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

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Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: A simple and effective method for enzyme stabilization

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Title
Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: A simple and effective method for enzyme stabilization
Other Titles
Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: A simple and effective method for enzyme stabilization
Author
Kim, Moon IlKim, JungbaeLee, JinwooJia, HongfeiBin Na, HyonYoun, Jong KyuKwak, Ja HunDohnalkova, AliceGrate, Jay W.Wang, PingHyeon, TaeghwanPark, Hyun GyuChang, Ho Nam
Keywords
IMMOBILIZATION; CATALYTIC ACTIVITY;  PROTEINS;  ACYLASE;  ENCAPSULATION;  BIOCATALYSIS;  CHYMOTRYPSIN;  CRYSTALS;  SUPPORT;  FOAMS
Issue Date
2007-02
Publisher
WILEY-BLACKWELL
Citation
BIOTECHNOLOGY AND BIOENGINEERING, v.96, no.2, pp.210 - 218
Abstract
alpha-chymotrypsin (CT) and lipase (LP) were immobilized in hierarchically-ordered mesocellular mesoporous silica (HMMS) in a simple but effective way for the enzyme stabilization, which was achieved by the enzyme adsorption followed by glutaraldehyde (GA) cross-linking. This resulted in the formation of nanometer scale crosslinked enzyme aggregates (CLEAs) entrapped in the mesocellular pores of HMMS (37 nm), which did not leach out of HMMS through narrow mesoporous channels (13 nm). CLEA of alpha-chymotrypsin (CLEA-CT) in HMMS showed a high enzyme loading capacity and significantly increased enzyme stability. No activity decrease of CLEA-CT was observed for 2 weeks under even rigorously shaking condition, while adsorbed CT in HMMS and free CT showed a rapid inactivation due to the enzyme leaching and presumably autolysis, respectively. With the CLEA-CT in HMMS, however, there was no tryptic digestion observed suggesting that the CLEA-CT is not susceptible to autolysis. Moreover, CLEA of lipase (CLEA-LP) in HMMS retained 30% specific activity of free lipase with greatly enhanced stability. This work demonstrates that HMMS can be efficiently employed as host materials for enzyme immobilization leading to highly enhanced stability of the immobilized enzymes with high enzyme loading and activity
URI
https://scholarworks.unist.ac.kr/handle/201301/12137
DOI
10.1002/bit.21107
ISSN
0006-3592
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ECHE_Journal Papers
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