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Effect of immobilization on the specificity and stability of choline oxidase
Author(s) -
Fischel Adam H.,
Holton Kortnie,
Schmitz Jonathan M.,
Watkins Linette M.
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.796.5
Subject(s) - choline oxidase , choline , chemistry , oxidase test , sepharose , betaine , enzyme , biochemistry , glycine , substrate (aquarium) , chromatography , biology , amino acid , acetylcholinesterase , ecology
Choline oxidase is a versatile enzyme that has uses in both industrial and medicinal settings. Choline oxidase is able to act as a biosensor and detect the presence of choline, as well as being able to produce glycine betaine, which is used in various industrial settings. In order for choline oxidase to be feasible in industrial synthesis pathways, it must have a broad specificity while maintaining activity over a range of pH and temperature. To this end, the specificity for two different substrates, temperature stability, and pH stability of choline oxidase were all determined. Following this, choline oxidase was immobilized through two different methods, by attachment to CnBr‐activated Sepharose beads, and by binding to a Polyethersulfone (PES) membrane. When immobilized with Sepharose beads, the temperature and pH stability of choline oxidase increased, while reducing the enzymes specificity for choline as a substrate at the same time. Support or Funding Information This work was supported by the James Madison University Department of Chemistry and Biochemistry and the Huntsman Corporation This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .