A mechanistic model for enzymatic saccharification of cellulose using continuous distribution kinetics II: cooperative enzyme action, solution kinetics, and product inhibition.
The projected cost for the enzymatic hydrolysis of cellulosic biomass continues to be a barrier for the commercial production of liquid transportation fuels from renewable feedstocks. Predictive models for the kinetics of the enzymatic reactions will enable an improved understanding of current limitations, such as the slow-down of the overall conversion rate, and may point the way for more efficient utilization of the enzymes in order to achieve higher conversion yields. A mechanistically based kinetic model for the enzymatic hydrolysis of cellulose was recently reported in Griggs et al. (2011) (Part I). In this article (Part II), the enzyme system is expanded to include solution-phase kinetics, particularly cellobiose-to-glucose conversion by β-glucosidase (βG), and novel adsorption and product inhibition schemes have been incorporated, based on current structural knowledge of the component enzymes. Model results show cases of cooperative and non-cooperative hydrolysis for an enzyme system consisting of EG(I) and CBH(I). The model is used to explore various potential rate-limiting phenomena, such as substrate accessibility, product inhibition, sterically hindered enzyme adsorption, and the molecular weight of the cellulose substrate.
National Renewable Energy Laboratory, National Bioenergy Center, 1617 Cole Boulevard, Golden, Colorado 80401, USA.
Andrew J
AJ
Griggs
Jonathan J
JJ
Stickel
James J
JJ
Lischeske
D044602:Cellulases / Q000378:metabolism*; D002482:Cellulose / Q000737:chemistry / Q000378:metabolism*; D043366:Cellulose 1,4-beta-Cellobiosidase / Q000378:metabolism*; D007700:Kinetics; D008962:Models, Theoretical; D001617:beta-Glucosidase / Q000378:metabolism
D002482:Cellulose; D044602:Cellulases; D001617:beta-Glucosidase; D043366:Cellulose 1,4-beta-Cellobiosidase