Degradation of hydroxylated compounds using laccase and horseradish peroxidase immobilized on microporous polypropylene hollow fiber membranes

Moeder, Monika; Martin, C.; Koeller, G.

doi:10.1016/j.memsci.2004.07.024

Cited by 42 publications

(20 citation statements)

References 27 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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“…The substrate range for laccase is fairly wide, including several polyphenolic, aromatic amines, aminophenols and 4-methyl-3-hydroxyanthranilic acid [2][3][4] , and etc. Basically any substrate with characteristics similar to a p-diphenol would be oxidized by laccases.…”

Section: Introductionmentioning

confidence: 99%

“…Laccase has been successfully immobilized on many different types of carriers, such as glass beads, alginate beads, polyaniline matrix, microporous polypropylene hollow fiber membranes, activated carbon, chitosan film and magnetic chitosan microsphere, modified PVDF microfiltration membrane [2,[8][9][10] .…”

Section: Introductionmentioning

confidence: 99%

Preparation of magnetic chitosan nanoparticles and immobilization of laccase

Fang

Huang

Ding

et al. 2009

J. Wuhan Univ. Technol.-Mat. Sci. Edit.

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The magnetic chitosan nanoparticles were prepared by reversed-phase suspension method using Span-80 as an emulsifier, glutaraldehyde as cross-linking reagent. And the nanoparticles were characterized by TEM, FT-IR and hysteresis loop. The results show that the nanoparticles are spherical and almost superparamagnetic. The laccase was immobilized on nanoparticles by adsorption and subsequently by cross-linking with glutaraldehyde. The immobilization conditions and characterizations of the immobilized laccase were investigated. The optimal immobilization conditions were as follows: 10 mL of phosphate buffer (0.1 M, pH 7.0) containing 50 mg of magnetic chitosan nanoparticles, 1.0 mg·mL -1 of laccase and 1% (v/v) glutaraldehyde, immobilization temperature of 4 ℃ and immobilization time of 4 h. The immobilized laccase exhibited an appreciable catalytic capability (480 units·g -1 support) and had good storage stability and operation stability. The K m of immobilized and free laccase for ABTS were 140.6 and 31.1 μM in phosphate buffer (0.1 M, pH 3.0) at 37 ℃, respectively. The immobilized laccase is a good candidate for the research and development of biosensors based on laccase catalysis.

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“…For practical applications, the expensive enzymes must be recovered and reused after the reaction. This is the reasoning behind the well-established strategy of enzyme immobilization on solid supports, which has been applied to HRP [22][23][24][25][26]. HRP has been immobilized on chitosan powder [27], aluminum oxide [28], functionalized polyethylene [29], collagen [30], titanium oxide [31], carbon nanotubes [32], and other templates [22][23][24][25][26].…”

Section: Peroxidases In Polymer Synthesismentioning

confidence: 99%

Oxireductases in the Enzymatic Synthesis of Water-Soluble Conducting Polymers

Ochoteco

Mecerreyes

2010

Advances in Polymer Science

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This chapter reviews recent advances in the field of biocatalytic synthesis of water-soluble conducting polymers. Biocatalysis is proposed as a versatile tool for synthesis of conducting polymers. First, the enzymatic synthesis of conducting polymers and its mechanism is discussed as well as the use of different type of enzymes. Next, we describe the use of a new bifunctional template (sodium dodecyl diphenyloxide disulfonate) in the synthesis of polyaniline as a strategy to improve the water solubility and electrical conductivity in the obtained polymer. The recent development of enzyme-catalyzed polymerization of 3,4-ethylenedioxythiophene (EDOT) in the presence of polystyrenesulfonate is discussed. This method results in PEDOT materials that show an electrical conductivity of 2 × 10 −3 S cm −1 and posses excellent film formation ability, as confirmed by atomic force microscopy images. Finally, a simple method for immobilizing horseradish peroxidases in the biocatalytic synthesis of water-soluble conducting polymers is presented. This method is based on a biphasic catalytic system in which the enzyme is encapsulated inside the ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate, while other components remain in the aqueous phase. The enzyme is easily recovered after reaction and can be reused several times.

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Degradation of hydroxylated compounds using laccase and horseradish peroxidase immobilized on microporous polypropylene hollow fiber membranes

Cited by 42 publications

References 27 publications

Biodegradation of bisphenols with immobilized laccase or tyrosinase on polyacrylonitrile beads

Biodegradation of bisphenols with immobilized laccase or tyrosinase on polyacrylonitrile beads

Preparation of magnetic chitosan nanoparticles and immobilization of laccase

Oxireductases in the Enzymatic Synthesis of Water-Soluble Conducting Polymers

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