PepJ is a new extracellular proteinase of Aspergillus nidulans

T. Emri, M. Szilágyi, L. Kiss, M. M-Hamvas, I. Pócsi

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Under carbon starvation, Aspergillus nidulans released a metallo-proteinase with activities comparable to those of PrtA, the major extracellular serine proteinase of the fungus. The relative molar mass of the enzyme was 19 kDa as determined with both denaturing and renaturing SDS PAGE, while its isoelectric point and pH and temperature optima were 8.6, 5.5 and 65 °C, respectively. The enzyme was stable at pH 3.5-10.5 and was still active at 95 °C in the presence of azocasein substrate. MALDI-TOF MS analysis demonstrated that the proteinase was encoded by the pepJ gene (locus ID AN7962.3), and showed high similarity to deuterolysin from Aspergillus oryzae. The size of the mature enzyme, its EDTA sensitivity and heat stability also supported the view that A. nidulans PepJ is a deuterolysin-type metallo-proteinase.

Original languageEnglish
Pages (from-to)105-109
Number of pages5
JournalFolia Microbiologica
Volume54
Issue number2
DOIs
Publication statusPublished - Mar 2009

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Aspergillus nidulans
Peptide Hydrolases
Enzymes
Aspergillus oryzae
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Isoelectric Point
Serine Proteases
Starvation
Edetic Acid
Polyacrylamide Gel Electrophoresis
Fungi
Carbon
Hot Temperature
Temperature
Genes

ASJC Scopus subject areas

  • Microbiology

Cite this

PepJ is a new extracellular proteinase of Aspergillus nidulans. / Emri, T.; Szilágyi, M.; Kiss, L.; M-Hamvas, M.; Pócsi, I.

In: Folia Microbiologica, Vol. 54, No. 2, 03.2009, p. 105-109.

Research output: Contribution to journalArticle

Emri, T. ; Szilágyi, M. ; Kiss, L. ; M-Hamvas, M. ; Pócsi, I. / PepJ is a new extracellular proteinase of Aspergillus nidulans. In: Folia Microbiologica. 2009 ; Vol. 54, No. 2. pp. 105-109.
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