Ionically Bound Peroxidase from Peach Fruit

Neves, Valdir Augusto

doi:10.1590/s1516-89132002000100002

Cited by 20 publications

(23 citation statements)

References 40 publications

(50 reference statements)

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“…According to the present results and those of other authors the enzymes from different sources appeared to behave differently in the presence of sugars on heating. Various oxidative enzymes such as peroxidases were less susceptible to thermal inactivation when heated in different sucrose solution concentration (Chang et al, 1988, Neves andLourenço, 1998;Neves, 2002). The protective effect of polyols on thermal denaturation of proteins is a fact; however, the mechanisms are still in discussion (Arakawa andTimashef, 1982, Neucere andSt Angelo, 1985).…”

Section: The Effect Of Sugars On Heat Stability and Activation Energymentioning

confidence: 99%

Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)

Neves

Picchi

Silva

2009

Braz. arch. biol. technol.

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Section: The Effect Of Sugars On Heat Stability and Activation Energymentioning

confidence: 99%

Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)

Neves

Picchi

Silva

2009

Braz. arch. biol. technol.

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“…Similarly highest activities were shown in case of tobacco leaf at 70°C, (Silva et al, 1990), in Ricinus at 60°C (Ryan et al 1994), in lima bean (Phaseolus limensis) seed at 55°C (Wang et al 2008), in sunflower at 50°C (Hager et al 2008) and in peach fruit at 40°C (Neves 2002;Neves and Lourenço 1998) and a ranges of 40-70°C…”

Section: Effect Of Temperaturementioning

confidence: 76%

“…Similarly, Native-PAGE result observed i.e. seven distinct bands in case of Ricinus communis (Kumar et al 2008) and three bands in case of crude and two bands for purified peroxidase from peach fruit (Neves 2002), different banding pattern of enzymes proved that enzyme are present in more than one form (isozymes).…”

Section: Native Pagementioning

confidence: 89%

“…In case of apple methionine, proline, tryptophan, and valine stimulated all four apple peroxidases, but cysteine showed inhibition in Golden delicious JK (Dubey et al 2007;Singh et al 2010). It was observed that the L-cysteine, inhibit the enzyme activity in case of peach (Neves 2002). Similarly, Ricinus peroxidases were stimulated by amino acids like L-proline and L-alanine, while DL-methionine and L-valine showed strong inhibition (Kumar et al 2008).…”

Section: Effect Of Amino Acidsmentioning

confidence: 99%

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Biochemical characterization of Santalum album (Chandan) leaf peroxidase

Kumar¹,

Kamle²,

Singh³

2011

Physiol Mol Biol Plants

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The Santalum peroxidase was extracted from the leaves and precipitated with double volume of chilled acetone. The optimum percent relative activity for the Santalum peroxidase was observed at pH 5.0 and 50°C temperature. The Santalum peroxidase per cent relative activity was stimulated in the presence of phenolic compounds like ferrulic acid and caffeic acids; however, indole-3-acetic acid (IAA) and protocatechuic acid act as inhibitors. All divalent cations Fe 2+ , Mn 2+ , Mg 2+ , Cu 2+ and Zn 2+ stimulate the relative activity of the Santalum peroxidase at concentration of 2.0 μM. Amino acids like L-alanine and L-valine activate the per cent relative activity, while L-proline and DL-methionine showed moderate inhibition for the Santalum peroxidase. However, a very low a concentration of cysteine acts as a strong inhibitor of Santalum peroxidase at the concentration of 0.4 mM. Native polyacrylamide gel electrophoresis (Native-PAGE) was performed for isoenzyme determination and two bands were observed. K m and V max values were calculated from Lineweaver-Burk graph. The apparent V max /K m value for O-dianisidine and H 2 O 2 were 400 and 5.0×105 Units/min/ mL respectively.

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“…[2][3][4] Plant peroxidases (POX) are usually found in roots, 4 latex, 5 flowers, 6 leaves, 5 seeds and fruits. 7,8 They are present in multiple ionic forms and their in vivo functions include cellular growth, the synthesis of cell walls, fruit growth and ripening, hormone regulation, lignification, senescence and defense mechanisms against abiotic and biotic stress. [2][3][4] Various types of POX can be found in the same plant species and these may differ significantly in molecular weight, substrate specificity and thermal stability.…”

Section: Introductionmentioning

confidence: 99%

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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Ionically Bound Peroxidase from Peach Fruit

Abstract: ABSTRACT

Cited by 20 publications

References 40 publications

Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)

Some Biochemical properties of polyphenoloxidase from spearmint (Mentha arvensis)

Biochemical characterization of Santalum album (Chandan) leaf peroxidase

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

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