Strain CIP 82.01 of and strain I.029 (previously designated “”) were compared. Strain I.029 produces a collagenase of high specific activity ( collagenase; EC Collagenase production is induced in strain CIP 82.01 by collagen or macromolecular fragments of collagen in a manner similar to collagenase induction in strain I.029; caseinolytic proteinase is constitutive. In this study we demonstrate that both strains also produce a constitutive extracellular endonuclease. Collagenases from both strains cleave either native collagen in its helical region or a similar synthetic peptide; both enzymes are inhibited by ethylenediamine tetraacetate, but not by diisopropyl fluorophosphate. The collagenase subunit (molecular weight, 35,000) of strain CIP 82.01 is similar in amino acid composition to the subunit of the strain I.029 enzyme, although some of the aspartic and threonine residues in strain CIP 82.01 are replaced by glutamic and serine residues in strain I.029. Surface radioiodination followed by two-dimensional electrophoresis showed that there are quantitative differences in the major outer membrane proteins of the two strains. Strains CIP 82.01 and I.029 differ qualitatively in resistance to ampicillin and carbenicillin, in cellobiose fermentation, in ornithine decarboxylase activity, and in halophilism. We propose that strain I.029, which was originally designated , be included within the species , but that this organism be distinguished from other strains of this species by the designation chemovar , with the corresponding collagenase designated “iophagus collagenase” (EC


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