Effects of the immobilization supports on the catalytic properties of immobilized mushroom tyrosinase: A comparative study using several substrates

Marín-Zamora, María Elisa; Rojas-Melgarejo, Francisco; Garcı́a-Cánovas, Francisco; Garcı́a-Ruiz, Pedro Antonio

doi:10.1016/j.jbiotec.2007.05.004

Cited by 30 publications

(18 citation statements)

References 35 publications

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“…There are many studies on the application of phenoloxidases immobilized on porous glass beads (Marin-Zamora et al 2007), chitosan beads (D'Annibale et al 1999;Ispas et al 2010;Tamura et al 2010;Zhang et al 2008), polymeric membranes (Georgieva et al 2008;Lante et al 2000;Moeder et al 2004;Rasera et al 2009) and cross-linked as aggregates (CLEAs) or on silica nanoparticles (Cabana et al 2009;Galliker et al 2010). We also employed the immobilized laccase for the bioremediation of waters polluted by phenol compounds, such as cathecol (Durante et al 2004), syringic acid (Attanasio et al 2005), BPA (Diano et al 2007) and phthalates (Mita et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Biodegradation of bisphenols with immobilized laccase or tyrosinase on polyacrylonitrile beads

et al. 2010

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The biodegradation of waters polluted by some bisphenols, endowed with endocrine activity, has been studied by means of laccase or tyrosinase immobilized on polyacrylonitrile (PAN) beads. Bisphenol A (BPA), Bisphenol B (BPB), Bisphenol F (BPF) and Tetrachlorobisphenol A (TCBPA) have been used. The laccase-PAN beads system has been characterized as a function of pH, temperature and substrate concentration. The biochemical parameters so obtained have been compared with those of the free enzyme to evidence the modification induced by the immobilization process. Once characterized, the laccase-PAN beads have been employed in a fluidized bed reactor to determine for each of the four bisphenols the degradation rate constant (k); the τ(50), i.e., the time to obtain the 50% of degradation, and the removal efficiency (RE(90)) after 90 min of enzyme treatment. The same parameters have been measured for each of the four pollutants with the same fluidized bed bioreactor loaded with tyrosinase-PAN beads. The internal comparison, i.e., in each of the two catalytic systems, has shown that both enzymes exhibit a removal efficiency in the following order BPF>BPA>BPB>TCBPA. The external comparison, i.e., the comparison between the two catalytic system, has shown that the catalytic power of laccase were higher than that of tyrosinase. The operational stability of both catalytic systems resulted excellent, since they maintained more than 80% of the initial activity after 30 days of work.

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Section: Introductionmentioning

confidence: 99%

Biodegradation of bisphenols with immobilized laccase or tyrosinase on polyacrylonitrile beads

et al. 2010

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“…Among them, laccases (EC 1.10.3.2) are multi-copper oxidase proteins that use molecular oxygen to oxidize various aromatic and non-aromatic compounds by a radical-catalyzed reaction mechanism [4][5][6]. Because of their broad specificity for the reducing substrates, laccases from white-rot fungi are receiving increasing attention as potential industrial enzymes in various applications, such as in chemical or medicinal synthesis, biobleaching, dye decolorization, wastewater treatment and/or soil remediation [7][8][9][10]. On the other hand, the use of these enzymes for practical applications, mainly as agents for environmental cleanup purposes, is still limited due to several reasons.…”

Section: Introductionmentioning

confidence: 99%

Preparation and characterization of epoxy-functionalized magnetic chitosan beads: laccase immobilized for degradation of reactive dyes

Bayramoğlu

Yılmaz

Arıca

2009

Bioprocess Biosyst Eng

112

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Cross-linked magnetic chitosan beads were prepared by phase-inversion technique in the presence of epichlorohydrin under alkaline condition, and used for covalent immobilization of laccase. The activity of the immobilized laccase on the magnetic chitosan was about 260 U (g/dry beads) with an enzyme loading of about 16.33 +/- 0.39 mg [(g/dry beads) mg/g]. Kinetic parameters, V (max) and K (m) values were determined as 21.7 U/mg protein and 9.4 microM for free enzyme, and 15.6 U/mg protein and 19.7 microM for the immobilized laccase, respectively. The operational and thermal stabilities of the immobilized laccase were improved compared to free counterpart. The immobilized laccase was operated in a batch reactor for the decolorization of reactive dyes from aqueous solution. The laccase immobilized on magnetic chitosan beads was very effective for removal of textile dyes from aqueous solution which creates an important environmental problem in the discharged textile dying solutions.

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“…The increase of the enzyme affinity toward the substrate probably due to the absorption of sucrose by the beads that it actually increases sucrose concentration in the locality of the binding sites of enzyme compared to free enzyme in bulk solution. Marín-Zamora et al [26], also recorded the same observation. Their K app m values for immobilized tyrosinase were much lower than the published value for the free enzyme.…”

Section: Kinetics Parameters Of Immobilized Enzymementioning

confidence: 55%

“…This phenomenon is also observed in invertase immobilized on nylon-6 microbeads [27], invertase immobilized in PVA hydrogel [28], and the adsorption of invertase on poly(acrylamide/maleic acid) hydrogel [29]. The value of maximum steady-state rate (V app max ) could also be directly affected by enzyme-support affinity [26]. This simply means an increase in V app max would be observed if the enzymesupport affinity is stronger as more enzyme could be immobilized.…”

Section: Kinetics Parameters Of Immobilized Enzymementioning

confidence: 80%

Hydrolysis of liquid pineapple waste by invertase immobilized in PVA–alginate matrix

Zain

Suardi

Idris

2010

Biochemical Engineering Journal

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Effects of the immobilization supports on the catalytic properties of immobilized mushroom tyrosinase: A comparative study using several substrates

Cited by 30 publications

References 35 publications

Biodegradation of bisphenols with immobilized laccase or tyrosinase on polyacrylonitrile beads

Biodegradation of bisphenols with immobilized laccase or tyrosinase on polyacrylonitrile beads

Preparation and characterization of epoxy-functionalized magnetic chitosan beads: laccase immobilized for degradation of reactive dyes

Hydrolysis of liquid pineapple waste by invertase immobilized in PVA–alginate matrix

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