Myrosinase from roots of Raphanus sativus
| Autor: | Nadia M. Abdallah, Mona M. Rashad, Sanaa T. El-Sayed, Etidal W. Jwanny, Abeer E. Mahmoud |
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| Rok vydání: | 1995 |
| Předmět: |
chemistry.chemical_classification
Chromatography biology Myrosinase Raphanus Substrate (chemistry) Plant Science General Medicine Horticulture biology.organism_classification Biochemistry chemistry.chemical_compound Enzyme chemistry Sinigrin Sephadex Yield (chemistry) Denaturation (biochemistry) Molecular Biology |
| Zdroj: | Phytochemistry. 39:1301-1303 |
| ISSN: | 0031-9422 |
| DOI: | 10.1016/0031-9422(95)00099-s |
| Popis: | Two myrosinase isoenzymes ( EC 3. 2. 3. 1 ) were extracted and purified by (NH 4 ) 2 SO 4 precipitation and DEAE-cellulose and Sephadex G-200 chromatography from radish root tissues with M r s 28 800 and 58 900. The most active one (120 U mg −1 ) was identified and characterized. The yield of the purified myrosinases was 21 mg (2398 U) of pure enzymes from 100 g of dry root tissues. The purity was ascertained by obtaining a single sharp band by disc electrophoresis. Optimal myrosinase activity on sinigrin was recorded in phosphate buffer, pH 6 – 6.5 at 37°. The K m for myrosinase with sinigrin as substrate was 0.47 mM at pH 6. The enzyme was stable for 45 min at 30 and 40° (18% denaturation). |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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