One-dimensional crosslinked enzyme aggregates in SBA-15: Superior catalytic behavior to conventional enzyme immobilization

Moon Il Kim; Jungbae Kim; Jinwoo Lee; Sujeong Shin; Hyon Bin Na; Taeghwan Hyeon; Hyun Gyu Park; Ho Nam Chang

doi:10.1016/j.micromeso.2007.07.009

One-dimensional crosslinked enzyme aggregates in SBA-15: Superior catalytic behavior to conventional enzyme immobilization

Moon Il Kim
, Jungbae Kim^*
, Jinwoo Lee
, Sujeong Shin
, Hyon Bin Na
, Taeghwan Hyeon
, Hyun Gyu Park
, Ho Nam Chang

^*Corresponding author for this work

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

71 Citations (Scopus)

Abstract

α-Chymotrypsin (CT) and lipase (LP) were immobilized in SBA-15 mesoporous silica by crosslinking adsorbed enzymes. This simple approach resulted in one-dimensional crosslinked enzyme aggregates (CLEAs) in the linear pore channels of SBA-15, which was very effective in preventing the enzyme leaching and consequently improving the enzyme stability. Both CLEAs of CT and LP showed negligible activity decrease under harsh shaking condition for one week while the conventional approaches including adsorption and covalent attachment resulted in more than 50-90% enzyme inactivation under the same condition. This effective stabilization results from the bent pore structure of SBA-15 with a high aspect ratio, which prevents the leaching of one-dimensional CLEAs and thereby achieves the higher enzyme loading capacity. Along with the higher specific activity than that of adsorbed enzymes, this CLEA approach is much simpler than that of covalent attachment by obviating the tedious processes for silica functionalization and enzyme attachment.

Original language	English
Pages (from-to)	18-23
Number of pages	6
Journal	Microporous and Mesoporous Materials
Volume	111
Issue number	1-3
DOIs	https://doi.org/10.1016/j.micromeso.2007.07.009
Publication status	Published - 2008 Apr 15
Externally published	Yes

Bibliographical note

Funding Information:
This work was supported by the Basic Research Program of the Korea Science & Engineering Foundation (Grant No. R01-2004-000-10293-0) and the Brain Korea 21 Project of the Ministry of Education. Jungbae Kim thank US Department of Energy (DOE) LDRD funds administrated by the Pacific Northwest National Laboratory and DARPA/MTO (Contract DE-AC05-76RL01830). The research was performed in part at the W.R. Wiley Environmental Molecular Sciences Laboratory, a national scientific user facility sponsored by the US Department of Energy’s Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory.

Keywords

CLEAs (crosslinked enzyme aggregates)
Enzyme immobilization
Mucor javanicus lipase
SBA-15
α-Chymotrypsin

ASJC Scopus subject areas

General Chemistry
General Materials Science
Condensed Matter Physics
Mechanics of Materials

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10.1016/j.micromeso.2007.07.009

Cite this

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title = "One-dimensional crosslinked enzyme aggregates in SBA-15: Superior catalytic behavior to conventional enzyme immobilization",

abstract = "α-Chymotrypsin (CT) and lipase (LP) were immobilized in SBA-15 mesoporous silica by crosslinking adsorbed enzymes. This simple approach resulted in one-dimensional crosslinked enzyme aggregates (CLEAs) in the linear pore channels of SBA-15, which was very effective in preventing the enzyme leaching and consequently improving the enzyme stability. Both CLEAs of CT and LP showed negligible activity decrease under harsh shaking condition for one week while the conventional approaches including adsorption and covalent attachment resulted in more than 50-90\% enzyme inactivation under the same condition. This effective stabilization results from the bent pore structure of SBA-15 with a high aspect ratio, which prevents the leaching of one-dimensional CLEAs and thereby achieves the higher enzyme loading capacity. Along with the higher specific activity than that of adsorbed enzymes, this CLEA approach is much simpler than that of covalent attachment by obviating the tedious processes for silica functionalization and enzyme attachment.",

