期刊
ACS SUSTAINABLE CHEMISTRY & ENGINEERING
卷 8, 期 17, 页码 6722-6733出版社
AMER CHEMICAL SOC
DOI: 10.1021/acssuschemeng.0c00779
关键词
Cellulose; Heterogeneous catalysis; Enzyme kinetics; Biofuels; Surface-reactions; Cellulase; Interfacial biocatalysis; Kinetic modeling
资金
- U.S. Department of Energy (DOE) Office of Science [DE-AC02-05CH11231]
- DOE BER Bioimaging Science Program [DE-SC0019228]
- ALS Doctoral Fellowship in Residence Program
- DOE OS Office of Workforce Development for Teachers and Scientists, Office of Science Graduate Student Research (SCGSR)
- Oak Ridge Institute for Science and Education for the DOE [DE-SC0014664]
- DOE/BER [DE-AC02-05CH11231]
- U.S. Department of Energy (DOE) [DE-SC0019228] Funding Source: U.S. Department of Energy (DOE)
Interfacial enzyme reactions require formation of an enzyme-substrate complex at the surface of a heterogeneous substrate, but often multiple modes of enzyme binding and types of binding sites complicate analysis of their kinetics. Excess heterogeneous substrate is often used as a justification to model the substrate as unchanging, but using the study of the enzymatic hydrolysis of insoluble cellulose as an example, we argue that reaction rates are dependent on evolving substrate interfacial properties. We hypothesize that the relative abundance of binding sites on cellulose where hydrolysis can occur (productive binding sites) and binding sites where hydrolysis cannot be initiated or is inhibited (nonproductive binding sites) contribute to rate limitations. We show that the initial total number of productive binding sites (the productive binding capacity) determines the magnitude of the initial burst phase of cellulose hydrolysis, while productive binding site depletion explains overall hydrolysis kinetics. Furthermore, we show that irreversibly bound surface enzymes contribute to the depletion of productive binding sites. Our model shows that increasing the ratio of productive to nonproductive binding sites promotes hydrolysis, while maintaining an elevated productive binding capacity throughout conversion is key to preventing hydrolysis slowdown.
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