CHARACTERISTICS OF AN EXTRACELLULAR PROTEINASE FROM MICROCOCCUS FREUDENREICHII

Abstract
An extracellular proteinase from Micrococcus freudenreichii is described. The enzyme hydrolyzes casein and crystalline β-lactoglobulin rapidly and crystalline bovine plasma albumin very slowly. The enzyme is most active at 50 °C. but is essentially inactivated in 15 minutes at 60 °C. The optimum pH for enzyme activity is 5.5 to 6.4. The possible role of the proteinase in cheese ripening is discussed.