Heat stability and effect of pH on enzyme activity of polyphenol oxidase in buriti (Mauritia flexuosa Linnaeus f.) fruit extract

- Thermal stability and effect of pH on the enzyme polyphenoloxidase from fruit of Mauritia flexuosa Linnaeus f.
- The enzyme had optimum temperaturet 35 °C and was relatively stable at 77 °C, with 59.93% loss of activity.
- The results suggest that Mauritia flexuosa Linnaeus f. has potential source of enzyme polyphenoloxidase.

Polyphenol oxidase (PPO) was extracted and characterized from ripe fruit of Mauritia flexuosa. Buriti PPO showed optimum activity at pH 7.0 and 35 °C, with complete inactivation in between 2.0 ≤ pH > 10, using catechol as substrate. The enzyme had optimum temperaturet 35 °C and was relatively stable at 77 °C, with 59.93% loss of activity. These results demonstrate that the enzyme has heat stability at higher temperatures and the possibility of being used to construct biosensors and other analytical methods in various fields of science.