| Autor: |
J R, Ramsay, I D, McEntee, P M, Hammond |
| Rok vydání: |
1992 |
| Předmět: |
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| Zdroj: |
Bioseparation. 2(6) |
| ISSN: |
0923-179X |
| Popis: |
Salicylate monooxygenase (EC: 1.14.13.1) has been produced and purified from Pseudomonas cepacia ATCC 29351 which has the ability to utilise salicylate as a sole carbon source. The bacterium was grown on a defined medium containing 2% (w/v) casamino acids and 0.15% (w/v) yeast extract at 25 degrees C; salicylate monooxygenase production was induced by the presence of up to 0.7% (w/v) sodium salicylate, to a level of approximately 2% of the soluble cell protein. The enzyme was purified over 50-fold, with a recovery of about 40%, by a combination of ion exchange and hydrophobic interaction chromatography. The purified enzyme had a specific activity of 14-15 U mg-1 protein and was essentially homogeneous. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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