Abstract
| Original language | English |
|---|---|
| Title of host publication | Applications of Enzymes to Lignocellulosics |
| Editors | Shawn D. Mansfield, John N. Saddler |
| Place of Publication | Washington, DC |
| Publisher | American Chemical Society ACS |
| Pages | 285-303 |
| ISBN (Print) | 0-8412-3831-6 |
| DOIs | |
| Publication status | Published - 2003 |
| MoE publication type | D2 Article in professional manuals or guides or professional information systems or text book material |
| Event | 223rd ACS National Meeting - Orlando, United States Duration: 7 Apr 2002 → 11 Apr 2002 |
Publication series
| Series | ACS Symposium Series |
|---|---|
| Volume | 855 |
| ISSN | 0097-6156 |
Conference
| Conference | 223rd ACS National Meeting |
|---|---|
| Country | United States |
| City | Orlando |
| Period | 7/04/02 → 11/04/02 |
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Characterization of the activity profile in cellulases derived from recombinant strains of Trichoderma reesei. / Zandona, F. A.; Cancelier, P. D.; Siika-aho, Matti; Ramos, L. P.
Applications of Enzymes to Lignocellulosics. ed. / Shawn D. Mansfield; John N. Saddler. Washington, DC : American Chemical Society ACS, 2003. p. 285-303 (ACS Symposium Series, Vol. 855).Research output: Chapter in Book/Report/Conference proceeding › Chapter or book article › Professional
TY - CHAP
T1 - Characterization of the activity profile in cellulases derived from recombinant strains of Trichoderma reesei
AU - Zandona, F. A.
AU - Cancelier, P. D.
AU - Siika-aho, Matti
AU - Ramos, L. P.
PY - 2003
Y1 - 2003
N2 - Enzyme preparations from eight deletion strains ofTrichoderma reesei were characterized with regard to their activity profile against several model substrates, and subsequently compared to the complete cellulase system of the industrial preparation Celluclast 1.5L (Novozymes, Denmark). The recombinant enzymes (Röhm Enzyme Finland Oy, Finland) comprised of 4 single (A, CBH I-; B, CBH II-; C, EG I-; D, EG II-), 2 double- ( E, CBH I/II-, F, EG I/II-) and 2 trideletion (G, EG II-/CBH I/II-; H, CBH II-/EG I/II-) enzymes. Compared to Celluclast 1.5L, deletion of both genes encoding for EG I and EG II (enzyme F) resulted in very little endoglucanase activity in the enzyme preparation, whereas the absence of both CBH I and CBH II (enzyme E) reduced filter paper activity by more than 75%. In general, for saccharification experiments in which less than 2% of the substrate was hydrolyzed to soluble sugars, EG-rich preparations (enzyme E at 200 mg/g) caused a considerable decrease in the degree of depolymerization (DP) of substrates with high amorphous character (e.g., filter paper fibers), whereas cellulose DP was not affected when substrates having a higher supramolecular organization were used (e.g., Avicel, Sigmacell or cotton fibers). By contrast, when CBH-rich preparations (enzyme F, 200 mg/g) were used, greater cellulose saccharification yields were observed (14%), and changes in cellulose DP were primarily due to the progressive removal of cellobiose residues from the termini of cellulose molecules.
AB - Enzyme preparations from eight deletion strains ofTrichoderma reesei were characterized with regard to their activity profile against several model substrates, and subsequently compared to the complete cellulase system of the industrial preparation Celluclast 1.5L (Novozymes, Denmark). The recombinant enzymes (Röhm Enzyme Finland Oy, Finland) comprised of 4 single (A, CBH I-; B, CBH II-; C, EG I-; D, EG II-), 2 double- ( E, CBH I/II-, F, EG I/II-) and 2 trideletion (G, EG II-/CBH I/II-; H, CBH II-/EG I/II-) enzymes. Compared to Celluclast 1.5L, deletion of both genes encoding for EG I and EG II (enzyme F) resulted in very little endoglucanase activity in the enzyme preparation, whereas the absence of both CBH I and CBH II (enzyme E) reduced filter paper activity by more than 75%. In general, for saccharification experiments in which less than 2% of the substrate was hydrolyzed to soluble sugars, EG-rich preparations (enzyme E at 200 mg/g) caused a considerable decrease in the degree of depolymerization (DP) of substrates with high amorphous character (e.g., filter paper fibers), whereas cellulose DP was not affected when substrates having a higher supramolecular organization were used (e.g., Avicel, Sigmacell or cotton fibers). By contrast, when CBH-rich preparations (enzyme F, 200 mg/g) were used, greater cellulose saccharification yields were observed (14%), and changes in cellulose DP were primarily due to the progressive removal of cellobiose residues from the termini of cellulose molecules.
U2 - 10.1021/bk-2003-0855.ch017
DO - 10.1021/bk-2003-0855.ch017
M3 - Chapter or book article
SN - 0-8412-3831-6
T3 - ACS Symposium Series
SP - 285
EP - 303
BT - Applications of Enzymes to Lignocellulosics
A2 - Mansfield, Shawn D.
A2 - Saddler, John N.
PB - American Chemical Society ACS
CY - Washington, DC
ER -