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Modelling of L-DOPA oxidation catalyzed by laccase (CROSBI ID 134217)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Tišma, Marina ; Žnidaršič-Plazl, Polona ; Plazl, Igor ; Zelić, Bruno ; Vasić-Rački, Đurđa Modelling of L-DOPA oxidation catalyzed by laccase // Chemical and biochemical engineering quarterly, 22 (2008), 3; 307-313

Podaci o odgovornosti

Tišma, Marina ; Žnidaršič-Plazl, Polona ; Plazl, Igor ; Zelić, Bruno ; Vasić-Rački, Đurđa

engleski

Modelling of L-DOPA oxidation catalyzed by laccase

The enzymatic oxidation of 3, 4-dihydroxyphenyl-L-alanine (L-DOPA) with laccase from Trametes versicolor has been investigated. The highest enzyme activity at pH 5.4 and at 25 º C was found. The reaction kinetics and the effect of dissolved oxygen concentration on the reaction rate were evaluated. A mathematical model, comprised of double-substrate Michealis-Menten kinetics and mass balances for L-DOPA and dissolved oxygen concentrations was developed in order to describe and to predict the process of L-DOPA oxidation. Kinetic parameters, Vm, Km(L-DOPA) and Km(O2) have been estimated and experimentally verified by a set of experiments with constant additional aeration for different initial concentrations of L-DOPA and dissolved oxygen. A significant increase in reaction rate at higher oxygen concentration in the inlet gas has been established. Using the developed model the influence of dissolved oxygen concentration on L-DOPA conversion was investigated.

L-DOPA; laccase; enzymatic oxidation; modelling

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Podaci o izdanju

22 (3)

2008.

307-313

objavljeno

0352-9568

Povezanost rada

Biotehnologija

Indeksiranost