Mycologia
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
DOI: 10.3852/mycologia.99.4.493
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pessoni, R. A. B.
Right arrow Articles by Figueiredo-Ribeiro, R. d. C. L.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Pessoni, R. A. B.
Right arrow Articles by Figueiredo-Ribeiro, R. d. C. L.
Agricola
Right arrow Articles by Pessoni, R. A. B.
Right arrow Articles by Figueiredo-Ribeiro, R. d. C. L.
Mycologia, 99(4), 2007, pp. 493-503.
© 2007 by The Mycological Society of America

Purification and properties of exo-inulinases from Penicillium janczewskii growing on distinct carbon sources


Rosemeire A. B. Pessoni

     Universidade Metodista de São Paulo, CP 5002, São Bernardo do Campo, SP 09735-460, Brazil

Marcia R. Braga
Rita de Cássia L. Figueiredo-Ribeiro 1

     Instituto de Botânica, Seção de Fisiologia e Bioquímica de Plantas, CP 4005, São Paulo, SP 01061-970, Brazil

Penicillium janczewskii, isolated from the rhizosphere of Vernonia herbacea, grows rapidly on media containing either sucrose or inulin, although inulin more than sucrose induced the production of inulinases. Three different extracellular ß-fructofuranosidases (two inulinases and one invertase) were purified from fungal cultures grown on sucrose or inulin, through precipitation with ammonium sulfate, and anion-exchange, hydrophobic interaction and gel filtration chromatographies. The optimum temperature of the three enzymes was approximately 60 C, optimum pH 4–5.5 and apparent molecular mass of 80 kDa. Km and Vmax values determined for invertase on sucrose were respectively 3.7 10–4 M and 7.9 10–2 µmol/min/mL, and on inulin 6.3 10–2 M and 2.09 10–2 µmol/min/mL. The values of km for the two inulinases were 8.11 10–4 and 2.62 10–3 M, being lower for inulin when compared to those obtained for sucrose. The inulinases did not produce oligofructans from inulin, indicating they are primarily exoinulinases. The differences found in inulinase induction patterns when inulin or sucrose was used seem to be related to modifications on the enzyme properties, mainly concerning substrate affinity.

Key words: ß-fructofuranosidases, enzyme purification, filamentous fungus, inulin, sucrose

1 Corresponding author. E-mail: ritarib{at}usp.br






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2007 by The Mycological Society of America.