Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica

A simple and effective method for enzyme stabilization

Il Kim Moon, Jungbae Kim, Jinwoo Lee, Hongfei Jia, Bin Na Hyon, Kyu Youn Jong, Hun Kwak Ja, Alice Dohnalkova, Jay W. Grate, Ping Wang, Taeghwan Hyeon, Gyu Park Hyun, Nam Chang Ho

Research output: Contribution to journalArticle

152 Citations (Scopus)

Abstract

α-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 α-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.

Original languageEnglish
Pages (from-to)210-218
Number of pages9
JournalBiotechnology and Bioengineering
Volume96
Issue number2
DOIs
Publication statusPublished - 2007 Feb 1
Externally publishedYes

Fingerprint

Silicon Dioxide
Enzymes
Stabilization
Silica
Chymotrypsin
Lipases
Lipase
Autolysis
Catalyst activity
Enzyme immobilization
Enzyme Stability
Immobilized Enzymes
Glutaral
Immobilization
Leaching
Adsorption
Digestion

Keywords

  • α-chymotrypsin
  • CLEAs (crosslinked enzyme aggregates)
  • Enzyme immobi
  • HMMS (hierarchically-ordered mesocellular mesoporous silica)
  • Lization
  • Mucor javanitus lipase

ASJC Scopus subject areas

  • Biotechnology
  • Microbiology

Cite this

Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica : A simple and effective method for enzyme stabilization. / Moon, Il Kim; Kim, Jungbae; Lee, Jinwoo; Jia, Hongfei; Hyon, Bin Na; Jong, Kyu Youn; Ja, Hun Kwak; Dohnalkova, Alice; Grate, Jay W.; Wang, Ping; Hyeon, Taeghwan; Hyun, Gyu Park; Ho, Nam Chang.

In: Biotechnology and Bioengineering, Vol. 96, No. 2, 01.02.2007, p. 210-218.

Research output: Contribution to journalArticle

Moon, IK, Kim, J, Lee, J, Jia, H, Hyon, BN, Jong, KY, Ja, HK, Dohnalkova, A, Grate, JW, Wang, P, Hyeon, T, Hyun, GP & Ho, NC 2007, 'Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: A simple and effective method for enzyme stabilization', Biotechnology and Bioengineering, vol. 96, no. 2, pp. 210-218. https://doi.org/10.1002/bit.21107
Moon, Il Kim ; Kim, Jungbae ; Lee, Jinwoo ; Jia, Hongfei ; Hyon, Bin Na ; Jong, Kyu Youn ; Ja, Hun Kwak ; Dohnalkova, Alice ; Grate, Jay W. ; Wang, Ping ; Hyeon, Taeghwan ; Hyun, Gyu Park ; Ho, Nam Chang. / Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica : A simple and effective method for enzyme stabilization. In: Biotechnology and Bioengineering. 2007 ; Vol. 96, No. 2. pp. 210-218.
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