A novel peroxidase from Ziziphus jujuba fruit: purification, thermodynamics and biochemical characterization properties.

ABSTRACT: In this study, peroxidase from Ziziphus jujuba was purified using ion exchange, and gel filtration chromatography resulting in an 18.9-fold enhancement of activity with a recovery of 20%. The molecular weight of Z. jujuba peroxidase was 56 kDa, as estimated by Sephacryl S-200. The purity was evaluated by SDS, which showed a single prominent band. The optimal activity of the peroxidase was achieved at pH 7.5 and 50 °C. Z. jujuba peroxidase showed catalytic efficiency (Kcat/Km) values of 25 and 43 for guaiacol and H₂O₂, respectively. It was completely inactivated when incubated with β-mercaptoethanol for 15 min. Hg²⁺, Zn²⁺, Cd²⁺, and NaN3 (5 mM) were effective peroxidase inhibitors, whereas Cu²⁺ and Ca²⁺ enhanced th

SUBMITTER: Zeyadi M 

PROVIDER: S-EPMC7224213 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature