Acceleration of hyaluronidase production in the course of batch cultivation of Clostridium perfringens can be achieved with bacteriolytic enzymes.
As Clostridium perfringens hyaluronidase has cell-bound enzyme features, an enzymatic approach has been designed to facilitate the release of hyaluronidase into culture through increasing the clostridial cell wall permeability. As a result of the application of lytic peptidase from Actinomyces rutgersensis, beta-N-acetylglucosaminidase and beta-N-acetylmuramidase (both from Bacillus subtilis) commercially available preparations at the end of the producer's exponential growth phase, a 5.3-, 4.8- and 4.0-fold acceleration, respectively (but no enhancement), of hyaluronidase production in the course of batch cultivation of Cl. perfringens has been achieved. This also resulted in an approximately 10-fold reduction in undesirable side lecithinase activity irrespective of the bacteriolytic enzyme preparation used.
Zukaite
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Immunobiotechnology Sector, Institute of Immunology, Vilnius, Lithuania.
Biziulevicius
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GA
D000118:Acetylglucosaminidase / Q000494:pharmacology; D000190:Actinomyces / Q000201:enzymology; D001412:Bacillus subtilis / Q000201:enzymology; D002473:Cell Wall / Q000187:drug effects; D003016:Clostridium perfringens / Q000201:enzymology* / Q000254:growth & development; D006026:Glycoside Hydrolases / Q000494:pharmacology; D006821:Hyaluronoglucosaminidase / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000494:pharmacology*; D010539:Permeability; D010740:Phospholipases / Q000032:analysis / Q000378:metabolism; D013997:Time Factors
D010740:Phospholipases; D006026:Glycoside Hydrolases; C026255:endo-N-acetylmuramidase; D006821:Hyaluronoglucosaminidase; D000118:Acetylglucosaminidase; D010447:Peptide Hydrolases