ENZYMATIC ACTIVITY OF UREASE IMMOBILIZED ON AMINO-FUNCTIONALIZED SILICA, TUNGSTEN AND TEFLON SURFACES EITHER DIRECTLY OR THROUGH PHOSPHOLIPID MATRICES

Authors
  1. Kallury, K.M.R.
  2. Thompson, M.
Corporate Authors
Defence Research Establishment Suffield, Ralston ALTA (CAN);Toronto Univ, Toronto ONT (CAN) Dept of Chemistry
Abstract
Amino-functionalized silica, tungsten/tungsten oxide and modified teflon surfaces were prepared by silanizing these hydroxylic supportswith N-(11-trifluoroacetamidoundecanoyl)-aminopropyltriethoxysilane and then removing the trifluoroacetyl protective group under mildly basic conditions. Urease was directly immobilized on these aminated solidsupports through the carboxylic moieties on the enzyme in the presence of a carbodiimide coupling agent. One of the aminated supports, viz,silica, was also reacted with urease in the presence of cyanuric chloride and phthaloyl chloride cross-linkers utilizing the epsilon-amino groups of the lysine residues on the enzyme. The attachment of urease to the aminated supports through a phospholipid cross-linker was accomplished by a five-step synthetic sequence. All the surfaces prepared were characterized by FTIR and XPS. In addition, the silica-based surfaces were also characterized by solid-state 13C-NMR. TRUNCATED
Report Number
DRES-CR-48-92 — Contract Report
Date of publication
15 May 1992
Number of Pages
51
DSTKIM No
93-00018
CANDIS No
127283
Format(s):
Hardcopy;Originator's fiche received by DSIS

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