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Applied and Environmental Microbiology, June 2001, p. 2754-2759, Vol. 67, No. 6
IABBAM Consiglio Nazionale delle Ricerche,
80147 Naples,1 Dipartimento di Chimica
Organica e Biochimica, Università di Napoli "Federico II,"
Complesso Universitario Monte S. Angelo, 80126 Naples,2 and CEINGE s.c.r.l., 80131 Naples,3 Italy
Received 9 November 2000/Accepted 22 March 2001
A new extracellular protease (PoSl; Pleurotus
ostreatus subtilisin-like protease) from P.
ostreatus culture broth has been purified and characterized.
PoSl is a monomeric glycoprotein with a molecular mass of 75 kDa, a pI
of 4.5, and an optimum pH in the alkaline range. The inhibitory profile
indicates that PoSl is a serine protease. The N-terminal and three
tryptic peptide sequences of PoSl have been determined. The homology of
one internal peptide with conserved sequence around the Asp residue of
the catalytic triad in the subtilase family suggests that PoSl is a
subtilisin-like protease. This hypothesis is further supported by the
finding that PoSl hydrolysis sites of the insulin B chain match
those of subtilisin. PoSl activity is positively affected by calcium. A
10-fold decrease in the Km value in
the presence of calcium ions can reflect an induced structural change in the substrate recognition site region. Furthermore, Ca2+
binding slows PoSl autolysis, triggering the protein to form a more
compact structure. These effects have already been observed for
subtilisin and other serine proteases. Moreover, PoSl protease seems to
play a key role in the regulation of P. ostreatus
laccase activity by degrading and/or activating different isoenzymes.
0099-2240/01/$04.00+0 DOI: 10.1128/AEM.67.6.2754-2759.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Purification, Characterization, and Functional Role
of a Novel Extracellular Protease from Pleurotus
ostreatus
*
Corresponding author. Mailing address: Dipartimento di
Chimica Organica e Biochimica, Università di Napoli "Federico
II," Complesso Universitario Monte S. Angelo, via Cinthia, 80126 Naples, Italy. Phone: 39 081 674310. Fax: 39 081 674313. E-mail:
sannia{at}unina.it.
Applied and Environmental Microbiology, June 2001, p. 2754-2759, Vol. 67, No. 6
0099-2240/01/$04.00+0 DOI: 10.1128/AEM.67.6.2754-2759.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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