Modelling of L-DOPA oxidation catalyzed by laccase

Summary: Enzymatic oxidation of 3,4-dihydroxyphenyl-L-alanine (L-DOPA) with laccase from Trametes versicolor was investigated. The highest enzyme activity at pH 5.4 and at 25 ºC was found. The reaction kinetics and the effect of dissolved oxygen concentration on the reaction rate were evaluated. A m...

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Matična publikacija: Chemical and biochemical engineering quarterly
22 (2008), 3 ; str. 307-313, 384
Glavni autor: Tišma, Marina (-)
Ostali autori: Žnidaršič-Plazl, Polona (-), Plazl, Igor, Zelić, Bruno, Vasić-Rački, Đurđa
Vrsta građe: Članak
Jezik: eng
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Online pristup: CABEQ
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100 1 |a Tišma, Marina 
245 1 0 |a Modelling of L-DOPA oxidation catalyzed by laccase /  |c M. [Marina] Tišma, P. [Polona] Žnidaršič-Plazl, I. [Igor] Plazl, B. [Bruno] Zelić, Đ. [Đurđa] Vasić-Rački. 
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504 |a Sažetak 
520 8 |a Summary: Enzymatic oxidation of 3,4-dihydroxyphenyl-L-alanine (L-DOPA) with laccase from Trametes versicolor was investigated. The highest enzyme activity at pH 5.4 and at 25 ºC 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 predict the process of L-DOPA oxidation. Kinetic parameters, , and were 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 was established at a higher oxygen concentration in the inlet gas. The developed model was used to investigate the influence of dissolved oxygen concentration on L-DOPA conversion 
653 0 |a L-DOPA  |a Lakaza  |a Otopljeni kisik 
700 1 |a Žnidaršič-Plazl, Polona 
700 1 |a Plazl, Igor 
700 1 |a Zelić, Bruno 
700 1 |a Vasić-Rački, Đurđa 
773 0 |t Chemical and biochemical engineering quarterly  |x 0352-9568  |g 22 (2008), 3 ; str. 307-313, 384  |w nsk.(HR-ZaNSK)000004762 
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