Alteration of enzyme activity and enantioselectivity by biomimetic encapsulation in silica particles

Chem Commun (Camb). 2012 Jan 30;48(9):1314-6. doi: 10.1039/c1cc14478b. Epub 2011 Dec 12.

Abstract

Direct encapsulation of esterase or lipase fused with the silica-precipitating R5 peptide from Cylindrotheca fusiformis in silica particles afforded high yields of active entrapped protein. The hydrolytic activity of both enzymes against p-nitrophenyl butyrate was similarly affected by encapsulation and the enantioselectivity of the esterase was both improved and inverted.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biomimetic Materials / chemistry
  • Biomimetics
  • Chemical Precipitation
  • Diatoms / chemistry
  • Diatoms / enzymology*
  • Enzyme Activation
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism*
  • Esterases / chemistry
  • Esterases / metabolism*
  • Lipase / chemistry
  • Lipase / metabolism*
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Silicon Dioxide / chemistry*

Substances

  • Enzymes, Immobilized
  • Peptides
  • Silicon Dioxide
  • Esterases
  • Lipase