TY - JOUR
T1 - Attachment of pentaammineruthenium(III) to Trichoderma reesei cellobiohydrolase I increases its catalytic activity
AU - Evans, Barbara R.
AU - Margalit, Ruth
AU - Woodward, Jonathan
PY - 1993/9/15
Y1 - 1993/9/15
N2 - Pentaammineruthenium(III) was covalently attached to cellobiohydrolase I (CBH I, EC 3.2.1.91), the major component of Trichoderma reesei cellulase, resulting in 0.7 mol ruthenium/mol CBH I and an electrode potential of +95 mV. Fractionation of modified CBH I by chromatofocusing resulted in the separation of fractions with a 1.4- to 3.2-fold increase in specific activity toward p-nitrophenylcellobioside, depending on the assay conditions, over that of native enzyme. The extent of the hydrolysis of insoluble cellulosic substrates (Avicel and newsprint) to glucose by modified CBH I was also greater than that observed by the native enzyme.
AB - Pentaammineruthenium(III) was covalently attached to cellobiohydrolase I (CBH I, EC 3.2.1.91), the major component of Trichoderma reesei cellulase, resulting in 0.7 mol ruthenium/mol CBH I and an electrode potential of +95 mV. Fractionation of modified CBH I by chromatofocusing resulted in the separation of fractions with a 1.4- to 3.2-fold increase in specific activity toward p-nitrophenylcellobioside, depending on the assay conditions, over that of native enzyme. The extent of the hydrolysis of insoluble cellulosic substrates (Avicel and newsprint) to glucose by modified CBH I was also greater than that observed by the native enzyme.
UR - https://www.scopus.com/pages/publications/0027337376
U2 - 10.1006/bbrc.1993.2071
DO - 10.1006/bbrc.1993.2071
M3 - Article
C2 - 8363625
AN - SCOPUS:0027337376
SN - 0006-291X
VL - 195
SP - 497
EP - 503
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -