REGULATION OF PROTEINASE FORMATION IN A SPECIES OF MICROCOCCUS

Abstract
Micrococcus sp. ATCC No. 407 (M. freudenreichii) produced relatively large amounts of extracellular proteinase in synthetic medium containing methionine, thiamine, biotin, NH4Cl, NaHCO3, NaCl, MgSO4, and FeSO4, with aspartic acid, asparagine, glutamic acid, or glutamine as the carbon source. The organism produced relatively small amounts of proteinase with succinate, malate, fumarate, maltose, maltotriose, or maltotetraose as the carbon source. In synthetic medium containing maltose, any one of several amino acids stimulated growth and proteinase production. The results indicated that the organism is a partial constitutive strain with respect to proteinase production and suggested that proteinase formation is controlled by a form of end-product induction. In the presence of inducer, carbon sources such as succinate or maltose caused suppression of proteinase formation, suggesting control by metabolic repression as well. Because extracellular proteinase formation is induced by amino acids and suppressed by carbon sources such as succinate or maltose, and because the organism can utilize amino acids as carbon sources for growth, it. is suggested that the function of extracellular proteinase in this organism is to ensure a supply of carbon for growth rather than a supply of amino acids for protein synthesis.