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Isolation and complementation of mutants of Streptomyces coelicolor "Mueller" DSM3030 deficient in lysozyme production
Streptomyces coelicolor "Mueller" excretes the lysozyme N-acetylmuramidase. Culture filtrates of this strain form a characteristic halo on agar plates containing freeze-dried Micrococcus luteus cells (lysoplate technique). The halo consists of a clear inner zone and a turbid outer ring. Si...
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Published in: | Applied microbiology and biotechnology 1989-01, Vol.30 (4), p.358-363 |
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Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Online Access: | Get full text |
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Summary: | Streptomyces coelicolor "Mueller" excretes the lysozyme N-acetylmuramidase. Culture filtrates of this strain form a characteristic halo on agar plates containing freeze-dried Micrococcus luteus cells (lysoplate technique). The halo consists of a clear inner zone and a turbid outer ring. Simulation experiments showed that the turbid outer ring is probably produced by lysozyme whereas the clear inner zone may be due to an additional protease action. Using the lysoplate technique UV- and NTG-mutagenized strains of S. coelicolor "Mueller" were screened for mutants defective in lysozyme production. Two mutants, SC11 and SC12, were identified. The mutant SC11 was selected for complementation studies. First, a transformation system was established. The use of a soft-agar overlay method was necessary to yield high regeneration rates of SC11 protoplasts. |
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ISSN: | 0175-7598 |