Single enzyme nanoparticles in nanoporous silica: A hierarchical approach to enzyme stabilization and immobilization

Jungbae Kim; Hongfei Jia; Chang won Lee; Seung wook Chung; Ja Hun Kwak; Yongsoon Shin; Alice Dohnalkova; Byung Gee Kim; Ping Wang; Jay W. Grate

doi:10.1016/j.enzmictec.2005.11.042

Single enzyme nanoparticles in nanoporous silica: A hierarchical approach to enzyme stabilization and immobilization

Jungbae Kim, Hongfei Jia, Chang won Lee, Seung wook Chung, Ja Hun Kwak, Yongsoon Shin, Alice Dohnalkova, Byung Gee Kim, Ping Wang, Jay W. Grate

Bioproducts and Biosystems Engineering

Research output: Contribution to journal › Article › peer-review

64 Scopus citations

Abstract

Single enzyme nanoparticles of α-chymotrypsin (SEN-CT), in which each CT molecule is surrounded by a thin polymeric organic/inorganic network, stabilized the CT activity in a shaking condition as well as in a non-shaking condition. Since SEN-CT is soluble in a buffer solution and less than 10 nm in size, SEN-CT could be further immobilized in nanoporous silica with an average pore size of 29 nm. Free CT and SEN-CT were immobilized in nanoporous silica (NPS), and nanoporous silica that was first silanized with aminopropyltriethoxysilane (amino-NPS) to generate a positive surface charge. The SEN-CT adsorbed in amino-NPS was more stable than CT immobilized by either adsorption in NPS or covalent bonding to amino-NPS. In shaking conditions, nanoporous silica provided an additional stabilization by protecting SEN-CT from shear stresses. At 22 °C with harsh shaking, free, NPS-adsorbed and NPS-covalently attached CT showed half lives of 1, 62, and 80 h, respectively; whereas SEN-CT adsorbed in amino-NPS showed no activity loss within 12 days. The combination of SENs and nanoporous silica, which makes an active and stable immobilized enzyme system, represents a new structure for biocatalytic applications.

Original language	English (US)
Pages (from-to)	474-480
Number of pages	7
Journal	Enzyme and Microbial Technology
Volume	39
Issue number	3
DOIs	https://doi.org/10.1016/j.enzmictec.2005.11.042
State	Published - Jul 3 2006

Bibliographical note

Funding Information:
This work was supported by U.S. Department of Energy (DOE) LDRD funds administered by the Pacific Northwest National Laboratory, and the DOE Office of Biological and Environmental Research under the Environmental Management Science Program. The research was performed at the W. R. Wiley Environmental Molecular Sciences Laboratory, a national scientific user facility sponsored by the U.S. Department of Energy's Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory. PNNL is operated for the Department of Energy by Battelle.

Keywords

Enzyme immobilization
Enzyme stabilization
Mesocellular foams
Nanoporous silica
Single enzyme nanoparticles
α-Chymotrypsin

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10.1016/j.enzmictec.2005.11.042

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title = "Single enzyme nanoparticles in nanoporous silica: A hierarchical approach to enzyme stabilization and immobilization",

abstract = "Single enzyme nanoparticles of α-chymotrypsin (SEN-CT), in which each CT molecule is surrounded by a thin polymeric organic/inorganic network, stabilized the CT activity in a shaking condition as well as in a non-shaking condition. Since SEN-CT is soluble in a buffer solution and less than 10 nm in size, SEN-CT could be further immobilized in nanoporous silica with an average pore size of 29 nm. Free CT and SEN-CT were immobilized in nanoporous silica (NPS), and nanoporous silica that was first silanized with aminopropyltriethoxysilane (amino-NPS) to generate a positive surface charge. The SEN-CT adsorbed in amino-NPS was more stable than CT immobilized by either adsorption in NPS or covalent bonding to amino-NPS. In shaking conditions, nanoporous silica provided an additional stabilization by protecting SEN-CT from shear stresses. At 22 °C with harsh shaking, free, NPS-adsorbed and NPS-covalently attached CT showed half lives of 1, 62, and 80 h, respectively; whereas SEN-CT adsorbed in amino-NPS showed no activity loss within 12 days. The combination of SENs and nanoporous silica, which makes an active and stable immobilized enzyme system, represents a new structure for biocatalytic applications.",

keywords = "Enzyme immobilization, Enzyme stabilization, Mesocellular foams, Nanoporous silica, Single enzyme nanoparticles, α-Chymotrypsin",

