Immobilization of tyrosinase on chitosan–clay composite beads

Dinçer, Ayşe; Becerik, Seda; Aydemir, Tülin

doi:10.1016/j.ijbiomac.2011.11.020

Cited by 100 publications

(46 citation statements)

References 36 publications

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“…Thus, lignin and tyrosinase cooperate in synergy to realize efficient oxidative processes. Tyrosinase has been widely studied because of its relevance in several applied areas [ 24 , 25 ], showing better performances in industrial applications when used in the immobilized form, as a consequence of its reusability, enhanced stability, and easier purification procedures [ 26 ]. In recent years, we described the preparation of heterogeneous catalysts for the synthesis of bioactive catechol derivatives by the immobilization of tyrosinase on microcapsules of the epoxy resin Eupergit [ 27 , 28 ], and as an alternative, by Layer-by-layer coating of the enzyme on Multi Walled Carbon Nanotubes (MWCNTs) [ 29 ].…”

Section: Introductionmentioning

confidence: 99%

Functionalized Tyrosinase-Lignin Nanoparticles as Sustainable Catalysts for the Oxidation of Phenols

et al. 2018

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Sustainable catalysts for the oxidation of phenol derivatives under environmentally friendly conditions were prepared by the functionalization of lignin nanoparticles with tyrosinase. Lignin, the most abundant polyphenol in nature, is the main byproduct in the pulp and paper manufacturing industry and biorefinery. Tyrosinase has been immobilized by direct adsorption, encapsulation, and layer-by-layer deposition, with or without glutaraldehyde reticulation. Lignin nanoparticles were found to be stable to the tyrosinase activity. After the enzyme immobilization, they showed a moderate to high catalytic effect in the synthesis of catechol derivatives, with the efficacy of the catalyst being dependent on the specific immobilization procedures.

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Section: Introductionmentioning

confidence: 99%

Functionalized Tyrosinase-Lignin Nanoparticles as Sustainable Catalysts for the Oxidation of Phenols

et al. 2018

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“…Entrapping enzymes within a matrix including gels, polymers, or inks is one approach for immobilization that does not compromise stability and biological activity. Chitosan, a natural biopolymer, is commonly used for enzyme immobilization, and shows excellent film-forming ability and biocompatibility [34,35]. Furthermore, chitosan-reduced graphene oxide (rGO) nanocomposites have proven to be highly effective in enhancing mechanical and electric properties [36][37][38][39], offering better mechanical and electrical stability.…”

Section: Introductionmentioning

confidence: 99%

Tyrosinase/Chitosan/Reduced Graphene Oxide Modified Screen-Printed Carbon Electrode for Sensitive and Interference-Free Detection of Dopamine

et al. 2019

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Featured Application: This biosensor was used for the detection of dopamine without interference from high concentrations (0.5 mM) of ascorbic acid. In addition, the electrode developed in this study presented a great sensitivity (22 nM) and a broad linear range compared with existing electrochemical sensors in the detection of dopamine. Moreover, the analysis of dopamine in physiological samples was examined.Abstract: Tyrosinase, chitosan, and reduced graphene oxide (rGO) are sequentially used to modify a screen-printed carbon electrode (SPCE) for the detection of dopamine (DA), without interference from uric acid (UA) or ascorbic acid (AA). The use of tyrosinase significantly improves the detection's specificity. Cyclic voltammetry (CV) measurements demonstrate the high sensitivity and selectivity of the proposed electrochemical sensors, with detection limits of 22 nM and broad linear ranges of 0.4-8 µM and 40-500 µM. The fabricated tyrosinase/chitosan/rGO/SPCE electrodes achieve satisfactory results when applied to human urine samples, thereby demonstrating their feasibility for analyzing DA in physiological samples.

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“…However, chitosan matrix is not rigid enough and can easily be dissociated by vigorous stirring during continuous use, hampering the application of immobilized enzymes on chitosan carriers in industrial manufacture [14]. To improve the strength and stability of chitosan support, some inorganic mechanical materials with high strengths have been mixed with chitosan to prepare composite materials, achieving obvious progresses in the stability and reusability of immobilized enzymes, compared with those on chitosan support [19][20][21][22]. Multiwalled carbon nanotube was mixed with chitosan to prepare an ideal composite carrier for β-glucosidase immobilization, improving its pH and storage stability and allowing its continuous use [20].…”

Section: Introductionmentioning

confidence: 99%

Improved Catalytic Performance of Lipase Supported on Clay/Chitosan Composite Beads

Shou

Dong

et al. 2017

Catalysts

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Clay/chitosan composite beads were prepared and used as the carrier to support lipase by adsorption, to improve the activity and stability of lipase in the hydrolysis of olive oil. Under conditions of pH 6.0, 25 • C and adsorption for 10 h, immobilized lipases on chitosan bead (CB-lipase) and three clay/chitosan composite beads, at different clay to chitosan proportions of 1:8 (CCB-8-lipase), 1:5 (CCB-5-lipase) and 1:3 (CCB-3-lipase), were prepared. By comparing the activity of these immobilized lipases, CCB-5-lipase showed the highest activity, followed by CCB-8-lipase > CCB-3-lipase > CB-lipase; this improvement was attributed to the synergetic effect of enrichment of olive oil by clay at the reaction surface and better biocompatibility of chitosan with lipase molecules. The optimum pH and temperature in the reaction respectively changed from 7.0 and 30 • C for free lipase to 7.5 and 35 • C for immobilized forms. Furthermore, the thermal stability and repeated usability of these immobilized lipases were sequenced as CCB-3-lipase > CCB-5-lipase > CCB-8-lipase > CB-lipase, due to greater rigidity of immobilized lipase with the addition of clay, which was further confirmed by SEM. The study shows that the incorporation of clay with chitosan creates a good synergetic effect to improve the catalytic performance of immobilized lipase on clay/chitosan composite.

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Immobilization of tyrosinase on chitosan–clay composite beads

Cited by 100 publications

References 36 publications

Functionalized Tyrosinase-Lignin Nanoparticles as Sustainable Catalysts for the Oxidation of Phenols

Functionalized Tyrosinase-Lignin Nanoparticles as Sustainable Catalysts for the Oxidation of Phenols

Tyrosinase/Chitosan/Reduced Graphene Oxide Modified Screen-Printed Carbon Electrode for Sensitive and Interference-Free Detection of Dopamine

Improved Catalytic Performance of Lipase Supported on Clay/Chitosan Composite Beads

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