Immobilized tyrosinase reactor for on-line HPLC application

Mushroom tyrosinase was covalently bonded with glutaraldehyde, as activating agent, to aminopropyl-controlled pore glass support by “in situ” immobilization technique. The Schiff's base double bond reduction with sodium cyanoborohydride was made as innovation. Catalytic activity and stability o...

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Bibliographic Details
Published in:Sensors and actuators. B, Chemical Chemical, 2007-02, Vol.121 (2), p.515-521
Main Authors: Girelli, Anna Maria, Mattei, Enrico, Messina, Antonella
Format: Article
Language:English
Subjects:
Bonding agents
Enzymes
Glass
HPLC
Immobilized enzyme
Kinetic parameters
Reactors
Reduction
Sodium
Solvents
Tyrosinase
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Description
Summary:Mushroom tyrosinase was covalently bonded with glutaraldehyde, as activating agent, to aminopropyl-controlled pore glass support by “in situ” immobilization technique. The Schiff's base double bond reduction with sodium cyanoborohydride was made as innovation. Catalytic activity and stability of the chromatographic reactor were evaluated using d,l-3,4-dihydroxyphenylalanine as substrate. The tyrosinase-IMER was characterized by investigation of various parameters influencing the enzymatic activity (pH, temperature, ionic strength and organic solvents). In addition kinetic measurements showed that, by removal of the external diffusional limitation, the enzyme selectivity towards substrate was improved whereas the activity was comparable with respect to that of free enzyme.
ISSN:0925-4005
1873-3077
DOI:10.1016/j.snb.2006.04.076