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Publication Date:
June 2005
ISSN:
1437-434X
DOI:
10.1515/HF.2000.084

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Holzforschung

International Journal of the Biology, Chemistry, Physics, and Technology of Wood

Editor-in-Chief: Faix, Oskar

Editorial Board Member: Daniel, Geoffrey / Militz, Holger / Rosenau, Thomas / Salmen, Lennart / Sixta, Herbert / Vuorinen, Tapani / Argyropoulos, Dimitris S. / Balakshin, Yu / Barnett, J. R. / Berry, Richard / Burgert, Ingo / Evans, Robert / Evtuguin, Dmitry V. / Frazier, Charles E. / Fukushima, Kazuhiko / Gellerstedt, Göran / Gindl-Altmutter, Wolfgang / Glasser, W. G. / Heitner, Cyril / Holmbom, Bjarne / Isogai, Akira / Kadla, John F. / Kleen, Marjatta / Koch, Gerald / Lachenal, Dominique / Mansfield, Shawn D. / Morrell, J.J. / Niemz, Peter / Pizzi, Antonio / Ragauskas, Arthur J. / Ralph, John / Rice, Robert W. / Salin, Jarl-Gunnar / Schmitt, Uwe / Schultz, Tor P. / Schwanninger, Manfred / Sipilä, Jussi / Tamminen, Tarja / Viikari, Liisa / Welling, Johannes / Willför, Stefan / Yoshihara, Hiroshi

8 Issues per year

Increased IMPACT FACTOR 2011: 1.748
5-year IMPACT FACTOR: 1.838
Rank 2 out of 21 in category Materials Science, Paper & Wood and 10 out of 59 in category Forestry in the 2011 Thomson Reuters Journal Citation Report/Science Edition.

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Hemicellulase Activity of Aerobic Fungal Cellulases

M. Lawoko / A. Nutt / H. Henriksson / G. Gellerstedt / G. Henriksson

Citation Information: Holzforschung. Volume 54, Issue 5, Pages 497–500, ISSN (Print) 0018-3830, DOI: 10.1515/HF.2000.084, June 2005

Publication History:
Published Online:
2005-06-01

Summary

Cellulases isolated from Trichoderma reesei and Phanerochaete chrysosporium were screened for hemicellulolytic, pectinolytic and cellulolytic activity using locust bean mannan, birchwood xylan, citrus fruit pectin and carboxymethylated cellulose (CMC) as substrates. The purpose of this work was to choose appropriate enzymes to include in a “miniature cellulase system” with minimal hemicellulase activity for the preparation of lignin-carbohydrate complexes (LCCs). The endoglucanases showed CMC activity whereas activity towards the substrate was not detected for the CBHs. Xylanase activity was observed for EG I and EG 38 whereas mannanase activity was observed for EG 44. None of the enzymes degraded pectin. The results suggest that CBH I, CBH II, CBH 58, EG II and EG III are good candidates for the effective preparation of LCCs. The possible biological function for the hemicellulolytic activity of cellulases is discussed.

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