A capillary membrane bioreactor using immobilized polyphenol oxidase for the removal of phenols from industrial effluents

Edwards, W; Bownes, R; Leukes, W.D.; Jacobs, E.P.; Sanderson, Ronald D.; Rose, P.D.; Burton, Stephanie G.

doi:10.1016/s0141-0229(98)00110-0

Cited by 82 publications

(29 citation statements)

References 19 publications

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“…Phenol was measured using a colorimetric assay using 4-aminoantipyrine and potassium ferricyanide under alkaline conditions to form a red quinone-type dye absorbing maximally at 510 nm (Edwards et al 1999).…”

Section: Determination Of the Concentration Of Phenolmentioning

confidence: 99%

“…1.14.18.1) catalyzes the conversion of phenols to o-quinones, which then undergo spontaneous, non-enzymatic polymerization in water, eventually forming water-insoluble polymers which can be separated from solution by filtration (Edwards et al 1999). Several techniques based on the PPO treatment have been developed for the remediation of industrial wastewaters but the cost of the processes has limited their use (Amjad et al 2006).…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of polyphenol oxidase on chitosan–SiO2 gel for removal of aqueous phenol

Shao

Yang

2007

Biotechnol Lett

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A partially purified potato polyphenol oxidase (PPO) was immobilized in a cross-linked chitosan-SiO2 gel and used to treat phenol solutions. Under optimized conditions (formaldehyde 20 mg/ml, PPO 4 mg/ml and pH 7.0), the activity of immobilized PPO was 1370 U/g and its Km value for catechol was 12 mM at 25 degrees C. The highest activity of immobilized enzyme was at pH 7.4. Immobilization stabilized the enzyme with 73 and 58% retention of activity after 10 and 20 days, respectively, at 30 degrees C whereas most of the free enzyme was inactive after 7 days. The efficiency of removing phenol (10 mg phenol/l) by the immobilized PPO was 86%, and about 60% removal efficiency was retained after five recycles. The immobilized PPO may thus be a useful for removing phenolic compounds from industrial waste-waters.

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Section: Determination Of the Concentration Of Phenolmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Immobilization of polyphenol oxidase on chitosan–SiO2 gel for removal of aqueous phenol

Shao

Yang

2007

Biotechnol Lett

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“…Some of these disadvantages can be overcome in an enzyme-based reactor, since enzymes are able to operate over a broad concentration range [16,17]. The potential advantages of this enzymatic treatment, as compared to *Corresponding author: Chinnathambi Velu, Research Associate, ARMATS BIOTEK Research Institute, Kottur, Chennai, India-600085, E-mail: chinna.velu1@ gmail.com conventional treatments, include application to recalcitrant materials, operation at high and low contaminant concentrations over a wide pH, temperature and salinity range.…”

Section: Introductionmentioning

confidence: 99%

Insilico Screening and Comparative Study on the Effectiveness of Textile Dye Decolourization by Crude Laccase Immobilised Alginate Encapsulated Beads from Pleurotus Ostreatus

Velu¹,

Veeramani²,

Suntharam³

et al. 2011

J Bioproces Biotechniq

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The necessity to safeguard the environment has increased the potential of enzyme usage in textile processing to ensure eco-friendly production. Laccase enzyme formulation has been used in textile processing such as biobleaching, dyeing, rove scouring, finishing, neps removal, printing, wash-off treatment, dye synthesis and effluent treatment. However, a high cost associated with biocatalyst production is still a hindrance to their use. Pleurotus ostreatus is a white-rot fungus that produces a ligninolytic enzyme complex rich in several laccase iso-enzymes. The main objective of this study is optimize influence of pH and stability of divalent metal ion-immobilzed crude laccase enzyme towards decolourization of prototype textile dyes such as Reactive red 80 (Red F3B) and Reactive blue 21(T Blue G). Wheat bran is used as a lead candidature for production of lignolytic enzyme using Pleurotus osteratus by solid state fermentation. Two divalent metal ions such as Zn2 + and Ca2 + were selected to study the influence of metal ions towards the dye decolourization. Results revealed that Ca2 + ion was better compared to Zn2 + ion towards enzyme immobilization and its influence on dye decolourization in the optimal pH 5.5. Finally, interactions between laccase and dyes were studied exclusively using Insilco structure based molecular docking methods.

