Laccase kinetic properties

Laccase, 36 318, 329, 40 122 see also Blue copper oxidases amino-acid sequences, 40 141 anaerobic reduction, 40 158-160 biological function, 40 124 electrochemistry, 36 360 fungal, 40 145-152 evolution, 40 153-154 inhibition, 40 162 kinetic properties, 40 157-162 molecular and spectroscopic properties, 40 125-126... 

As previously mentioned, laccase is very closely related to ascorbate oxidase. The principal molecular architecture and arrangement of the mononuclear and trinuclear copper centers are the same. Furthermore, spectroscopic and kinetic properties are similar in many circumstances. Therefore, the catalytic mechanism of the dioxygen reduction should be the same for both. Kinetic studies on fungal and tree laccases have been... 

Mathematical modeling of biosensors has been successfully used to investigate the kinetic peculiarities of the biosensor action. The numerical simulation became a powerful framework for numerical investigation of the impact of model parameters on the biosensor action and to optimize the biosensor configuration [7]. Recently, the computational modeling of the laccase-based biosensor qualitatively explained and confirmed the experimentally observed synergistic effect of the mediator on the biosensor response [21]. The numerical simulation of an amperometric biosensor based on an enzyme-loaded carbon nanotube (CNT) layer deposited on a perforated membrane highlighted the dependence of the steady-state biosensor current on the anisotropic properties of CNT. It was also shown that the sensitivity of the biosensors... 

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