Purification and characterization of cationic peroxidase from ginger (Zingiber officinale)

Abstract

Background: Due 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. Results: The 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 H 2 O 2 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 K m values of 3.1 and 7.1 mM and V max values of 0.6 and 0.31 units/assay using H 2 O 2 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 Hg 2+ and Cu 2+ cations. Conclusion: PGII could be used in several applications due to its catalytic properties, thermal stability, broad pH, and acting on several phenolic compounds.

One‐Step Isolation and Biochemical Characterization of A Novel Peroxidase Enzyme from Jerusalem Artichoke (Helianthus Tuberosus L.)

“…Molecular weights of peroxidase isoenzymes purified from other sources in the literature were determined using the same method. Molecular weights of these peroxidases isolated from different sources were reported to be 76 kDa for zucchini, [11] 69.3 kDa for red cabbage, [24] 46.5 kDa for vanilla bean, [25] 43 kDa for ginger, [26] 104 kDa for jackfruit, [27] and 44.02 kDa for cress [28] . Molecular weights of PODs vary between 40 and 105 kDa according to the purified source.…”

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

“…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), ginger (El‐Khonezy, Abd‐Elaziz, Dondeti, Fahmy, & Mohamed, 2020), and reported their molecular weights as 45, 104, 76, and 42 kDa, respectively. Differences in molecular weights of PODs purified from various sources are associated with various post‐translational changes in the polypeptide, including the number and composition of glycan chains (Thongsook & Barrett, 2005).…”

Extraction, Purification and Characterization of Peroxidase from Okra (Abelmoschus esculentus)

“…It was mentioned [7,20], that the optimum pH for the activity of peroxidase extracted from ginger (Zingiber officinale) and medicinal plant Artocarpus lakoocha was 6. Whereas, [21], mentioned that the optimal pH for the turnip roots (Brassica rapa var.…”

“…Figure (7) shows the thermal stability of the peroxidase when incubated for 15 minutes at temperatures ranging between (25-80) o C, with a difference of 5 degrees between each treatment. The enzyme retained its entire activity when incubated at temperatures ranging between (25-55 o C) for 15 minutes, then the activity started to decrease as the temperature increased above 55C.…”

“…These are superior in their capacity to absorb and transport water, making them ideal for use in dough. In addition, peroxidase can modify the gluten network by cross-linking the gluten proteins or by introducing arabinoxylans to gluten proteins [6,7]. Research on peroxidase enzymes from a wide variety of plants suggested that the enzyme's physical and kinetic properties, as well as its substrate choice, may vary greatly, even within a single source [8,9].…”