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“…1 Extraction of high activity PPO is desirable, since this enzyme is important in analytical methods for total phenol content determinations in several biological and pharmaceutical samples, such as hydroquinone in cosmetic creams and photographic developers and paracetamol in pharmaceutical formulations. 1,3,4,[12][13][14][15][16] The purpose of this paper is to describe the performance of Jackfruit crude extracts, a new and relatively unexplored enzymatic source, in homogeneous phase phenol oxidation reactions, using atmospheric oxygen as oxidizing agent. The factors considered are pH, concentration of the phosphate buffer and the kind identity of some commercially available biophenols extractors.…”

Section: Introductionmentioning

confidence: 99%

“…This fact is also confirmed by other investigations. 1,3,4,8,13 A factorial design can provide new and efficient approaches to study enzymatic performance by an investigation of simultaneous changes in some selected experimental factors. The values of the several effects show that pH has a decisive influence on PPO activity.…”

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confidence: 99%

Factorial Design Evaluation of Some Experimental Factors for Phenols Oxidation using Crude Extracts from Jackfruit (Artocarpus integrifolia)

Cestari

Vieira

Nascimento

et al. 2002

J. Braz. Chem. Soc.

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Este estudo apresenta algumas informações adicionais sobre a utilização alternativa do extrato bruto da jaca, em reações de oxidação seletivas de fenóis. Foram avaliados os substratos catecol, o-, me p-cresóis e pirogalol. Estudaram-se também os efeitos do pH, da concentração do tampão fosfato, bem como a utilização de alguns tipos de agentes extratores de biofenóis. Utilizando-se o procedimento convencional univariado, a atividade enzimática foi maior com o substrato catecol, em tampão fosfato pH 5,0, de concentração 0,10 mol L -1 e agente comercial extrator de fenóis Polyclar SB-100 â . Usando-se um planejamento fatorial, do tipo 2 3 , constatou-se que os melhores desempenhos catalíticos foram em pH 5,0 e concentração de tampão 0,050 mol L -1 , para o substrato catecol. A variação no tipo de extrator não mostrou importância estatística. Pelo método multivariado, obtiveram-se os melhores resultados para a oxidação seletiva do catecol. Assim, conclui-se que para aumentar o desempenho catalítico do extrato, deve-se utilizar preferencialmente a metodologia multivariada.This study presents some additional information on the alternative utilization of Jackfruit crude extracts in selective phenol oxidation reactions, using catechol and the o-, m-e p-cresols and pyrogallol substracts. The effects of pH, concentration of phosphate buffer and kinds of natural phenol extractors are evaluated. By using the conventional univariate procedure, the best enzymatic activities were obtained with the catechol substract, phosphate buffer (pH 5.0) at a concentration 0.10 mol L -1 , and the commercial polymer Polyclar SB-100 â as natural phenol extractor. Using a full 2 3 factorial design the best catalytic results were obtained by employing phosphate buffer at pH 5.0 and it 0.050 mol L -1 . However, the kind of phenol extractor was not statistically important. The best results for selective catechol oxidation were obtained by using the multivariate technique. In this way, the multivariate methodology is indicated to increase the performance of the crude extract in the selective oxidation reactions.Keywords: homogeneous enzymatic catalysis, jackfruit, phenol oxidations, factorial designs IntroductionRecently, an increasing trend has been observed in the use of new biocatalytic materials in place of pure enzymes, for the development of several different research lines, especially those related to the development of biosensors 1 and enzyme-catalyzed methods of analysis. 2 The use of such materials offers some advantages with regard to those procedures based on the use of pure and isolated enzymes, especially by providing a better lifetime and lower cost. 3,4 Natural and undesirable browning reactions, using atmospheric oxygen as oxidant, occur by the catalysis of, mainly, the enzyme polyphenol oxidase (PPO). 3-5 PPO is a copper-containing oxidase having catecholase and/or cresolase activity. PPO catalyses o-hydroxylation of monophenols to give o-diphenols (cresolase activity) and o-diphenols to o-quinones (catecholase activity). For P...

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A capillary membrane bioreactor using immobilized polyphenol oxidase for the removal of phenols from industrial effluents

Cited by 82 publications

References 19 publications

Immobilization of polyphenol oxidase on chitosan–SiO2 gel for removal of aqueous phenol

Immobilization of polyphenol oxidase on chitosan–SiO2 gel for removal of aqueous phenol

Insilico Screening and Comparative Study on the Effectiveness of Textile Dye Decolourization by Crude Laccase Immobilised Alginate Encapsulated Beads from Pleurotus Ostreatus

Factorial Design Evaluation of Some Experimental Factors for Phenols Oxidation using Crude Extracts from Jackfruit (Artocarpus integrifolia)

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