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 | |
| Publication status | Published - 2008 Apr 15 |
| Externally published | Yes |
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Keywords
- α-Chymotrypsin
- CLEAs (crosslinked enzyme aggregates)
- Enzyme immobilization
- Mucor javanicus lipase
- SBA-15
ASJC Scopus subject areas
- Catalysis
- Materials Science(all)
Cite this
One-dimensional crosslinked enzyme aggregates in SBA-15 : Superior catalytic behavior to conventional enzyme immobilization. / Kim, Moon Il; Kim, Jungbae; Lee, Jinwoo; Shin, Sujeong; Na, Hyon Bin; Hyeon, Taeghwan; Park, Hyun Gyu; Chang, Ho Nam.
In: Microporous and Mesoporous Materials, Vol. 111, No. 1-3, 15.04.2008, p. 18-23.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - One-dimensional crosslinked enzyme aggregates in SBA-15
T2 - Superior catalytic behavior to conventional enzyme immobilization
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
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.
KW - α-Chymotrypsin
KW - CLEAs (crosslinked enzyme aggregates)
KW - Enzyme immobilization
KW - Mucor javanicus lipase
KW - SBA-15
UR - http://www.scopus.com/inward/record.url?scp=41649097552&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=41649097552&partnerID=8YFLogxK
U2 - 10.1016/j.micromeso.2007.07.009
DO - 10.1016/j.micromeso.2007.07.009
M3 - Article
AN - SCOPUS:41649097552
VL - 111
SP - 18
EP - 23
JO - Microporous and Mesoporous Materials
JF - Microporous and Mesoporous Materials
SN - 1387-1811
IS - 1-3
ER -