섬유

immobilization of acetylcholinesterase on solid surfaces' chemistry and activity studies (for biosensor technology)

  • 출판일1999.03
  • 저자
  • 서지사항
  • 등록일 2016.11.02
  • 조회수 432
a method for covalent attachment of the enzyme acetylcholinesterase on two different solid surfaces (glass and platinum) is described. the chemistry includes covalent bond formation between a hydroxyl group on the surface, a thiol-terminal silane, a heterobifunctional crosslinker, and the enzyme. the activity of the immobilized enzyme has been determined spectrophotometrically using two different substrates, acetylcholine and butyrylthiocholine. it is determined that after immobilization, acetylcholinesterase retains at least 50 percent of its activity on glass and 15 percent of its activity on platinum surfaces when assayed using butyrylthiocholine as a substrate. the general procedure described for the immobilization of enzymes should find broad use in the fabrication of enzyme electrodes and in biosensor technology
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