author = "Jungbae Kim and Hongfei Jia and Lee, {Chang won} and Chung, {Seung wook} and Kwak, {Ja Hun} and Yongsoon Shin and Alice Dohnalkova and Kim, {Byung Gee} and Ping Wang and Grate, {Jay W.}",

note = "Funding Information: This work was supported by U.S. Department of Energy (DOE) LDRD funds administered by the Pacific Northwest National Laboratory, and the DOE Office of Biological and Environmental Research under the Environmental Management Science Program. The research was performed at the W. R. Wiley Environmental Molecular Sciences Laboratory, a national scientific user facility sponsored by the U.S. Department of Energy's Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory. PNNL is operated for the Department of Energy by Battelle.",

year = "2006",

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doi = "10.1016/j.enzmictec.2005.11.042",

language = "English (US)",

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T1 - Single enzyme nanoparticles in nanoporous silica

T2 - A hierarchical approach to enzyme stabilization and immobilization

AU - Kim, Jungbae

AU - Jia, Hongfei

AU - Lee, Chang won

AU - Chung, Seung wook

AU - Kwak, Ja Hun

AU - Shin, Yongsoon

AU - Dohnalkova, Alice

AU - Kim, Byung Gee

AU - Wang, Ping

AU - Grate, Jay W.

N1 - Funding Information: This work was supported by U.S. Department of Energy (DOE) LDRD funds administered by the Pacific Northwest National Laboratory, and the DOE Office of Biological and Environmental Research under the Environmental Management Science Program. The research was performed at the W. R. Wiley Environmental Molecular Sciences Laboratory, a national scientific user facility sponsored by the U.S. Department of Energy's Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory. PNNL is operated for the Department of Energy by Battelle.

PY - 2006/7/3

Y1 - 2006/7/3

N2 - Single enzyme nanoparticles of α-chymotrypsin (SEN-CT), in which each CT molecule is surrounded by a thin polymeric organic/inorganic network, stabilized the CT activity in a shaking condition as well as in a non-shaking condition. Since SEN-CT is soluble in a buffer solution and less than 10 nm in size, SEN-CT could be further immobilized in nanoporous silica with an average pore size of 29 nm. Free CT and SEN-CT were immobilized in nanoporous silica (NPS), and nanoporous silica that was first silanized with aminopropyltriethoxysilane (amino-NPS) to generate a positive surface charge. The SEN-CT adsorbed in amino-NPS was more stable than CT immobilized by either adsorption in NPS or covalent bonding to amino-NPS. In shaking conditions, nanoporous silica provided an additional stabilization by protecting SEN-CT from shear stresses. At 22 °C with harsh shaking, free, NPS-adsorbed and NPS-covalently attached CT showed half lives of 1, 62, and 80 h, respectively; whereas SEN-CT adsorbed in amino-NPS showed no activity loss within 12 days. The combination of SENs and nanoporous silica, which makes an active and stable immobilized enzyme system, represents a new structure for biocatalytic applications.

AB - Single enzyme nanoparticles of α-chymotrypsin (SEN-CT), in which each CT molecule is surrounded by a thin polymeric organic/inorganic network, stabilized the CT activity in a shaking condition as well as in a non-shaking condition. Since SEN-CT is soluble in a buffer solution and less than 10 nm in size, SEN-CT could be further immobilized in nanoporous silica with an average pore size of 29 nm. Free CT and SEN-CT were immobilized in nanoporous silica (NPS), and nanoporous silica that was first silanized with aminopropyltriethoxysilane (amino-NPS) to generate a positive surface charge. The SEN-CT adsorbed in amino-NPS was more stable than CT immobilized by either adsorption in NPS or covalent bonding to amino-NPS. In shaking conditions, nanoporous silica provided an additional stabilization by protecting SEN-CT from shear stresses. At 22 °C with harsh shaking, free, NPS-adsorbed and NPS-covalently attached CT showed half lives of 1, 62, and 80 h, respectively; whereas SEN-CT adsorbed in amino-NPS showed no activity loss within 12 days. The combination of SENs and nanoporous silica, which makes an active and stable immobilized enzyme system, represents a new structure for biocatalytic applications.

KW - Enzyme immobilization

KW - Enzyme stabilization

KW - Mesocellular foams

KW - Nanoporous silica

KW - Single enzyme nanoparticles

KW - α-Chymotrypsin

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U2 - 10.1016/j.enzmictec.2005.11.042

DO - 10.1016/j.enzmictec.2005.11.042

M3 - Article

AN - SCOPUS:33646796717

SN - 0141-0229

VL - 39

SP - 474

EP - 480

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

IS - 3

ER -

Single enzyme nanoparticles in nanoporous silica: A hierarchical approach to enzyme stabilization and immobilization

Abstract

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