Characterization of soybean peroxidase for the treatment of aqueous phenols

Wright, H. E.; Nicell, Jim A.

doi:10.1016/s0960-8524(99)00007-3

Cited by 127 publications

(78 citation statements)

References 24 publications

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“…Another work by Wright and Nicell [14] showed that nearly complete removal of phenol was observed over a pH range of 5 to 9, with the maximum removal at pH 6 by using high dose of soybean peroxidase (SBP). The optimum operating pH for jicama peroxidase was…”

Section: Effect Of Phmentioning

confidence: 99%

“…Since then, horseradish peroxidase (HRP) became the most explored plant peroxidase, and its ability in removing various phenolic compounds from aqueous solutions are well documented [11]- [13]. Peroxidases from other sources such as soybean seed hulls, bitter gourd, cauliflower, potato and white radish have also been evaluated for their performances in treating phenol, and the reported results were encouraging [14]- [17].…”

Section: Introductionmentioning

confidence: 99%

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Comparison of two Agricultural Wastes for Phenol Removal Via Peroxidase-Catalyzed Enzymatic Approach

et al. 2016

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Abstract. Agricultural wastes of jicama and luffa skin peels were used as the source for peroxidase extraction. The extracted crude enzymes showed similar activities, 1.34U/mL and 1.22U/mL for jicama and luffa peroxidase respectively. These peroxidases were used to treat phenol under varying operating conditions of buffer pH, hydrogen peroxide concentration, enzyme volume and temperature. Jicama peroxidase demonstrated a phenol removal efficiency of approximately 90% at buffer pH 7, 1mM hydrogen peroxide using 1.5mL enzyme at 25 o C. Luffa peroxidase required a higher dosage of hydrogen peroxide, and exhibited a removal efficiency of 84% at 8mM with other operating conditions same as jicama peroxidase. Jicama peroxidase is sensitive to pH change and more susceptible to thermal denaturation. Luffa peroxidase showed a better stability in terms of temperature.

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Section: Effect Of Phmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Comparison of two Agricultural Wastes for Phenol Removal Via Peroxidase-Catalyzed Enzymatic Approach

et al. 2016

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“…A number of other plants such as potatoes, cauliflower, cherries, soybeans and several fungi may also be used as sources of peroxidase enzymes. Soybeans, in particular, may represent a valuable source of peroxidase since the enzyme is found in the seed coat, which is a waste product from soybean-based industries (Wright and Nicell, 1999). In this case, it may be possible to use the solid waste from the soybean industry to treat the wastewaters of various chemical industries.…”

Section: Enzyme Costmentioning

confidence: 99%

Environmental applications of enzymes

Nicell¹

2001

IER

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Enzymatic processes fall between the two traditional categories of chemical and biological treatment systems since they involve chemical reactions based on the action of biological catalysts. A variety of enzymes from plants and microorganisms have been reported to play important roles in an array of waste treatment applications. Before the full potential of enzymes may be realized, a number of significant issues remain to be addressed. These include: development of low-cost sources of enzymes in quantities that are required at the industrial scale; demonstration of the feasibility of utilizing the enzymes efficiently under the conditions encountered during wastewater treatment; characterization of reaction products and assessment of their impact on downstream processes or on the environment into which they are released; and identification of methods for the disposal of solid residues, among others.

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“…A peroxidase tem sido utilizada em biotecnologia e várias outras áreas da ciência, para estabelecimento de diagnósticos clínicos e avaliação de processos patológicos 6,9,11,12,16,22,25 , em análise de qualidade dos alimentos 3,23,30,32 , na construção de biossensores para análise qualitativa e quantitativa de formulações farmacêuticas, cosméticas e outras análises que envolvam a presença ou a formação de peróxidos e outros processos enzimáticos 5,24,28,34,35,36 .…”

Section: Introductionunclassified

“…Existe a possibilidade de que a medida da atividade de peroxidase em extrato de plantas não reflita sua real atividade in vivo 7 e a determinação do substrato específico in vivo permanece como ponto crucial para estabelecer o papel fisiológico das isoperoxidases aniônica, catiônica ou neutra 2,10,26,33. Tem sido identificada a importância fisiológica da peroxidase no controle do crescimento, lignificação 1 , biossíntese da parede celular 27,31 , defesa contra patógenos e esta enzima pode ainda causar mudanças indesejáveis no aroma, gosto, cor, textura e também a perda de nutrientes em alimentos 14,29,30,32 .A peroxidase tem sido utilizada em biotecnologia e várias outras áreas da ciência, para estabelecimento de diagnósticos clínicos e avaliação de processos patológicos 6,9,11,12,16,22,25 , em análise de qualidade dos alimentos 3,23,30,32 , na construção de biossensores para análise qualitativa e quantitativa de formulações farmacêuticas, cosméticas e outras análises que envolvam a presença ou a formação de peróxidos e outros processos enzimáticos 5,24,28,34,35,36 .Devido à ampla utilização das peroxidases há um interesse crescente por novas fontes desta enzima. O Brasil possui ampla variedade de vegetais que podem se constituir em fonte inesgotável de enzimas 34,35 .…”