keywords = "CLEAs (crosslinked enzyme aggregates), Enzyme immobilization, Mucor javanicus lipase, SBA-15, α-Chymotrypsin",

author = "Kim, \{Moon Il\} and Jungbae Kim and Jinwoo Lee and Sujeong Shin and Na, \{Hyon Bin\} and Taeghwan Hyeon and Park, \{Hyun Gyu\} and Chang, \{Ho Nam\}",

note = "Funding Information: This work was supported by the Basic Research Program of the Korea Science \& Engineering Foundation (Grant No. R01-2004-000-10293-0) and the Brain Korea 21 Project of the Ministry of Education. Jungbae Kim thank US Department of Energy (DOE) LDRD funds administrated by the Pacific Northwest National Laboratory and DARPA/MTO (Contract DE-AC05-76RL01830). The research was performed in part at the W.R. Wiley Environmental Molecular Sciences Laboratory, a national scientific user facility sponsored by the US Department of Energy{\textquoteright}s Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory. ",

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AU - Kim, Moon Il

AU - Kim, Jungbae

AU - Lee, Jinwoo

AU - Shin, Sujeong

AU - Na, Hyon Bin

AU - Hyeon, Taeghwan

AU - Park, Hyun Gyu

AU - Chang, Ho Nam

N1 - Funding Information: This work was supported by the Basic Research Program of the Korea Science & Engineering Foundation (Grant No. R01-2004-000-10293-0) and the Brain Korea 21 Project of the Ministry of Education. Jungbae Kim thank US Department of Energy (DOE) LDRD funds administrated by the Pacific Northwest National Laboratory and DARPA/MTO (Contract DE-AC05-76RL01830). The research was performed in part at the W.R. Wiley Environmental Molecular Sciences Laboratory, a national scientific user facility sponsored by the US Department of Energy’s Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory.

PY - 2008/4/15

Y1 - 2008/4/15

N2 - α-Chymotrypsin (CT) and lipase (LP) were immobilized in SBA-15 mesoporous silica by crosslinking adsorbed enzymes. This simple approach resulted in one-dimensional crosslinked enzyme aggregates (CLEAs) in the linear pore channels of SBA-15, which was very effective in preventing the enzyme leaching and consequently improving the enzyme stability. Both CLEAs of CT and LP showed negligible activity decrease under harsh shaking condition for one week while the conventional approaches including adsorption and covalent attachment resulted in more than 50-90% enzyme inactivation under the same condition. This effective stabilization results from the bent pore structure of SBA-15 with a high aspect ratio, which prevents the leaching of one-dimensional CLEAs and thereby achieves the higher enzyme loading capacity. Along with the higher specific activity than that of adsorbed enzymes, this CLEA approach is much simpler than that of covalent attachment by obviating the tedious processes for silica functionalization and enzyme attachment.

AB - α-Chymotrypsin (CT) and lipase (LP) were immobilized in SBA-15 mesoporous silica by crosslinking adsorbed enzymes. This simple approach resulted in one-dimensional crosslinked enzyme aggregates (CLEAs) in the linear pore channels of SBA-15, which was very effective in preventing the enzyme leaching and consequently improving the enzyme stability. Both CLEAs of CT and LP showed negligible activity decrease under harsh shaking condition for one week while the conventional approaches including adsorption and covalent attachment resulted in more than 50-90% enzyme inactivation under the same condition. This effective stabilization results from the bent pore structure of SBA-15 with a high aspect ratio, which prevents the leaching of one-dimensional CLEAs and thereby achieves the higher enzyme loading capacity. Along with the higher specific activity than that of adsorbed enzymes, this CLEA approach is much simpler than that of covalent attachment by obviating the tedious processes for silica functionalization and enzyme attachment.

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KW - Enzyme immobilization

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KW - SBA-15

KW - α-Chymotrypsin

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ER -

One-dimensional crosslinked enzyme aggregates in SBA-15: Superior catalytic behavior to conventional enzyme immobilization

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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