Correlation Engine 2.0
Clear Search sequence regions

  • behavior (1)
  • biosensor (3)
  • brevibacterium (1)
  • catalysis (1)
  • cholesterol (5)
  • ChOx (5)
  • electron transfer (1)
  • factors (2)
  • fad (5)
  • flavin (3)
  • ionic liquid (8)
  • native (1)
  • reagent (1)
  • Sizes of these terms reflect their relevance to your search.

    The influence of several factors on the activity of cholesterol oxidase (ChOx) transiently exposed to a room temperature ionic liquid (RTIL) was studied. Presence of flavin adenine dinucleotide (FAD, prosthetic group of ChOx) during exposure to RTIL makes the procedure enzyme-friendly, while the use of RTIL (green reagent) makes it environmentally-friendly. Following exposure to RTIL and its subsequent removal, FAD becomes part of the molecular structure of the refolded protein (a molecular "wire"). This makes the procedure used here a molecular one. The factors studied were: FAD presence in RTIL during modification, water presence during exposure to RTIL, and ratio FAD:RTIL during "wiring". Performance parameters monitored were: enzyme activity before and after "wiring" (expressed as (dA/dt)/mg enzyme, and measured spectrophotometrically), peak current in an amperometric biosensor for cholesterol detection, and linearity of the biosensor response depending on cholesterol concentration. After RTIL removal, the modified enzyme (ME) retained a high percentage of the added FAD, which supplemented that of the native enzyme (functioning as a "wire" and enhancing electron transfer kinetics), and a fraction of the initial activity. Used in an amperometric biosensor, ME showed catalytic activity, linear behavior as a function of cholesterol concentration, and stability.


    Mihaela D Leonida, Benedict Aurian-Blajeni. Molecularly "wired" cholesterol oxidase for biosensing. The protein journal. 2015 Feb;34(1):68-72

    Expand section icon Mesh Tags

    Expand section icon Substances

    PMID: 25579496

    View Full Text