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Kwak, Ja Hun
Molecular Catalysis lab
Research Interests
  • Heterogeneous catalysis, molecular catalysis, ASlumima, zeolites

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

Cited 33 times inthomson ciCited 34 times inthomson ci
Title
Single enzyme nanoparticles in nanoporous silica: A hierarchical approach to enzyme stabilization and immobilization
Other Titles
Single enzyme nanoparticles in nanoporous silica: A hierarchical approach to enzyme stabilization and immobilization
Author
Kim, JungbaeJia, HongfeiLee, Chang-wonChung, Seung-wookKwak, JahunShin, YongsoonDohnalkova, AliceKim, Byung-GeeWang, PingGrate, Jay W.
Keywords
MESOPOROUS SILICA; CATALYTIC ACTIVITY; ORGANIC-SOLVENTS; BIOCATALYSIS; CHYMOTRYPSIN; SUPPORT; SURFACE
Issue Date
2006-07
Publisher
ELSEVIER SCIENCE INC
Citation
ENZYME AND MICROBIAL TECHNOLOGY, v.39, no.3, pp.474 - 480
Abstract
Single enzyme nanoparticles of alpha-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 degrees 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. (c) 2006 Elsevier Inc. All rights reserved
URI
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DOI
10.1016/j.enzmictec.2005.11.042
ISSN
0141-0229
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ECHE_Journal Papers
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