Hemicellulase activity of aerobic fungal cellulases
2000 (English)In: Holzforschung, ISSN 0018-3830, Vol. 54, no 5, 497-500 p.Article in journal (Refereed) Published
Cellulases isolated from Trichoderma reesei and Phanerochaete chrysosporium were screened for hemi-cellulolytic, 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.
Place, publisher, year, edition, pages
2000. Vol. 54, no 5, 497-500 p.
cellulose-binding domain (CBD), cellobiohydrolase (CBH), carboxymethylated cellulose (CMC), endoglucanase (EG), lignin carbohydrate complexes (LCCs), Phanerochaete chrysosporium, Trichoderma reesei, phanerochaete-chrysosporium, trichoderma-reesei, residual lignin, kraft pulps, cellulose, purification, polymers, enzyme, bonds
IdentifiersURN: urn:nbn:se:kth:diva-20070DOI: 10.1515/HF.2000.084ISI: 000089643300010OAI: oai:DiVA.org:kth-20070DiVA: diva2:338763
QC 20100525 NR 201408042010-08-102010-08-102012-01-31Bibliographically approved