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Formation and Properties of the Extracellular Proteinase of Aspergillus flavus O-1 Micromycete Active against Fibrillar Proteins

Formation and Properties of the Extracellular Proteinase of Aspergillus flavus O-1 Micromycete... It has been shown that the Aspergillus flavus O-1 micromycete secretes a complex of at least two proteolytic enzymes. The most active enzyme was isolated via preparative isoelectric focusing and characterized as a serine proteinase with a molecular weight of 17 kDa and a pI of 7.82. The proteinase had a broad substrate specificity and was able to degrade fibrillar proteins such as collagen, elastin, and fibrin. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Formation and Properties of the Extracellular Proteinase of Aspergillus flavus O-1 Micromycete Active against Fibrillar Proteins

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Publisher
Springer Journals
Copyright
Copyright © Pleiades Publishing, Inc. 2021. ISSN 0003-6838, Applied Biochemistry and Microbiology, 2021, Vol. 57, No. 5, pp. 586–593. © Pleiades Publishing, Inc., 2021. Russian Text © The Author(s), 2021, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2021, Vol. 57, No. 5, pp. 458–466.
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/s0003683821050069
Publisher site
See Article on Publisher Site

Abstract

It has been shown that the Aspergillus flavus O-1 micromycete secretes a complex of at least two proteolytic enzymes. The most active enzyme was isolated via preparative isoelectric focusing and characterized as a serine proteinase with a molecular weight of 17 kDa and a pI of 7.82. The proteinase had a broad substrate specificity and was able to degrade fibrillar proteins such as collagen, elastin, and fibrin.

Journal

Applied Biochemistry and MicrobiologySpringer Journals

Published: Sep 1, 2021

Keywords: Aspergillus flavus; proteinases; serine proteinases; proteolytic activity

References