Properties of Extracellular Proteinase of the Micromycete Aspergillus ustus 1 and Its High Activity during Fibrillary-Proteins Hydrolysis

A new, nonglycosylated, serine proteinase capable of hydrolyzing collagen, elastin, and fibrin was isolated from a complex preparation of proteins formed by the micromycete A. ustus 1 under solid-state fermentation. The enzyme had a molecular weight of 33 kDa and a pI of 4.6. The pH-optimum (6.0) and temperature optimum (41°C) of the work of this proteinase were also determined.