Red Cabbage (Brassica oleracea) as a New Source of High-Thermostable Peroxidase

Fortea, María Isabel; Pellicer, José A.; Serrano-Martínez, Ana; López-Miranda, Santiago; Lucas-Abellán, Carmen; Núñez‐Delicado, Estrella

doi:10.1021/jf302483q

Cited by 17 publications

(33 citation statements)

References 54 publications

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“…inset; closed circles), red cabbage POD (Fortea et al . ), marula fruit (Mdluli ) and lower than that obtained for melon (Rodríguez‐López et al . ), pepper (Serrano‐Martínez et al .…”

Section: Resultsmentioning

confidence: 84%

“…The K M value for H 2 O 2 (1.1 mM) (Table ) was higher than that described for membrane‐bound red cabbage POD (0.82 mM) (Fortea et al . ). This kinetic profile contrasts with that obtained for horseradish, asparagus, turnip and red alga peroxidase (Hiner et al .…”

Section: Resultsmentioning

confidence: 97%

“…The K M value for ABTS (0.43 mM) (Table ) was higher than that described for membrane‐bound red cabbage POD (0.2 mM) (Fortea et al . ).…”

Section: Resultsmentioning

confidence: 97%

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Kinetic Characterization and Thermal Properties of Two Acidic Peroxidases from White Cabbage (Brassica OleraceaL.)

Pellicer

Lucas-Abellán

Serrano-Martínez

et al. 2016

Journal of Food Biochemistry

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Soluble and membrane-bound peroxidases (POD) were extracted from white cabbage. Optimum activity was obtained at pH 4.0 for both enzymes. The K M and V m values for H 2 O 2 were found to be 0.62 mM and 6.5 lM/min, respectively, for soluble POD; and 1.1 mM and 7.75 lM/min, respectively, for membrane-bound POD. The K M and V m values for ABTS were found to be 0.92 mM and 7.4 lM/ min, respectively, for soluble POD; and 0.43 mM and 6.95 lM/min, respectively, for membrane-bound POD. The effect of several reducing agents was studied. The effect of cyclodextrins was studied and the complexation constant between ABTS and HP-b-CDs was calculated (K c 5 303 M 21). A thermal inactivation study showed a first-order inactivation kinetic for both enzymes and the Arrhenius plot yielded a straight line with a slope equivalent to activation energy of 153.1 kj/mol for membrane-bound POD and 49.1 kj/mol for soluble POD. PRACTICAL APPLICATIONSRoots of horseradish serve at present as the major source of commercially available peroxidase. However, this peroxidase has certain problems with regard stability and inactivation under certain conditions, hence the interest in finding novel plant peroxidases with greater stability and similar applicability. White cabbage peroxidase could be highly promising for biotechnological applications, taking into account, its high activity, low cost of the raw material and the easy extraction method described.

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Section: Resultsmentioning

confidence: 84%

Section: Resultsmentioning

confidence: 97%

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Kinetic Characterization and Thermal Properties of Two Acidic Peroxidases from White Cabbage (Brassica OleraceaL.)

Pellicer

Lucas-Abellán

Serrano-Martínez

et al. 2016

Journal of Food Biochemistry

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“…[39][40][41] For example, this diversity of forms of peroxidases have been found at cucumber peelings, which showed two isoforms, 42 at tomato fruits, which showed four isoforms, 43 at broccoli stems, which showed three isoforms, 44 at horseradish root, which showing seven isoforms and at coconut endosperm, which showed two isoforms. 45,46 Peroxidase is a key enzyme in controlling plant differentiation and development, and one possible reason for the occurrence of multiple forms of POX is the diversity of biological functions and importance of POX to the growth and self-defense of plants.…”

