Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Microbiology 149 (2003), 2941-2946; DOI  10.1099/mic.0.26346-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
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 CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ramírez-Coronel, M. A.
Right arrow Articles by Augur, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ramírez-Coronel, M. A.
Right arrow Articles by Augur, C.
Agricola
Right arrow Articles by Ramírez-Coronel, M. A.
Right arrow Articles by Augur, C.
Microbiology 149 (2003), 2941-2946; DOI  10.1099/mic.0.26346-0
© 2003 Society for General Microbiology

A novel tannase from Aspergillus niger with {beta}-glucosidase activity

M. Ascención Ramírez-Coronel1,2, Gustavo Viniegra-González1, Alan Darvill3 and Christopher Augur2,{dagger}

1 Departamento de Biotecnología, Universidad Autónoma Metropolitana, Av. Michoacán y la Purísima s/n, Colonia Vicentina, Iztapalapa, México DF, CP 09340, Mexico
2 IRD-México, Cicerón 609, Los Morales, CP 11530, México DF, Mexico
3 Complex Carbohydrate Research Center, The University of Georgia, 220 Riverbend Road, Athens, GA 30602-4712, USA

Correspondence
Christopher Augur
caugur{at}esil.univ-mrs.fr

An extracellular tannase was produced from solid-state cultures of Aspergillus niger. The enzyme was purified to homogeneity from the cell-free culture broth by preparative isoelectric focusing and by FPLC using anion-exchange and gel-filtration chromatography. SDS-PAGE analysis as well as gel localization studies of purified tannase indicated the presence of two enzyme forms, with molecular masses of 90 kDa and 180 kDa. The tannase had an isoelectric point of 3·8, a temperature optimum of 60–70 °C and a pH optimum of 6·0. The substrate specificity of the tannase was determined by HPLC analysis of tannin substrates and products. The enzyme was able to remove gallic acid from both condensed and hydrolysable tannins. Internal sequences were obtained from each of the gel-purified and trypsin-digested tannase forms. The peptide sequences obtained from both forms were identical to sequences within a {beta}-glucosidase from Aspergillus kawachii. The purified tannase was tested for {beta}-glucosidase activity and was shown to hydrolyse cellobiose efficiently. However, no {beta}-glucosidase activity was detected when the enzyme was assayed in the presence of tannic acid.


Abbreviations: HPAEC-PAD, high-performance anion-exchange chromatography-pulsed amperometric detection; PUF, polyurethane foam; SmF, submerged fermentation; SSF, solid-state fermentation

{dagger}Present address: Laboratoire de Microbiologie, IRD, Université de Provence CESB/ESIL, Case 925, 163, Avenue de Luminy, F-13288 Marseille Cedex 9, France.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2003 Society for General Microbiology.