Attachments of pentaammineruthenium(III) to Trichoderma reesei cellobiohydrolase I increases its catalytic activity.
Pentaammineurthenium(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.
Evans
B R
BR
Chemical Technology Division, Oak Ridge National Laboratory, TN 37831-6194.
Margalit
R
R
Woodward
J
J
D043366:Cellulose 1,4-beta-Cellobiosidase; D006026:Glycoside Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007700:Kinetics; D008970:Molecular Weight; D011485:Protein Binding; D012428:Ruthenium / Q000378:metabolism* / Q000494:pharmacology; D017975:Ruthenium Compounds; D014242:Trichoderma / Q000201:enzymology*
D017975:Ruthenium Compounds; C063246:pentaammineruthenium(3+); D012428:Ruthenium; D006026:Glycoside Hydrolases; D043366:Cellulose 1,4-beta-Cellobiosidase