Reaction kinetics for laccase-catalyzed polymerization of 1-naphthol

Aktaş, Nahit; Çiçek, H.; Ünal, Arzu; Ki̇barer, Günay; Kolankaya, Nazif; Tanyolaç, Abdurrahman

doi:10.1016/s0960-8524(01)00063-3

Cited by 58 publications

(17 citation statements)

References 19 publications

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“…Among different possible laccase inducers known from the literature [24][25][26][27][28][29][30][31][32] ethanol, alkali lignin, guaiacol, veratryl alcohol, and eugenol were selected for the present study. Maximal activities obtained within 17 days of T. versicolor submerged cultivation in synthetic media containing various inducers are listed in Table 2.…”

Section: Effect Of Various Inducers On Laccase Productionmentioning

confidence: 99%

Optimization of Laccase Production by Trametes versicolor Cultivated on Industrial Waste

Tišma

Žnidaršič–Plazl

Vasić-Rački

et al. 2011

Appl Biochem Biotechnol

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Laccases are very interesting biocatalysts for several industrial applications. Its production by different white-rot fungi can be stimulated by a variety of inducing substrates, and the use of lignocellulosic wastes or industrial by-products is one of the possible approaches to reduce production costs. In this work, various industrial wastes were tested for laccase production by Trametes versicolor MZKI G-99. Solid waste from chemomechanical treatment facility of a paper manufacturing plant showed the highest potential for laccase production. Enzyme production during submerged cultivation of T. versicolor on the chosen industrial waste has been further improved by medium optimization using genetic algorithm. Concentrations of five components in the medium were optimized within 60 shake-flasks experiments, where the highest laccase activity of 2,378 U dm(-3) was achieved. Waste from the paper industry containing microparticles of CaCO(3) was found to stimulate the formation of freely dispersed mycelium and laccase production during submerged cultivation of T. versicolor. It was proven to be a safe and inexpensive substrate for commercial production of laccase and might be more widely applicable for metabolite production by filamentous fungi.

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Section: Effect Of Various Inducers On Laccase Productionmentioning

confidence: 99%

Optimization of Laccase Production by Trametes versicolor Cultivated on Industrial Waste

Tišma

Žnidaršič–Plazl

Vasić-Rački

et al. 2011

Appl Biochem Biotechnol

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“…[20] The main drawback of these biotransformations is the extensive polymerization that may arise from the radical mechanism of the oxidative process, producing quite often a complex mixture of polyphenolic oligomers. [21] As a part of our general interest in biocatalysis [22] and, more specifically, in the enzyme-catalyzed carbon-carbon bond formation, [23] we have started an investigation on the synthetic exploitation of laccases for the oxidative dimerization of phenolic derivatives such as tetrahydronaphthol, [24] estradiol, [25] and, more recently, totarol. [26] The preparative-scale oxidation of resveratrol was also one of our synthetic goals, and a couple of years ago we described the laccase-catalyzed dimerization of 1: under the best reaction conditions, the dehydrodimer 2 was isolated in 31 % yields; we have also shown that the laccase-mediated oxidation of 1 took place at the para 4'-OH.…”

Section: Trans-resveratrolmentioning

confidence: 99%

Laccase‐Catalyzed Dimerization of Hydroxystilbenes

et al. 2007

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A series of hydroxystilbenes, analogues of the bioactive phytoalexin resveratrol, were synthesized and submitted to the catalytic action of a laccase from Trametes pubescens in a biphasic system made of ethyl acetate and acetate buffer. Oxidation took place at the 4'-hydroxy (4-hydroxy) position of the hydroxystilbenic moieties, followed by radicalradical coupling dimerization reactions. Most of the products were isolated in good yields and fully characterized. Depending on the substrates, three different dimeric products could be identified, the main products usually being 4-O-a-ß-5 (dihydrofuran-like) dimers.

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“…b Kinetic parameters for laccase from T. versicolor at pH 5.0, 258C with substrate 1-naphtol at a dissolved oxygen concentration of 20.3 mg/L (Aktas et al, 2001).…”

Section: Resultsmentioning

confidence: 99%

Metabolic control analysis of an enzymatic biofuel cell

Glykys

Banta

2008

Biotech & Bioengineering

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Metabolic control analysis (MCA) is an analytical technique that aims to quantify the distribution of control that enzymes exhibit over the steady-state fluxes through a metabolic network. In an enzymatic biofuel cell, the flux of interest is the electrical current generated by the system. Regardless of transport limitations and other constraints, kinetic limitations can become potential bottlenecks in the operation of a biofuel cell. We have used an indirect approach to MCA to investigate a common osmium-mediated glucose oxidase/laccase enzymatic biofuel cell. The results of the analysis show that the control of the electron flux strongly depends on the total mediator concentrations and the extent of polarization of the individual electrodes. The effect of varying oxygen concentrations is also examined, as oxygen is required for the cathode, but it participates in a non-productive reaction at the anode. Under normal operating conditions the electrodes will be highly polarized and will both contain high mediator concentrations. This configuration will result in a dominant FCC at the anode, and the conditions that are needed for balanced flux control between the anode and cathode are explored. As increasingly complex bioelectrocatalytic systems and architectures are envisioned, MCA will be a valuable framework to facilitate their design and subsequent operation.

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Reaction kinetics for laccase-catalyzed polymerization of 1-naphthol

Cited by 58 publications

References 19 publications

Optimization of Laccase Production by Trametes versicolor Cultivated on Industrial Waste

Optimization of Laccase Production by Trametes versicolor Cultivated on Industrial Waste

Laccase‐Catalyzed Dimerization of Hydroxystilbenes

Metabolic control analysis of an enzymatic biofuel cell

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