title: Purification and characterization of polyphenol oxidase from jackfruit ( Artocarpus heterophyllus ) bulbs.
abstract: Polyphenol oxidase (PPO) from jackfruit bulb was purified through acetone precipitation, ion-exchange column, and gel filtration column. PPO was a dimer with the molecular weight of 130 kDa determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration. The Km was 8.3 and 18.2 mM using catechol and 4-methylcatechol as substrates, respectively. The optimum pH was 7.0 (catechol as the substrate) or 6.5 (4-methylcatechol as the substrate). The optimum temperature was 8 °C. The enzyme was stable below 40 °C. The activation energy (Ea) of heat inactivation was estimated to be 103.30 kJ/mol. The PPO activity was activated by Mn(2+), SDS, Tween-20, Triton X-100, citric acid, and malic acid but inhibited by K(+), Zn(2+), Mg(2+), Ca(2+), Ba(2+), cetyl trimethyl ammonium bromide (CTAB), kojic acid, tropolone, glutathione (GSH), cysteine (Cys), and ascorbic acid (AA). Cys and AA were effective to reduce browning of jackfruit bulbs during the storage at 8 °C for 15 days.
authors: College of Biotechnology, and ‡Institute of Biomedicine, Guilin Medical University , Guilin 541004, People's Republic of China.
authors: Yi-Ming
authors: YM
authors: Tao
authors: Le-Yi
authors: LY
authors: Yao
authors: Qiu-Yan
authors: QY
authors: Qin
authors: Wang
authors: W
authors: Shen
mesh_terms: D031622:Artocarpus / Q000737:chemistry / Q000201:enzymology*; D004156:Catechol Oxidase / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D004795:Enzyme Stability; D007700:Kinetics; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D010940:Plant Proteins; D004156:