Extraction, Purification, and Characterization of Olive (<i>Olea europaea</i> L., cv. Chemlal) Polyphenol Oxidase.

ABSTRACT: Among fruits susceptible to enzymatic browning, olive polyphenol oxidase (OePPO) stood out as being unisolated from a natural source until this study, wherein we successfully purified and characterized the enzyme. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of heated and nonheated OePPO revealed distinct molecular weights of 35 and 54 kDa, respectively, indicative of its oligomeric nature comprising active and C-terminal subunits. OePPO displayed latency, fully activating with 5 mM SDS under optimal conditions of pH 7.5 and 15 °C. The enzyme demonstrated monophenolase activity and showcased the highest efficiency toward hydroxytyrosol. Despite its low optimal temperature, OePPO exhibited high thermal resistance, maintaining stability up

SUBMITTER: Derardja AE 

PROVIDER: S-EPMC10870767 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature