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

Maciel, Hermelinda Penha Freire; Gouvêa, Cibele Marli Cação Paiva; Pastore, Gláucia Maria

doi:10.1590/s0101-20612007000200002

Cited by 5 publications

(3 citation statements)

References 32 publications

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“…Thus, the wastewater from textile industries is considered as one of the most polluting among all industrial wastes, thereby requiring appropriate treatment technologies. Peroxidases have been shown to have great potential in the decolorization process to decrease textile industry pollutant residues [166,167]. Uses of peroxidases, such as horseradish, Brassica campestres turnip, tomato, bitter gourd, soybean, Ipomea palmata and Saccharum spontaneum peroxidases, for degrading and detoxifying polyaromatic hydrocarbons, polychlorinated biphenyls, and other synthetic industrial dyes have been reported [168][169][170][171][172][173][174][175][176][177][178].…”

Section: Application In De-colorization Of Industrial Dyesmentioning

confidence: 99%

A Comprehensive Review on Function and Application of Plant Peroxidases

Pandey¹,

Awasthi²,

Singh³

et al. 2017

Biochem Anal Biochem

245

213

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Peroxidases, one of the key antioxidant enzymes, are widely distributed in nature and catalyze oxidation of various electron donor substrates concomitant with the decomposition of H 2 O 2. The non-animal plant peroxidases (class III peroxidase) are involved in various essential physiological processes of plant growth and development throughout their life cycle. In view of the capability of peroxidases to catalyze the redox reaction for a wide range of substrates, they are considered as one of the important enzyme from the point of view of their various medicinal, biochemical, immunological, biotechnological and industrial applications. They have been successfully used for biopulping and biobleaching in the paper and textile industries. Peroxidases have also been used in organic synthesis, bioremediation, as well as various analytical applications in diagnostic kits, ELISA. Peroxidase based biosensors find application in analytical systems for determination of hydrogen peroxide, glucose, alcohols, glutamate, and choline etc. Thus, in view of array of physiological functions as well as industrial applications, the peroxidases have conquered a dominant position in research groups and become one of the most extensively studied enzymes. In this direction, the present review embodies the classification, mechanism of action, major physiological functions as well as industrial applications of plant peroxidases.

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Section: Application In De-colorization Of Industrial Dyesmentioning

confidence: 99%

A Comprehensive Review on Function and Application of Plant Peroxidases

Pandey¹,

Awasthi²,

Singh³

et al. 2017

Biochem Anal Biochem

245

213

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show abstract

“…As peroxidases são encontradas em diversas espécies do reino vegetal, e a mais importante, do ponto de vista comercial, é a enzima isolada da raiz forte (Armoracia rusticana) também conhecida como raiz ardida, rábano de cavalo ou rábano rusticana, na forma purificada (Horseradish peroxidase -HRP). A raiz forte é geralmente cultivada e colhida em países de clima frio (Maciel et al, 2007). Cooper e Nicell (1996) verificaram uma atividade específica da HRP purificada de 83,0  4,5 U.mg -1 .…”

Section: Peroxidases De Vegetaisunclassified

Extraction and Purification of Vegetable Peroxidase: A Review

Haas¹,

Vaz²,

Kempka³

2019

PTQ

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Peroxidases are enzymes that catalyze the oxidation of various substrates, maintaining their enzymatic activity in wide ranges of pH and temperatures. These enzymes are used in processes for the degradation of dyes and phenolic compounds. Peroxidases are present in the tissues of several plants, and the search for new sources of this enzyme is necessary. This literature review aims to compile information about the extraction and/or purification of peroxidases contained in different plant tissues, presenting extraction methods, purification processes, enzymatic activities and their increments, according to the chemical and physical processes applied. Several plant sources can be raw material to obtain these enzymes, through different forms of extraction, where the processes of comminution predominate in the presence of buffer solution. For partial purification, are used precipitation with solvents (acetone and ethanol) and salts (ammonium sulfate) and centrifugation. For purification, chromatographic processes are used, in which molecular exclusion and affinity chromatography are prominent. It is concluded that there is a wide range of possibilities for obtaining the enzyme peroxidase from plants, with variability in the enzymatic activity when different extraction methods are applied. The purification methods used provide increases in the specific activity of the peroxidases.

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“…These enzymes catalyze a variety of reactions, including the oxidation of various organic and inorganic compounds in the presence of peroxides, such as hydrogen peroxide. Peroxidase activity in the plants is related to the regulation of growth and differentiation processes, such as the inhibition of growth by regulating the cell wall lignification; morphogenic changes in response to physical, chemical and biological stress; wound healing; pathogen defense; the regulation of cell elongation; and other characteristics (Kao 2003;Nieves et al 2003;Piza et al 2003;Campos et al 2004;Maciel 2007;Freitas et al 2008). Other biochemical components considered are the contents of total and reducing sugars, amino acids and soluble proteins.…”

Section: Introductionmentioning

confidence: 99%

Cytokinin Dehydrogenase activity in primary roots and characterization of primary metabolites from leaves and rootlets of Ricinus Communis

Marques

Freitas

Guedes

et al. 2013

Braz. arch. biol. technol.

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The aim of this study was to determine the activity of cytokinin dehydrogenase (CKX) and to measure other biochemical components in the primary leaves and radicles of castor seedlings (BRS Energia) in the initial phase of growth. The crude protein extract obtained after a 1-h extraction from the root tissues of seedlings showed nodetectable CKX enzymatic activity when incubated with the substrate isopentenyl adenine for 1 h. However, after precipitation with ammonium sulfate at 70% saturation, the pellet showed CKX activity. The peroxidase enzyme activity was higher in the leaves than in the radicles. The total and reducing sugar content was 1.5 times higher in the leaves than in the radicles. The amino acid and protein contents were 6.4 and 9.2 times higher in the leaves than in the radicles, respectively.

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

Cited by 5 publications

References 32 publications

A Comprehensive Review on Function and Application of Plant Peroxidases

A Comprehensive Review on Function and Application of Plant Peroxidases

Extraction and Purification of Vegetable Peroxidase: A Review

Cytokinin Dehydrogenase activity in primary roots and characterization of primary metabolites from leaves and rootlets of Ricinus Communis

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