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Original Articles

Purification and Characterization of Polyphenol Oxidase from Hemşin Apple (Malus communis L.)

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Pages 2735-2745 | Received 17 Sep 2014, Accepted 25 Jan 2015, Published online: 31 Jul 2015

Figures & data

TABLE 1 Purification of polyphenol oxidase (PPO) from Hemşin apple (Malus communis L.)

FIGURE 1 DE52-Cellulose (Diethylaminoethyl cellulose) column. (-●-) symbolize the protein content, which was spectrophotometrically measured by the absorbance at 280 nm. (-○-) symbolize the PPO activity, which was measured by the activity assay. (-∆-) symbolize the linear gradient buffer which containing (0,1–1 M) NaCl.

FIGURE 1 DE52-Cellulose (Diethylaminoethyl cellulose) column. (-●-) symbolize the protein content, which was spectrophotometrically measured by the absorbance at 280 nm. (-○-) symbolize the PPO activity, which was measured by the activity assay. (-∆-) symbolize the linear gradient buffer which containing (0,1–1 M) NaCl.

TABLE 2 The optimum conditions for and the kinetic and thermodynamic characteristics of purified Hemşin apple (Malus communis L.) PPO activity. (kcat: turnover number, Vmax: maximum velocity, Km: Michaelis-Menten constant, Vo: catalytic efficacy, Ea: activation energy, ∆H: enthalpy)

FIGURE 2 Optimum temperature of PPO from Malus communis L. The Arrhenius plots for heat inactivation of the purified PPO.

FIGURE 2 Optimum temperature of PPO from Malus communis L. The Arrhenius plots for heat inactivation of the purified PPO.

FIGURE 3 Determination of stable pH for PPO from Malus communis L.

FIGURE 3 Determination of stable pH for PPO from Malus communis L.

TABLE 3 The inhibition effects of metal ions on Hemşin apple (Malus communis L.) PPO activity

TABLE 4 The activation effects of metal ions on Hemşin apple (Malus communis L.) PPO activity

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