Bicontinuous Nanoporous Frameworks: Caged Longevity for Enzymes

Angew Chem Int Ed Engl. 2016 Sep 12;55(38):11495-8. doi: 10.1002/anie.201605609. Epub 2016 Aug 11.

Abstract

The preparation of bicontinuous nanoporous covalent frameworks, which are promising for caging active enzymes, is demonstrated. The frameworks have three- dimensionally continuous, hydrophilic pores with widths varying between 5 and 30 nm. Enzymes were infiltrated into the bicontinuous pore by applying a pressured enzyme solution. The new materials and methods allowed the amount of caged proteins to be controlled precisely. The resulting enzyme-loaded framework films could be recycled many times with nearly no loss of catalytic activity. Entropic trapping of proteins by a bicontinuous pore with the right size distribution is an unprecedented strategy toward facile in vitro utilization of biocatalysts.

Keywords: bicontinuous nanoporous structures; enzyme nanoreactors; microfluidics; nanoporous films; organic sol-gel synthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocatalysis
  • Enzymes / chemistry*
  • Enzymes / metabolism
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism
  • Hydrophobic and Hydrophilic Interactions
  • Lipase / chemistry
  • Lipase / metabolism
  • Nanopores*
  • Oleic Acid / metabolism
  • Polyethylene Glycols / chemistry
  • Time Factors

Substances

  • Enzymes
  • Enzymes, Immobilized
  • Oleic Acid
  • Polyethylene Glycols
  • Lipase