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 language | English |
|---|---|
| Pages (from-to) | 105-109 |
| Number of pages | 5 |
| Journal | Folia Microbiologica |
| Volume | 54 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Mar 2009 |
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ASJC Scopus subject areas
- Microbiology
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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 journal › Article
}
TY - JOUR
T1 - PepJ is a new extracellular proteinase of Aspergillus nidulans
AU - Emri, T.
AU - Szilágyi, M.
AU - Kiss, L.
AU - M-Hamvas, M.
AU - Pócsi, I.
PY - 2009/3
Y1 - 2009/3
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=65649126844&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=65649126844&partnerID=8YFLogxK
U2 - 10.1007/s12223-009-0015-8
DO - 10.1007/s12223-009-0015-8
M3 - Article
VL - 54
SP - 105
EP - 109
JO - Folia Microbiologica
JF - Folia Microbiologica
SN - 0015-5632
IS - 2
ER -