Purification, characterization and selected inhibition properties of peroxidase from haricot bean (<i>Phaseolus vulgaris</i> L.)

Köktepe, Tubanur; Altın, Sevgi; Tohma, Hatice; Gülçın, İlhami; Köksal, Ekrem

doi:10.1080/10942912.2017.1360903

Cited by 9 publications

(16 citation statements)

References 37 publications

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“…Differences in the molecular weight of POX enzymes could be due to differences in amino acid sequence or the degree of glycosylation [37,38]. Maize peroxidase, ionically bound to the cell wall with a molecular weight of 45 kDa was described and considered as a monomer [35]; the soluble bean POX with the same molecular weight was also previously described [39]. The amino acid sequence length of bean and maize sPOX obtained by LC-MS/MS was in the range of 305-370, which is the recorded length of polypeptide chains of secretory peroxidase class III [37].…”

Section: Discussionmentioning

confidence: 99%

Partial characterization of bean and maize root peroxidases and their ability to crosslink potato protein

Glušac

Isaschar-Ovdat

Fishman

et al. 2019

Arch biol sci (Beogr)

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Two fractions of Class III peroxidases (POX; EC 1.11.1.7), soluble and ionically bound to the cell wall, were partially purified from bean and maize roots and characterized. According to the measured K m , both the soluble and ionically bound to the cell wall fractions of POX had high affinity for H 2 O 2 and the high specificity for caffeic acid. Approximate molecular weights of POX in their tertiary (native) structure were determined by modified sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE). Proteomic analysis resolved the identity and pI of different enzyme bands. The ability of maize and bean soluble peroxidase to crosslink native potato proteins was evaluated. The results obtained by SDS-PAGE showed that both POX enzymes were capable of crosslinking potato protein, in particular patatin, a globular protein, with and without the presence of H 2 O 2 . To investigate the possible role of phenolic compounds in facilitating crosslinking, commercial horseradish peroxidase (HRP) with/without the addition of caffeic acid was used to crosslink potato protein.Information provided here could be useful for the purification of POX from maize and bean roots and for examination of protein-protein interactions. Keywords: soluble peroxidase; ionic cell wall-bound peroxidase; bean and maize root; potato protein; protein crosslinking; phenolic compounds Abbreviations: cPOX -covalent bound peroxidase; iPOX -ionically cell wall-bound peroxidase; iPOXb -ionically cell wall-bound bean peroxidase; iPOXc -ionically cell wall-bound maize peroxidase; sPOX -soluble peroxidase; sPOXbsoluble bean peroxidase; sPOXc -soluble maize peroxidase Arch Biol Sci. 2019;71(2):293-303 https://doi.

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Section: Discussionmentioning

confidence: 99%

Partial characterization of bean and maize root peroxidases and their ability to crosslink potato protein

Glušac

Isaschar-Ovdat

Fishman

et al. 2019

Arch biol sci (Beogr)

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“…with the values of V max 1,749 OD/min and K M 113.2 mM (Enachi et al, 2018). Meanwhile, POD obtained from haricot bean showed the affinity for guaiacol and H 2 O 2 with the K M values of 0.0154 mM and 0.065 mM (Köktepe et al, 2017). Additionally, Capone et.…”

Section: Substrate Specificitymentioning

confidence: 94%

“…As can be seen in Figure 2, the occurred specific binding of RBP to affinity matrices that is the critical factor of purification was confirmed by detecting a single band at 31.2 kDa. Other authors purified PODs from haricot bean (Köktepe, Altın, Tohma, Gülçin, & Köksal, 2017), jackfruit (Tao, Wang, Luo, & Yan, 2018), zucchini (Wang, Wang, Wang, Wang, & Huang, 2019) (Thongsook & Barrett, 2005).…”

Section: Molecular Weight Determinationmentioning

confidence: 99%

A novel peroxidase from runner bean ( Phaseolus coccineus L.): Enhanced affinity purification, characterization, and dye decolorization activity

Öztekіn

Tasbasi

2020

J. Food Biochem.

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PODs form a large family of enzymes that contain heme groups and use various hydroperoxides as electron acceptors. They catalyze the redox-mediated oxidation reaction of various organic and inorganic compounds (Jin, Li, Long, & Zhang, 2018). The molecular weights of PODs generally range from 30 to 150 kDa, considering the sources from which they are obtained. Plant PODs are divided into three large groups according to the differences in their primary structure. Class I includes intracellular plants, bacteria, and yeast PODs, while Class II includes the heme group-containing PODs with the capability of oxidizing high reduction potential substrates and manganese. Class III plant PODs typically refer to plant enzymes that are excreted outside the cells or transported into vacuoles (Hiraga, Sasaki, Ito,

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“…botrytis) buds as 44 kDa, [53] and for haricot bean (Phaseolus vulgaris) as 45 kDa. [33] Also, a denatured POD from Euphorbia tirucalli, which migrated in SDS-PAGE, had a single band with a MW of 44 kDa. [60] The differences in the MW of plant POD could be due to differences in amino acid sequences depending on glycosylation levels.…”

Section: Chromatography Studiesmentioning

confidence: 99%

“…[28][29][30] POD has been purified from many different sources like wheat, [31] spinach, [32] and bean. [33] Some of their biochemical properties including thermal stability, optimum and stable pH, optimum temperature, and enzyme kinetics have been determined. In general, similar methods like ammonium sulphate precipitation, dialysis, ion exchange, and gel filtration chromatographies have been used for purification studies, especially made from plant sources.…”

Section: Introductionmentioning

confidence: 99%

Purification and selected biochemical properties of peroxidase from cress (Lepidium sativum sub sp. sativum)

Altay

Köktepe

Durmaz

et al. 2018

International Journal of Food Properties

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Cress (Lepidium sativum) is an annual herb from Brassicaceae family, and in some regions. It is known as peppergrass, garden cress, garden peppercress, pepperwort, or poor man's pepper. Cress is an important medicinal plant in some countries including Turkey. This plant has major scientific and therapeutic significance. Peroxidase (POD, E.C.1.11.1.7) is an oxidoreductase enzyme produced by a number of organisms. In this study, POD enzyme was purified from cress by ammonium sulphate precipitation, gel filtration, and CM-Sephadex ion-exchange chromatographies. K m and V max values were calculated from the Lineweaver-Burk graph for H 2 O 2 and guaiacol substrates and the substrate specificity of POD was investigated. The results showed that substrate specificity of H 2 O 2 is better than substrate specificity of guaiacol for this enzyme. The inhibition effects of three cations (Al 3+ , Cu 2+ , and Cr 3+) and one organic compound of cetyl trimethylammonium bromide were performed and their inhibition types were determined. Finally, optimum pH, optimum temperature, optimum ionic strength, and stable pH were determined.

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Purification, characterization and selected inhibition properties of peroxidase from haricot bean (Phaseolus vulgaris L.)

Cited by 9 publications

References 37 publications

Partial characterization of bean and maize root peroxidases and their ability to crosslink potato protein

Partial characterization of bean and maize root peroxidases and their ability to crosslink potato protein

A novel peroxidase from runner bean ( Phaseolus coccineus L.): Enhanced affinity purification, characterization, and dye decolorization activity

Purification and selected biochemical properties of peroxidase from cress (Lepidium sativum sub sp. sativum)

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