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dc.contributor.authorKostylev, Maximen_US
dc.date.accessioned2013-09-16T16:37:59Z
dc.date.available2013-09-16T16:37:59Z
dc.date.issued2013-08-19en_US
dc.identifier.otherbibid: 8267376
dc.identifier.urihttps://hdl.handle.net/1813/34175
dc.description.abstractLignocellulosic biomass is a potential source of sustainable transportation fuels, but efficient enzymatic saccharification of cellulose is a key challenge in its utilization. Enzymatic digestion of cellulose is a complex, heterogeneous process. An enzyme must repeatedly take multiple steps to hydrolyze the substrate to product. In addition, most bulk cellulose contains crystalline, semi-crystalline, and amorphous fractions, whose ratio likely changes during digestion. Access to substrate, rather than hydrolysis, is widely accepted to be the rate limiting step, as we showed experimentally using Cel9A, and the rate of digestion rapidly and continuously drops off as digestion proceeds. Predictive kinetic models typically incorporate different parameters and constants to account for the possible factors responsible for such behavior. Cellulose hydrolysis by individual cellulases and their mixtures can be modeled with a simple two-parameter model based on a modified classical kinetics scheme. Analogous to a fractal kinetics approach, the specific activity constant is replaced with a time-dependent activity coefficient in order to account for the continuous decrease in the digestion rate. The parameter that quantifies the time dependence of the digestion rate is an intrinsic constant for a given cellulase or mixture on a given substrate. The developed kinetic model was utilized in studies aimed to understand the function of aromatic residues located near the active site tunnel entrance of Cel48A and to develop a distinct model of synergistic cooperation between Cel48A and Cel9A. Additional experiments were carried out to establish experimentally the catalytic base in family 48 glycoside hydrolases.en_US
dc.language.isoen_USen_US
dc.subjectCellulasesen_US
dc.subjectThermobifida fuscaen_US
dc.subjectCel9Aen_US
dc.subjectCel48Aen_US
dc.subjectcelluloseen_US
dc.subjectbiomassen_US
dc.subjectsynergismen_US
dc.titleStudies Of Thermobifida Fusca Cellulases Cel9A And Cel48A Using A Novel Kinetic Modeling Approach For The Enzymatic Digestion Of Cellulose.en_US
dc.typedissertation or thesisen_US
thesis.degree.disciplineBiochemistry
thesis.degree.grantorCornell Universityen_US
thesis.degree.levelDoctor of Philosophy
thesis.degree.namePh. D., Biochemistry
dc.contributor.chairWilson, David Ben_US
dc.contributor.committeeMemberNicholson, Linda Ken_US
dc.contributor.committeeMemberChen, Pengen_US


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