Abstract
The microscopic kinetics of enzymes at the single-molecule level often deviate considerably from those expected from bulk biochemical experiments. Here, we propose a coarse-grained-model approach to bridge this gap, focusing on the unexpectedly slow bulk hydrolysis of crystalline cellulose by cellulase, which constitutes a major obstacle to mass production of biofuels and biochemicals. Building on our previous success in tracking the movements of single molecules of cellulase on crystalline cellulose, we develop a mathematical description of the collective motion and function of enzyme molecules hydrolyzing the surface of cellulose. Model simulations robustly explained the experimental findings at both the microscopic and macroscopic levels and revealed a hitherto-unknown mechanism causing a considerable slowdown of the reaction, which we call the crowding-out effect. The size of the cellulase molecule impacted significantly on the collective dynamics, whereas the rate of molecular motion on the surface did not.
| Original language | English |
|---|---|
| Article number | 098102 |
| Number of pages | 5 |
| Journal | Physical Review Letters |
| Volume | 122 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - 7 Mar 2019 |
| MoE publication type | Not Eligible |
Fingerprint
Keywords
- Biochemistry
- Biomolecular processes
- Chemical kinetics
Cite this
}
Bridging the Micro-Macro Gap between Single-Molecular Behavior and Bulk Hydrolysis Properties of Cellulase. / Ezaki, Takahiro (Corresponding Author); Nishinari, Katsuhiro; Samejima, Masahiro; Igarashi, Kiyohiko (Corresponding Author).
In: Physical Review Letters, Vol. 122, No. 9, 098102, 07.03.2019.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Bridging the Micro-Macro Gap between Single-Molecular Behavior and Bulk Hydrolysis Properties of Cellulase
AU - Ezaki, Takahiro
AU - Nishinari, Katsuhiro
AU - Samejima, Masahiro
AU - Igarashi, Kiyohiko
PY - 2019/3/7
Y1 - 2019/3/7
N2 - The microscopic kinetics of enzymes at the single-molecule level often deviate considerably from those expected from bulk biochemical experiments. Here, we propose a coarse-grained-model approach to bridge this gap, focusing on the unexpectedly slow bulk hydrolysis of crystalline cellulose by cellulase, which constitutes a major obstacle to mass production of biofuels and biochemicals. Building on our previous success in tracking the movements of single molecules of cellulase on crystalline cellulose, we develop a mathematical description of the collective motion and function of enzyme molecules hydrolyzing the surface of cellulose. Model simulations robustly explained the experimental findings at both the microscopic and macroscopic levels and revealed a hitherto-unknown mechanism causing a considerable slowdown of the reaction, which we call the crowding-out effect. The size of the cellulase molecule impacted significantly on the collective dynamics, whereas the rate of molecular motion on the surface did not.
AB - The microscopic kinetics of enzymes at the single-molecule level often deviate considerably from those expected from bulk biochemical experiments. Here, we propose a coarse-grained-model approach to bridge this gap, focusing on the unexpectedly slow bulk hydrolysis of crystalline cellulose by cellulase, which constitutes a major obstacle to mass production of biofuels and biochemicals. Building on our previous success in tracking the movements of single molecules of cellulase on crystalline cellulose, we develop a mathematical description of the collective motion and function of enzyme molecules hydrolyzing the surface of cellulose. Model simulations robustly explained the experimental findings at both the microscopic and macroscopic levels and revealed a hitherto-unknown mechanism causing a considerable slowdown of the reaction, which we call the crowding-out effect. The size of the cellulase molecule impacted significantly on the collective dynamics, whereas the rate of molecular motion on the surface did not.
KW - Biochemistry
KW - Biomolecular processes
KW - Chemical kinetics
UR - http://www.scopus.com/inward/record.url?scp=85062984719&partnerID=8YFLogxK
U2 - 10.1103/PhysRevLett.122.098102
DO - 10.1103/PhysRevLett.122.098102
M3 - Article
VL - 122
JO - Physical Review Letters
JF - Physical Review Letters
SN - 0031-9007
IS - 9
M1 - 098102
ER -