Coupling two enzymes into a tandem nanoreactor utilizing a hierarchically structured MOF
Abstract
A hierarchical porous metal–organic framework (MOF), PCN-888, containing three types of cavities was utilized to couple two enzymes into a tandem nanoreactor. The largest cavity (6.2 nm) can only accommodate one molecule of glucose oxidase (GOx). The intermediate cavity (5.0 nm) can accommodate one and only one molecule of horseradish peroxidase (HRP). The small cavity (2.0 nm) has sufficient size for neither GOx nor HRP, and remains open as a substrate diffusion pathway. The coupling of the two enzymes can only be achieved through a unique stepwise encapsulation with a specific order (GOx first, followed by HRP). The tandem nanoreactor shows excellent catalytic performances and negligible enzyme leaching. Its catalytic activity is well maintained within several catalytic cycles. Moreover, PCN-888 can provide protection to the encapsulated enzymes against trypsin digestion, indicating the in vitro and in vivo stability of the nanoreactor.
- Authors:
-
- Texas A&M Univ., College Station, TX (United States). Dept. of Chemistry
- Texas A&M Univ., College Station, TX (United States). Dept. of Chemistry, and Dept. of Materials Science and Engineering
- Publication Date:
- Research Org.:
- Energy Frontier Research Centers (EFRC) (United States). Center for Gas Separations Relevant to Clean Energy Technologies (CGS); Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1388631
- Alternate Identifier(s):
- OSTI ID: 1333963
- Grant/Contract Number:
- SC0001015; DBI-0116835; AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Chemical Science
- Additional Journal Information:
- Journal Volume: 7; Journal Issue: 12; Related Information: CGS partners with University of California, Berkeley; University of California, Davis; Lawrence Berkeley National Laboratory; University of Minnesota; National Energy Technology Laboratory; Texas A&M University; Journal ID: ISSN 2041-6520
- Publisher:
- Royal Society of Chemistry
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; membrane; carbon capture; materials and chemistry by design; synthesis (novel materials); synthesis (self-assembly); synthesis (scalable processing)
Citation Formats
Lian, Xizhen, Chen, Ying-Pin, Liu, Tian-Fu, and Zhou, Hong-Cai. Coupling two enzymes into a tandem nanoreactor utilizing a hierarchically structured MOF. United States: N. p., 2016.
Web. doi:10.1039/c6sc01438k.
Lian, Xizhen, Chen, Ying-Pin, Liu, Tian-Fu, & Zhou, Hong-Cai. Coupling two enzymes into a tandem nanoreactor utilizing a hierarchically structured MOF. United States. https://doi.org/10.1039/c6sc01438k
Lian, Xizhen, Chen, Ying-Pin, Liu, Tian-Fu, and Zhou, Hong-Cai. Thu .
"Coupling two enzymes into a tandem nanoreactor utilizing a hierarchically structured MOF". United States. https://doi.org/10.1039/c6sc01438k. https://www.osti.gov/servlets/purl/1388631.
@article{osti_1388631,
title = {Coupling two enzymes into a tandem nanoreactor utilizing a hierarchically structured MOF},
author = {Lian, Xizhen and Chen, Ying-Pin and Liu, Tian-Fu and Zhou, Hong-Cai},
abstractNote = {A hierarchical porous metal–organic framework (MOF), PCN-888, containing three types of cavities was utilized to couple two enzymes into a tandem nanoreactor. The largest cavity (6.2 nm) can only accommodate one molecule of glucose oxidase (GOx). The intermediate cavity (5.0 nm) can accommodate one and only one molecule of horseradish peroxidase (HRP). The small cavity (2.0 nm) has sufficient size for neither GOx nor HRP, and remains open as a substrate diffusion pathway. The coupling of the two enzymes can only be achieved through a unique stepwise encapsulation with a specific order (GOx first, followed by HRP). The tandem nanoreactor shows excellent catalytic performances and negligible enzyme leaching. Its catalytic activity is well maintained within several catalytic cycles. Moreover, PCN-888 can provide protection to the encapsulated enzymes against trypsin digestion, indicating the in vitro and in vivo stability of the nanoreactor.},
doi = {10.1039/c6sc01438k},
journal = {Chemical Science},
number = 12,
volume = 7,
place = {United States},
year = {Thu Jul 14 00:00:00 EDT 2016},
month = {Thu Jul 14 00:00:00 EDT 2016}
}
Web of Science
Figures / Tables:
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