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

• Published in: Applied biochemistry and microbiology Vol. 57; no. 2; pp. 200 - 205
• Main Authors: Popova, E. A., Kreyer, V. G., Komarevtsev, S. K., Shabunin, S. V., Osmolovskiy, A. A.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01-03-2021; Springer Nature B.V
• Subjects: Biochemistry; Biomedical and Life Sciences; Collagen; Elastin; Fermentation; Fibrin; Life Sciences; Medical Microbiology; Microbiology; Molecular weight; Proteinase; Proteins; Serine; Serine proteinase; Solid state fermentation; collagenolytic enzymes; proteinases of micromycetes; enzymes highly active in relation to fibrillar proteins
• ISSN: 0003-6838; 1608-3024
• DOI: 10.1134/S0003683821020125

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.