Abstract
Amino acid-analogue-resistant mutants of the cyanobacterium Spirulina platensis were isolated using amino acid analogues β-2-thienylalanine, p-fluorophenylalanine, ethionine and azetidine-2-carboxylic acid. The growth and other cellular contents in these mutants were less than in the parent. The internal free amino acid pool showed varying amounts. Maximal overproduction occurred of proline whereas overproduction of aspartic acid, alanine and lysine was much less.
References
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Geeta, G., Singh, P. Isolation and characterization of amino acid-analogue-resistant mutants of Spirulina platensis. World Journal of Microbiology and Biotechnology 16, 397–399 (2000). https://doi.org/10.1023/A:1008973016441
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DOI: https://doi.org/10.1023/A:1008973016441