Abstract
BackgroundDue to versatility in reaction catalyzed by peroxidases, they have potential applications in different areas in the health sciences, food industry, and diagnostic purposes. Therefore, the aim of this study is to investigate the properties of peroxidase from ginger to be meeting the perquisites of several applications.ResultsThe cationic peroxidase (GPII) was purified to homogeneity by anion exchange chromatography using DEAE–Sepharose column followed by cation exchange chromatography using CM–Sepharose column and finally Sephacryl S-200 column. The molecular mass of GPII was 42 kDa. GPII shows oxidizing activity with several phenolic compounds by using H2O2 as the second substrate. The natural plant phenolic compounds as pyrogallol, catechol, and guaiacol were found to be excellent electron donors for the enzyme compared to other phenolic compounds. GPII exhibited Km values of 3.1 and 7.1 mM and Vmax values of 0.6 and 0.31 units/assay using H2O2 and guaiacol as substrates, respectively. The enzyme exhibited maximal peroxidase activity at broad pH’s 6.0–7.5 and 50 °C. GPII was thermal stable up to 50 °C and retained 66% of its activity at 70 °C after 1 h incubation. The GPII activated by most divalent cations tested and inhibited by Hg2+ and Cu2+ cations.ConclusionPGII could be used in several applications due to its catalytic properties, thermal stability, broad pH, and acting on several phenolic compounds.
Highlights
Due to versatility in reaction catalyzed by peroxidases, they have potential applications in different areas in the health sciences, food industry, and diagnostic purposes
Due to versatility in reaction catalyzed by peroxidases, and their ubiquitous nature, they have potential applications in different areas in the health sciences, food industry, and diagnostic purposes (Pandey et al 2017; Abdel-Aty et al 2018)
Despite the variety of plant peroxidase sources, there is no previous study on peroxidase from Zingiber officinale commonly known as ginger, originated in the IndoMalayan region, is widely distributed across the
Summary
Due to versatility in reaction catalyzed by peroxidases, they have potential applications in different areas in the health sciences, food industry, and diagnostic purposes. The non-animal plant peroxidases, belonging to Class III peroxidase, are enzymes that participate in diverse physiological and biochemical functions in higher plant cells and are, interesting objects of current biochemical research (Has-Schön et al 2005; Pandey et al 2017) They are implicated in various vital processes in vivo include cell wall edification, cellular growth, differentiation and development, in hormone catabolism, lignin polymerization, suberization, fruit growth and ripening, ethylene biosynthesis, plasma membrane redox systems and the generation of H2O2, auxin metabolism, senescence, and defense mechanisms against abiotic and biotic stress (Chen et al 2012; Mohamed et al 2014; Aslmoshtaghi and Shahsavar 2016; Galende et al 2016; Julião et al 2016). Despite the variety of plant peroxidase sources, there is no previous study on peroxidase from Zingiber officinale commonly known as ginger, originated in the IndoMalayan region, is widely distributed across the
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