Section: 38mentioning

confidence: 96%

Partial Purification and Thermal Stability of Two Peroxidases from Pithecellobium dulce (Roxb.) Benth. Aril

et al. 2016

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Resumo: Duas formas de peroxidase (POX), denominadas PdPI e PdPII, foram parcialmente purificadas de arilos de Pithecellobium dulce, utilizando precipitação com sulfato de amônio e cromatografia de troca iônica. O zimograma das proteínas obtidas após precipitação com sulfato de amônio na faixa de 60 a 90% de saturação (fração F6090), mostrou duas bandas com atividade peroxidásica. Na coluna de celulose DE-52, a atividade peroxidásica foi detectada nos picos não adsorvido (PdPI) e adsorvido (PdPII) eluído com NaCl 0,2 mol L -1 , sugerindo que a PdPI (~114 KDa) e a PdPII (~77 KDa) são proteínas básicas e ácidas, respectivamente, sendo a PdPI estável a 80 ºC. Este é o primeiro relato de purificação parcial de POX obtida de arilos de P. dulce, indicando que esta espécie pode ser uma nova fonte de enzimas para utilização em biossensores e outras aplicações biotecnológicas. Palavras-chave:Enzimas; Atividade peroxidásica; P. dulce; Zimograma. AbstractTwo peroxidase (POX) forms, named PdPI and PdPII, were partially purified from the Pithecellobium dulce aril, using ammonium sulfate precipitation and anion exchange chromatography. Zymography of the proteins obtained after precipitation in the range of 60-90% ammonium sulfate (F6090 fraction) showed two bands with peroxidase activity. In DE-52 cellulose column, the peroxidase activity was detected in unadsorbed peak (PdPI) and adsorbed peak eluted with 0.2 mol L -1 NaCl (PdPII) suggesting that PdPI (~114 KDa) and PdPII (~77 KDa) are basic and acidic proteins, respectively, being PdPI stable at 80 ºC. This is the first report of partial purification of POX from P. dulce aril, indicating that this species may be a new source of enzymes for use in biosensors and other biotechnological applications.

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“…The class III plant peroxidases have been reported to play crucial roles in the plant life cycle [13] such as cell wall metabolism [9], lignification [10], suberization [11], auxins metabolism [12], wound healing, reactive oxygen species (ROS) and reactive nitrogen species (RNS) metabolism [13,14], fruit growth and ripening [15], defense against pathogens [16] etc.…”

Section: Introductionmentioning

confidence: 99%

A Defense Associated Peroxidase from Lemon Having Dye Decolorizing Ability and Offering Resistance to Heat, Heavy Metals and Organic Solvents

Veda¹,

ey²,

Bhagat³

et al. 2016

Biochem Anal Biochem

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Peroxidases have ability to catalyze redox reaction of a wide range of phenolic as well as non-phenolic compounds and exhibited various physiological roles in plant life cycle. From the point of view of industrial applications of peroxidases, the isolation and characterization of peroxidases offering resistance to higher pH and temperature, salts, organic solvents is highly desirable. In this direction, a partial cDNA clone of peroxidase from lemon was isolated and characterized. The peroxidase was found to be defense associated as evident by the higher expression in diseased condition than that of healthy one at both the transcript and enzymatic activity levels. This defense related peroxidase from lemon leaves was purified to homogeneity using quick two step processes of heat treatment and affinity chromatography. The native peroxidase was found to be a heterotrimer of 200 kDa, consisting of two subunits each of 66 kDa while, one subunit of 70 kDa. The purified peroxidase was found to be stable towards heat (retained 92% activity at 80°C for 1 h) and organic solvents, namely ethanol, methanol and isopropanol (retained 30-50% activity in the presence of 50% (v/v) of these solvents for 1 h). Purified peroxidase also exhibited tolerance to heavy metal ions such as Cd 2+ , Ni 2+ and Cs 2+ . The purified lemon peroxidase was found to efficiently oxidize the industrial dyes in the order of aniline blue>methyl orange> indigo carmine >trypan blue > crystal violet, such that 40-54% dye decolorization was observed within 4 h. Thus, the properties exhibited by purified lemon peroxidase make it a promising candidate enzyme for industrial exploitation.

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Red Cabbage (Brassica oleracea) as a New Source of High-Thermostable Peroxidase

Cited by 17 publications

References 54 publications

Kinetic Characterization and Thermal Properties of Two Acidic Peroxidases from White Cabbage (Brassica OleraceaL.)

Kinetic Characterization and Thermal Properties of Two Acidic Peroxidases from White Cabbage (Brassica OleraceaL.)

Partial Purification and Thermal Stability of Two Peroxidases from Pithecellobium dulce (Roxb.) Benth. Aril

A Defense Associated Peroxidase from Lemon Having Dye Decolorizing Ability and Offering Resistance to Heat, Heavy Metals and Organic Solvents

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