Streptomycetes excreting dd-carboxypeptidases |
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Authors: | W Kurzątkowski J Solecka J Filipek J D Kurzątkowski W Kuryłowicz |
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Institution: | (1) State Institute of Hygiene, Chocimska 24, 00-791 Warsaw, Poland;(2) Pharmaceutical Faculty, Medical Academy of Warsaw, Banacha 1, 02-097 Warsaw, Poland |
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Abstract: | Summary Excretion of exocellular dd-carboxypeptidases was tested using 128 strains of streptomycetes. Exocellular enzyme activity was shown in 13% of the trains investigated. Streptomyces strains showed low activity of excretion of dd-carboxypeptidases: 2.7–4.8 M of released C-terminal d-alanine (d-Ala) residue/1 culture supernatant per minute. Saccharopolyspora erythraea mutants produced considerably higher levels of exocellular enzymes, the dynamics of excretion depending upon the medium used. The highest activity of exocellular dd-carboxypeptidase production was 44 M d-Ala/1 culture supernatant per minute. The affinity of exocellular dd-carboxypeptidase of S. erythraea 64-575 for -lactam antibiotics was assessed by a statistical computer programme. The enzyme showed the lowest affinity for sodium cefotaxime, ID50(M) = 7.5 × 10–6, and the highest for potassium cephalosporin C, ID50(M) = 5.0 × 10–9, ID50(M) representing the molar concentration of -lactan antibiotics which decreased by 50% the release of d-Ala.
Offprint requests to: W. Kurzatkowski |
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