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Articles

Investigation of a wild pear species (Pyrus elaeagnifolia subsp. Elaeagnifolia Pallas) from Antalya, Turkey: polyphenol oxidase properties and anti-xanthine oxidase, anti-urease, and antioxidant activity

Pages 585-595 | Received 12 Nov 2015, Accepted 24 Mar 2016, Published online: 02 Oct 2016

Figures & data

Table 1. Substrate specificity of the PePPO.

Figure 1. Gel revealed by incubating with 100 mM of L-Dopa as a substrate of polyphenol oxidase.

Figure 1. Gel revealed by incubating with 100 mM of L-Dopa as a substrate of polyphenol oxidase.

Figure 2. (a) pH-activity profile for PePPO; (b) pH stability of PePPO; (c) Optimum temperature of PePPO; and (d) Thermal stability of PePPO.

Figure 2. (a) pH-activity profile for PePPO; (b) pH stability of PePPO; (c) Optimum temperature of PePPO; and (d) Thermal stability of PePPO.

Table 2. The IC50 values of some inhibitors.

Table 3. Effect of various metal ions on PePPO activity.

Table 4. Antioxidant activity values of AePep.

Table 5. Each enzyme IC50 and % inhibition values of the AePep samples.

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