Immobilized tyrosinase reactor for on-line HPLC application. Development and characterization

Anna Maria Girelli; Enrico Mattei; Antonella Messina

doi:10.1016/j.snb.2006.04.076

Immobilized tyrosinase reactor for on-line HPLC application. Development and characterization

Anna Maria Girelli, Enrico Mattei, Antonella Messina

Fondazione IRCCS Istituto Nazionale dei Tumori

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	515-521
Number of pages	7
Journal	Sensors and Actuators, B: Chemical
Volume	121
Issue number	2
DOIs	https://doi.org/10.1016/j.snb.2006.04.076
Publication status	Published - Feb 20 2007

Keywords

HPLC
Immobilized enzyme
Kinetic parameters
Tyrosinase

ASJC Scopus subject areas

Analytical Chemistry
Electrochemistry
Electrical and Electronic Engineering

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abstract = "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.",

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T1 - Immobilized tyrosinase reactor for on-line HPLC application. Development and characterization

AU - Girelli, Anna Maria

AU - Mattei, Enrico

AU - Messina, Antonella

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Y1 - 2007/2/20

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AB - 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.

KW - HPLC

KW - Immobilized enzyme

KW - Kinetic parameters

KW - Tyrosinase

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Immobilized tyrosinase reactor for on-line HPLC application. Development and characterization

Abstract

Keywords

ASJC Scopus subject areas

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