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

Jhonatam de Oliveira Carvalho; José Fábio França Orlanda

doi:10.1016/j.foodchem.2017.04.101

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

Food Chem. 2017 Oct 15:233:159-163. doi: 10.1016/j.foodchem.2017.04.101. Epub 2017 Apr 19.

Authors

Jhonatam de Oliveira Carvalho¹, José Fábio França Orlanda²

Affiliations

¹ Federal Institute of Education, Science and Technology of Maranhão, Açailândia Campus, 65.930-000, Açailândia, MA, Brazil.
² Laboratory of Environmental Biotechnology (LABITEC), Maranhão Tocantina Region State University (UEMASUL), Center for Natural, Maths and Technological Sciences (CECENT), 65.901-480 Imperatriz, MA, Brazil. Electronic address: josefabio@uemasul.edu.br.

PMID: 28530561
DOI: 10.1016/j.foodchem.2017.04.101

Abstract

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.

Keywords: Enzyme activity; Enzyme stability; Polyphenol oxidase.

MeSH terms

Arecaceae*
Catechol Oxidase
Enzyme Stability
Fruit
Hot Temperature
Hydrogen-Ion Concentration
Kinetics
Plant Extracts

Substances

Plant Extracts
Catechol Oxidase