TY - JOUR
T1 - Kinetics of Enzymatic Reactions at the Solid/Liquid Interface in Nanofluidic Channels
AU - Yamamoto, Koki
AU - Morikawa, Kyojiro
AU - Imanaka, Hiroyuki
AU - Imamura, Koreyoshi
AU - Kitamori, Takehiko
N1 - Funding Information:
The authors would like to thank Prof. Masaya Miyazaki from the Kyushu University and Prof. Kiichi Sato from Gunma University for fruitful discussions. Fabrication and observation facilities were provided in part by the Academic Consortium for Nano and Micro Fabrication of four universities (The University of Tokyo, Tokyo Institute of Technology, Keio University, and Waseda University, Japan) and the Advanced Characterization Nanotechnology Platform of the University of Tokyo, supported by the “Nanotechnology Platform” of the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan. The authors gratefully acknowledge Core Research for Evolutional Science and Technology (CREST) of the Japan Science and Technology Agency (JST) grant no. JPMJCR14G1, and in part, from the Taiwan, Ministry of Science and Technologyunder grant no. MOST 109-2639-E-007-001-ASP and MOST 110-2639-E-007-002-ASP for financial support.
Publisher Copyright:
© 2022 American Chemical Society.
PY - 2022
Y1 - 2022
N2 - Nanostructures can realize highly efficient reactions due to their structural advantages. However, the mechanism of accelerating enzyme reactions in a nanospace is still unknown from a kinetic perspective because it is difficult to control a well-defined nanospace, enzyme density, and reaction time. Here, we investigated kinetic parameters of an immobilized enzyme in micro- and nanochannels using nanofabrication, partial enzyme patterning, fluidic control, and a high sensitivity detection system. Devices with channel depths of 300 nm, 4.4 μm, and 13.6 μm were fabricated. Kinetic parameters were determined by the Michaelis-Menten model. Compared to the bulk reaction, all kcats for immobilized enzyme reactors were decreased, although the kcats were approximately the same for the immobilized enzyme reactors of different depths. An ultrafast enzyme reaction could overcome the drawback due to immobilization by an increase of the apparent [E]0 due to the decreased channel depth.
AB - Nanostructures can realize highly efficient reactions due to their structural advantages. However, the mechanism of accelerating enzyme reactions in a nanospace is still unknown from a kinetic perspective because it is difficult to control a well-defined nanospace, enzyme density, and reaction time. Here, we investigated kinetic parameters of an immobilized enzyme in micro- and nanochannels using nanofabrication, partial enzyme patterning, fluidic control, and a high sensitivity detection system. Devices with channel depths of 300 nm, 4.4 μm, and 13.6 μm were fabricated. Kinetic parameters were determined by the Michaelis-Menten model. Compared to the bulk reaction, all kcats for immobilized enzyme reactors were decreased, although the kcats were approximately the same for the immobilized enzyme reactors of different depths. An ultrafast enzyme reaction could overcome the drawback due to immobilization by an increase of the apparent [E]0 due to the decreased channel depth.
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U2 - 10.1021/acs.analchem.2c02878
DO - 10.1021/acs.analchem.2c02878
M3 - Article
AN - SCOPUS:85141495424
SN - 0003-2700
JO - Analytical Chemistry
JF - Analytical Chemistry
ER -