Oxirane-immobilized Lentinula edodes laccase: stability and phenolics removal efficiency in olive mill wastewater

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

doi:10.1016/s0168-1656(99)00224-2

Cited by 151 publications

(71 citation statements)

References 33 publications

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“…Also, they could be used for decolorizing dye house effluents that are hardly decolorized by conventional sewage treatment plants [42,[211][212][213]. In addition to dye house effluents, laccases can decolorize waste waters from olive oil mills [214] and pulp mills [215,216] by removing colored phenolic compounds.…”

Section: Bioremediationmentioning

confidence: 99%

Laccases and Their Applications: A Patent Review

Kunamneni

Plou²,

Ballesteros³

et al. 2008

BIOT

276

172

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Abstract:Laccases are an interesting group of multi copper enzymes, which have received much attention of researchers in last decades due to their ability to oxidize both phenolic and non-phenolic lignin related compounds as well as highly recalcitrant environmental pollutants. This makes these biocatalysts very useful for their application in several biotechnological processes. Such applications include the detoxification of industrial effluents, mostly from the paper and pulp, textile and petrochemical industries, polymer synthesis, bioremediation of contaminated soils, wine and beverage stabilization. Laccases are also used as catalysts for the manufacture of anti-cancer drugs and even as ingredients in cosmetics. Recently, the utility of laccases has also been applied to nanobiotechnology. This paper reviews recent and important patents related to the properties, heterologous production, molecular cloning, and applications of laccases within different industrial fields as well as their potential extension to the nanobiotechnology area.

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Section: Bioremediationmentioning

confidence: 99%

Laccases and Their Applications: A Patent Review

Kunamneni

Plou²,

Ballesteros³

et al. 2008

BIOT

276

172

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“…Previously, between 70 and 98% of the protein immobilised and 67-96% of laccase activity, recovery was reported with different carrier materials [52][53][54]. Out of a number of different carrier materials previously tested for laccase immobilization such as activated carbon [55], Eupergit ® C [56], Sepharose [57], silica-based matrices [58] and porous glass [53,59] only alumina was used in this study as it seems to be more suitable for application in dye decolourization, due to its mechanical stability.…”

Section: Redyeingmentioning

confidence: 99%

An acid-stable laccase from Sclerotium rolfsii with potential for wool dye decolourization

Ryan

Schnitzhofer

Tzanov

et al. 2003

Enzyme and Microbial Technology

108

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The plant pathogen basidiomycete S. rolfsii secretes two laccases (SRL1 and SRL2) with molecular weights of 55 and 86 kDa, respectively. Laccase production was shown to be inducible by the addition of 2,5-xylidine to the cultural media. After treatment with a combination of chitinase and ␤-1,3-glucanase, two different laccases were isolated from the sclerotia depending on the stage of sclerotia development.The more prominent laccase, SRL1, was purified and found to decolourize the industrially important wool azo dye Diamond Black PV 200 without the addition of redox mediators. The enzyme (pI 5.2) was active in the acidic pH range, showing an optimal activity at pH 2.4, with ABTS as substrate. The optimum temperature for activity was determined to be 62 • C. Enzyme stability studies revealed that SRL1 was notably stable at 18 • C and pH 4.5, retaining almost full activity after a week. Oxidation of tyrosine was not detectable under the reaction conditions but the enzyme did oxidize a variety of the usual laccase substrates. SRL1 was strongly inhibited by sodium azide and fluoride. Dye solutions decolourized with the immobilized laccase were successfully used for redyeing.

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“…Laccase, covalently immobilised on various supports, has been evaluated for the treatment of pollutants such as phenols and dyes (D'Annibale et al 2000;Durán et al 2002;Kunamneni et al 2008;Russo et al 2008). However, to our knowledge, immobilised laccases on Eupergit supports have not yet been evaluated for the oxidative degradation of endocrine disruptor chemicals (EDCs), specifically, estrone, 17b-estradiol or 17a-ethinylestradiol.…”

Section: Introductionmentioning

confidence: 99%

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

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Laccase from Myceliophthora thermophila was covalently immobilised on Eupergit C and Eupergit C 250L yielding specific activities of up to 17 and 80 U/g, respectively. Due to its superior activity, Eupergit C 250L was chosen for further research. The somewhat lower catalytic efficiency (based on the ratio between the turnover number and the Michaelis constant, k cat /K M ) of the immobilised enzyme in comparison with that of the free enzyme was balanced by its increased stability and broader operational window related to temperature and pH. The feasibility of the immobilised laccase was tested by using a packed bed reactor (PBR) operating in consecutive cycles for the removal of Acid Green 27 dye as model substrate. High degrees of elimination were achieved (88, 79, 69 and 57% in 4 consecutive cycles), while the levels of adsorption on the support varied from 18 to 6%, proving that dye removal took place mainly due to the action of the enzyme. Finally, a continuous PBR with the solid biocatalyst was applied for the treatment of a solution containing the following endocrine disrupting chemicals: estrone (E1), 17b-estradiol (E2) and 17a-ethinylestradiol (EE2). At steady-state operation, E1 was degraded by 65% and E2 and EE2 were removed up to 80% and only limited adsorption of these compounds on the support, between 12 and 22%, was detected. In addition, a 79% decrease in estrogenic activity was detected in the effluent of the enzymatic reactor while only 14% was attained by inactivated laccase.

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Oxirane-immobilized Lentinula edodes laccase: stability and phenolics removal efficiency in olive mill wastewater

Cited by 151 publications

References 33 publications

Laccases and Their Applications: A Patent Review

Laccases and Their Applications: A Patent Review

An acid-stable laccase from Sclerotium rolfsii with potential for wool dye decolourization

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

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