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| Content Provider | PubMed Central |
|---|---|
| Author | Hermes, H. F. M. Tandler, R. F. Sonke, T. Dijkhuizen, L. Meijer, E. M. |
| Abstract | An l-amino amidase from Mycobacterium neoaurum ATCC 25795 responsible for the enantioselective resolution of dl-α-methyl valine amide was purified and characterized. The purification procedure included ammonium sulfate fractionation, gel filtration, and anion-exchange chromatography, which resulted in a homogeneous preparation of the enzyme with a native molecular mass of 136 kDa and a subunit molecular mass of 40 kDa. The purified enzyme displayed the highest activity at 50°C and at pH 8.0 and 9.5. The enzyme was strongly inhibited by the metal-chelating agent 1,10-phenanthroline, the disulfide-reducing agent dithiothreitol, and the cysteine proteinase inhibitor iodoacetamide. The purified amino amidase showed a unique l-enantioselective activity towards a broad range of both α-H- and α-alkyl-substituted amino acid amides, with the highest activity towards the cyclic amino acid amide dl-proline amide. No activity was measured with dl-mandelic acid amide nor with the dipeptide l-phenylalanine-l-leucine. The highest catalytic efficiency (k cat/K m ratio) was measured with dl-α-allyl alanine amide, dl-α-methyl phenylalanine amide, and dl-α-methyl leucine amide. |
| Starting Page | 153 |
| File Format | |
| ISSN | 10985336 |
| e-ISSN | 10985336 |
| Journal | Applied and Environmental Microbiology |
| Issue Number | 1 |
| Volume Number | 60 |
| Language | English |
| Publisher Date | 1994-01-01 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Ecology Food Science Applied Microbiology and Biotechnology Biotechnology |
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