Heated proteins are still active in a functionalized nanoporous support

Small. 2013 Jul 8;9(13):2228-32. doi: 10.1002/smll.201202409. Epub 2013 Feb 7.

Abstract

Even under heated conditions, the nearly native conformation and activity of a protein can be hoarded in a functionalized nanoporous support via non-covalent interaction. Surprisingly, the protein released from the heated protein-nanoporous composite can maintain its nearly native conformation and activity, while free proteins are permanently denatured under the same treatment.

Keywords: glucose oxidase; mesoporous silica; protein denaturation; protein release.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Glucose Oxidase / metabolism*
  • Hot Temperature*
  • Hydrogen-Ion Concentration
  • Nanopores* / ultrastructure
  • Porosity
  • Protein Conformation
  • Protein Denaturation*
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Silicon Dioxide / chemistry
  • Spectrometry, Fluorescence

Substances

  • Proteins
  • Silicon Dioxide
  • Glucose Oxidase