Abstract
AbstractDifferent bacterial strains were investigated for their benzylpenicillin destroying activity. The possible degrading products, benzylpenicilloic acid (BPA), 6‐aminopenicillanic acid (6‐APA) or penicic acid (PA) were screened by thin layer chromatography, using a new solvent system. Near all the strains tested, produce at different levels a β‐lactamase as observed from the BPA production. Acylase was not produced by the strains investigated. Neither 6‐APA nor PA were found, although small amounts of these products could not be detected by this qualitative method. BPA production from benzylpenicillin was measured quantitatively as a function of the enzymatic activity of the β‐lactamase.These experiments were carried out on the washed bacterial cells, the cell‐free growth medium and the cells treated with toluene. Most of the β‐lactamase activity was produced extracellularly by the bacteria; lower levels were found in the washed cell suspensions.
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