Comparative studies on immobilized laccase behaviour in packed-bed and batch reactors

Rekuć, Adriana; Jastrzembska, Bogna; Liesienė, Jolanta; Bryjak, Jolanta

doi:10.1016/j.molcatb.2008.09.007

Cited by 37 publications

(17 citation statements)

References 30 publications

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“…In our study, E1, E2 and EE2 were degraded for the first time by Myceliophthora thermophila laccase immobilised on Eupergit C 250L support. However, the use of PBRs with immobilised enzymes could present some disadvantages such as: passive or poor aeration, slow mass transfer, the high pressure drop in the bed can provoke its compactation and hence biocatalyst damage, the possible formation of insoluble products which would lead to clogging phenomena, limitation in substrate's diffusion, intra particle diffusion limitations on reaction rates and possible leakage of the biocatalyst from the support (Gómez et al 2007;Murry et al 2002;O'Neill et al 1971;Osma et al 2010;Rekuc et al 2009). Additionally, long-term operation of packed bed reactor is still a challenge.…”

Section: Decolourisation Of a Model Synthetic Dye By Immobilised Laccasementioning

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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Section: Decolourisation Of a Model Synthetic Dye By Immobilised Laccasementioning

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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“…From the different approaches found in the literature to immobilise laccases (Arica et al, 2009;Durán et al, 2002 and references therein;Georgieva et al, 2008;Rekuc et al, 2009;Russo et al, 2008;Teerapatsakul et al, 2008;Wang et al, 2008;Zhang et al, 2009) attachment by covalent bond on alumina pellets was selected to perform the present study, since it was shown to be a very suitable method for laccase immobilisation retaining high activities (Rodríguez-Couto et al, 2007). In addition, laccases from Trametes hirsuta, Sclerotium rolfsii, Trametes villosa, Trametes modesta and Trametes pubescens were successfully immobilised on alumina pellets and efficiently decolourised several synthetic dyes (Abadulla et al, 2000;Kandelbauer et al, 2004;Rodríguez-Couto et al, 2007;Ryan et al, 2003;Zille et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Transformation pathway of Remazol Brilliant Blue R by immobilised laccase

Osma

Toca-Herrera

Rodríguez‐Couto

2010

Bioresource Technology

133

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“…This rather low degree of bioconversion for the biomass compared with the cell-free extract may be due to mass transfer limitations (Fig. 5c), which has been reported by several researchers [25,26]. The presence of catalase in the reaction mixture was also investigated on the degree of conversion as shown in Fig.…”

Section: Biocatalysis At Moderate Pressures and Atmospheric Pressure mentioning

confidence: 74%

Bioconversion of d-glucose into d-glucosone by Glucose 2-oxidase from Coriolus versicolor at Moderate Pressures

Karmali

Coelho

2010

Appl Biochem Biotechnol

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Abstract:The immobilized glucose 2-oxidase (pyranose oxidase, pyranose:oxygen-2-oxidoreductase, EC 1.1.3.10) from Coriolus versicolor was used to convert D-glucose into D-glucosone at moderate pressures, up to 150 bar, with compressed air in a modified commercial batch reactor. Several parameters affecting biocatalysis at moderate pressures were investigated as follows: pressure, different forms of immobilized biocatalysts, glucose concentration, pH, temperature and the presence of catalase. Glucose 2-oxidase (GOX2) was purified by immobilized metal affinity chromatography on epoxy-activated Sepharose 6B-IDA-Cu(II) column at pH 6.0. Purified enzyme and catalase were immobilized into a polyethersulfone (PES) membrane in the presence of glutaraldehyde and gelatin. Enhancement of the bioconversion of D-glucose was done by the pressure since an increase in the pressure with compressed air increases the conversion rates. The optimum temperature and pH for bioconversion of D-glucose were found to be 62 degrees C and pH 6.0, respectively and the activation energy (E(a)) was 28.01 kJ mol(-1). The apparent kinetic constants (V(max)' K(m)', K(cat)' and K(cat)/K(m)') for this bioconversion were 2.27 U mg(-1) protein, 11.15 mM, 8.33 s(-1) and 747.38 s(-1) M(-1), respectively. The immobilized biomass of C. versicolor as well as crude extract containing GOX2 activity were also useful for bioconversion of D-glucose at 65 bar with a yield of 69.9 +/-3.8% and 91.3 +/-1.2%, respectively. The immobilized enzyme was apparently stable for several months without any significant loss of enzyme activity. On the other hand, this immobilized enzyme was also stable at moderate pressures, since such pressures did not affect significantly the enzyme activity. (C)

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Comparative studies on immobilized laccase behaviour in packed-bed and batch reactors

Cited by 37 publications

References 30 publications

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

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

Transformation pathway of Remazol Brilliant Blue R by immobilised laccase

Bioconversion of d-glucose into d-glucosone by Glucose 2-oxidase from Coriolus versicolor at Moderate Pressures

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