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- W4285494908 abstract "Abstract In the current study, polyphenol oxidase (PPO), responsible for enzymatic browning in fruits, was purified from Posof Badele apple (PB) ( Malus domestica L. ) in two steps as acetone precipitation and affinity chromatography. After purification, the purity of PBPPO was checked by using SDS-PAGE. It was figured out that PBPPO had maximum activity at pH 6.0 and 10 °C and it was stable at pH 5.5 and temperatures of 0–30 °C. Besides, it was determined that Al 3+ and Cu 2+ metal ions activated the enzyme and the PBPPO was strongly inhibited by ascorbic acid with a K i constant of 1.67 ± 0.35 µM. Inhibitor-enzyme interactions were examined by molecular docking studies and it was revealed that ascorbic acid had the lowest docking score of −6.54 kcal/mol. We wanted to draw attention to the PB apple, which is red inside as well as outside and very rich in terms of nutrient content." @default.
- W4285494908 created "2022-07-15" @default.
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- W4285494908 date "2022-07-01" @default.
- W4285494908 modified "2023-09-27" @default.
- W4285494908 title "Purification and characterization of catechol oxidase from Posof Badele apple (<i>Malus domestica L</i>): <i>in vitro</i> and <i>in silico</i> studies" @default.
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- W4285494908 doi "https://doi.org/10.1515/ijfe-2022-0022" @default.
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