TY - JOUR
T1 - Crowding and confinement effects on enzyme stability in mesoporous silicas
AU - Shin, Sujeong
AU - Kim, Han Sol
AU - Kim, Moon Il
AU - Lee, Jinwoo
AU - Park, Hyun Gyu
AU - Kim, Jungbae
N1 - Funding Information:
This work was supported by the Global Research Laboratory Program ( 2014K1A1A2043032 ) through the National Research Foundation of Korea (NRF) grant funded by the Korea government Ministry of Science and ICT (MSIT). This work was supported by the Korea CCS R&D Center (Korea CCS 2020 Project) grant funded by the Korea government ( MSIT ) in 2019 ( KCRC-2018M1A8A1057172 ). This work was also supported by the Korea Institute of Energy Technology Evaluation and Planning (KETEP) and the Korea government Ministry of Trade, Industry & Energy ( MOTIE ) ( 20182010600430 ). We thank Li Na Kim for helping revision experiments. Appendix A
Funding Information:
This work was supported by the Global Research Laboratory Program (2014K1A1A2043032) through the National Research Foundation of Korea (NRF) grant funded by the Korea government Ministry of Science and ICT (MSIT). This work was supported by the Korea CCS R&D Center (Korea CCS 2020 Project) grant funded by the Korea government (MSIT) in 2019 (KCRC-2018M1A8A1057172). This work was also supported by the Korea Institute of Energy Technology Evaluation and Planning (KETEP) and the Korea government Ministry of Trade, Industry & Energy (MOTIE) (20182010600430). We thank Li Na Kim for helping revision experiments.
Publisher Copyright:
© 2019
PY - 2020/2/1
Y1 - 2020/2/1
N2 - To understand the protein functions within a cell, where proteins exist in an extremely crowded and confined state, various modeling and experimental methods have been proposed. Here, we propose a new experimental approach to modulate the macromolecular crowding and/or confinement effects by using mesoporous silicas with two different pore structures. SBA-15 and MSU-F with linear and mesocellular pore structures, respectively, were used to adsorb a model enzyme, glucose oxidase (GOx), in various concentrations ranging from 3 to 430 mg ml−1. The concentration of adsorbed GOx in the mesopores, representing the degree of crowding, showed a good correlation with thermal enzyme stability. Interestingly, the increase of thermal stability as a function of macromolecular crowding showed different correlations depending on the pore structure of mesoporous silicas. It represents that combination of crowding and confinement effects can promote different microenvironments for enzyme molecules, while mesoporous silicas can impose controlled crowding and confinement effects on enzymes due to their uniform and tunable pore structures. It is anticipated that this new and simple approach can provide a tool to elucidate crowding and confinement effects on the protein functions, including its stability in vivo, because the mesopore environments could mimic the real macromolecular cell system under crowding.
AB - To understand the protein functions within a cell, where proteins exist in an extremely crowded and confined state, various modeling and experimental methods have been proposed. Here, we propose a new experimental approach to modulate the macromolecular crowding and/or confinement effects by using mesoporous silicas with two different pore structures. SBA-15 and MSU-F with linear and mesocellular pore structures, respectively, were used to adsorb a model enzyme, glucose oxidase (GOx), in various concentrations ranging from 3 to 430 mg ml−1. The concentration of adsorbed GOx in the mesopores, representing the degree of crowding, showed a good correlation with thermal enzyme stability. Interestingly, the increase of thermal stability as a function of macromolecular crowding showed different correlations depending on the pore structure of mesoporous silicas. It represents that combination of crowding and confinement effects can promote different microenvironments for enzyme molecules, while mesoporous silicas can impose controlled crowding and confinement effects on enzymes due to their uniform and tunable pore structures. It is anticipated that this new and simple approach can provide a tool to elucidate crowding and confinement effects on the protein functions, including its stability in vivo, because the mesopore environments could mimic the real macromolecular cell system under crowding.
KW - Confinement effect
KW - Crowding effect
KW - Mesoporous silicas
UR - http://www.scopus.com/inward/record.url?scp=85076632754&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2019.12.034
DO - 10.1016/j.ijbiomac.2019.12.034
M3 - Article
C2 - 31812745
AN - SCOPUS:85076632754
VL - 144
SP - 118
EP - 126
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
SN - 0141-8130
ER -