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

Research output: Contribution to journalArticlepeer-review

68 Citations (Scopus)


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 languageEnglish
Pages (from-to)18-23
Number of pages6
JournalMicroporous and Mesoporous Materials
Issue number1-3
Publication statusPublished - 2008 Apr 15
Externally publishedYes


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

ASJC Scopus subject areas

  • Chemistry(all)
  • Materials Science(all)
  • Condensed Matter Physics
  • Mechanics of Materials


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