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Extração e caracterização parcial de peroxidase de folhas de Copaifera langsdorffii Desf.

Maciel¹,

Gouvêa²,

Pastore³

2007

Ciênc. Tecnol. Aliment.

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ResumoEm recentes publicações têm sido descritos vários processos para obtenção de peroxidases. O propósito deste trabalho foi extrair peroxidase de folhas de Copaifera langsdorffii e caracterizar parcialmente a enzima usando planejamento experimental e teste univariado, para confirmação dos resultados obtidos por planejamento experimental. A atividade da peroxidase foi medida usando sistema guaiacol: peróxido de hidrogênio. A peroxidase isolada apresentou 81,6% da atividade da horseradish peroxidase e é de fácil obtenção, a partir de folhas de uma árvore abundante em todo o país. A peroxidase semi-purificada (COP) foi obtida pela precipitação do extrato bruto com acetona 65% (v.v -1 ), produzindo o pó cetônico. A COP apresentou atividade ótima na faixa de pH 5,0 a 7,0 e temperatura de 5 a 45 °C, com atividade máxima em pH 6,0 e 35 °C. A enzima mostrou-se estável em temperaturas inferiores a 50 °C e pH entre 4,5 e 9,0, por até 24 horas. A peroxidase foi inativada após 4 horas a 80 °C e após 3 minutos a 96 °C. Esta enzima demonstra possibilidade para ser usada como reagente para diagnósticos, construção de biossensores e outros métodos analíticos em vários campos da ciência. Palavras-chave: copaíba; enzima; extrato vegetal. AbstractIn the literature, several processes have been described to obtain peroxidases. The purpose of this work was to obtain peroxidase from Copaifera langsdorffii leaves and characterize it partially using a factorial design of experiments and univaried tests, to confirm the results obtained by the factorial design of experiments. Peroxidase activity was measured using the guaiacol: hydrogen peroxide system. The isolated peroxidase presented 81.6% of horseradish peroxidase activity and was easy to obtain from leaves of an abundant tree distributed all over the country. Semi-purified peroxidase (COP) was precipitated with acetone 65% (v.v -1 ) of the crude extract, obtaining the acetone powder. The COP optimum reaction pH values were between 5.0-7.0 and the temperatures between 5 and 45 °C, with a maximum activity at pH 6.0 and 35 °C. The enzyme was stable in temperatures below 50 °C and pH from 4.5 to 9.0 for up to 24 hours. The peroxidase was inactivated after 4 hours at 80 °C and after 3 minutes at 96 °C. This enzyme can possibly be used as a diagnostic reagent, biosensor and for other analytical methods in several fields of Sciences. Keywords: copaiba; enzyme; vegetal extract.Extração e caracterização parcial de peroxidase de folhas de Copaifera langsdorffii Desf. Extraction and partial characterization of peroxidase from Copaifera langsdorffii Desf. LeavesHermelinda Penha Freire MACIEL 1 , Cibele Marli Cação Paiva GOUVÊA 2 *, Gláucia Maria PASTORE 1 IntroduçãoAs peroxidases (E.C. 1.11.1.7, doador H 2 O 2 oxidorredutase) catalisam a redução do peróxido de hidrogênio ou outro peróxido orgânico, enquanto um doador de elétrons é oxidado. São abundantes em vários organismos incluindo as plantas superiores, com múltiplas isoformas sintetizadas e reguladas por estímulos diversos 8,22 . Nas últ...

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Characterization of soybean peroxidase for the treatment of aqueous phenols

Cited by 127 publications

References 24 publications

Comparison of two Agricultural Wastes for Phenol Removal Via Peroxidase-Catalyzed Enzymatic Approach

Comparison of two Agricultural Wastes for Phenol Removal Via Peroxidase-Catalyzed Enzymatic Approach

Environmental applications of enzymes

Extração e caracterização parcial de peroxidase de folhas de Copaifera langsdorffii Desf.

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