| Autor: |
Brearley, G., Price, C., Atkinson, T., Hammond, P. |
| Zdroj: |
Applied Microbiology & Biotechnology; 1994, Vol. 41 Issue 6, p670-676, 7p |
| Abstrakt: |
The L-amino acid oxidase (L-aao) from Bacillus carotarum 2Pfa was purified to homogeneity, as judged by polyacrylamide gel electrophoresis, from crude sonicated cell extract by a combination of anion exchange chromatography and gel filtration. The purified enzyme was a dimer with a native relative molecular mass of approximately 102,000 to 115,000 and comprised two identical subunits of 54,000. The isoelectric point of the L-aao was at pH 4.8 the ph optimum was at 8.0-8.5 and the temperature optimum was at approximately 50° C. It was stable for several months at + 4° C and at −20° C. The enzyme contained 2 mol flavin adenine dinucleotide (FAD)/mol enzyme and exhibited relatively broad range substrate specificity, oxidising a total of ten L-amino acids and , albeit to a much lesser extent, seven D-amino acids. Kinetic studies revealed that the three aromatic L-amino acids were the preferred substrates. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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