The enzyme collagenase occurs rarely among the fungi and bacteria. In reviewing the subject, Mandi (1) in 1961 concluded that only the clostridial (Clostridium perfrin pens and C. his tolyticum) enzyme was an authentic collagenase. The criteria she proposed for distinguishing an enzyme as a specific collagcnase were the reduction in viscosity of undenatured collagen and the concomitant release of dialyzable hydroxyproline-containing units at physiologic pH. Previous work by the senior author

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... has described enzymes elaborated by an aetinomycete, (Streptomyces madurae) and a fungus, (Trichophyton schoenleinii) which fulfilled these criteria for collagenasc. Schoellman (3) has recently described a collagenase from strains of Pseudomono.s aeruginosa. This report is concerned with the possible significance of the enzyme to the pathogenic potential of the aetinomycete Streptomyces madurae, an etiologic agent of human mycetoma or maduramycosis. MATERIALS AND METHODS Organism. S. madurae isolated from a case of mycetoma was maintained on trypticase soy agar (TSA) as stock culture. Organisms for animal inoculation and exposure to mutagen were grown in tryptiease SOY broth with 0.2% Tween 80 (TSBT) for two weeks at 25° C. The Tween was required to obtain single cells. Collagenase assay. Preparation of substrate, and the assays for viscosity and hydroxyproline were previously described (2). A modification of the ninhydrin method of Mandl (1) was used for preliminary testing. To 10 mg collagen (Worthington) were added 5 ml 0.067 M phosphate buffer (pH