albicans by Ion exchange chromatography and gel filtration Sephacryl S-200 column. Results: Different strains of C.albicans isolated from leukemic patients with candidemia were used for production of proteinase enzyme. Wheat bran incorporated in Sabouraud s broth to increase production of proteinase by the organism. The specific activity of purified enzyme was 400 unit/mg, fold of 19.68, and a yield of 8.48 % .The molecular weight of enzyme is 57676 daltons when estimated by using Sephacryl S-200. Stability of proteinase enzyme and its activity at different pH and temperature were studied in details. Conclusion: Consecutive elevation of the enzymes specific activity values with the respective steps of purification. A more virulent strains the more reproducible of proteinase enzyme Keywords: Aspartyl proteinase ; C. albicans'. Purification; Sephacryl S-200. | ||
| Keywords | ||
| Aspartyl proteinase; albicans; Purification; Sephacryl S | ||
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