Characterization of immobilized laccase from Lentinula edodes and its use in olive-mill wastewater treatment

D’Annibale, Alessandro; Stazi, Silvia Rita; Vinciguerra, Vittorio; Mattia, Elena Di; Sermanni, Giovanni Giovannozzi

doi:10.1016/s0032-9592(98)00144-7

Cited by 143 publications

(60 citation statements)

References 39 publications

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“…The two activity peaks detected suggest the presence of an isozyme or indicate that this laccase presents two distinct pH optima, like observed in Agaricus bisporus (32) and Monocillium saxena (28). No laccase activity was detected at pH values higher than 6.5, which is in agreement with findings for other fungal species, such as L. edodes (5,33). The Km app was 101.6 µM and Vmax app was 0.84 µM.s -1 .…”

supporting

confidence: 86%

Laccase production by Lepista sordida

Cavallazzi¹,

Oliveira²,

Kasuya³

2004

Braz. J. Microbiol.

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supporting

confidence: 86%

Laccase production by Lepista sordida

Cavallazzi¹,

Oliveira²,

Kasuya³

2004

Braz. J. Microbiol.

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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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“…The amino groups of chitosan are nucleophilic and reactive at higher pHs, allowing chitosan to be cross-linked under mild conditions to create gel matrixes of various shapes and sizes including beads, membranes, and fibers. Several enzymes such as tyrosinase, HRP, catalase, laccase, and urease have been immobilized on a matrix containing chitosan by the sol-gel method [37,38,96,[98][99][100].…”

Section: Immobilization On Organic Supportsmentioning

confidence: 99%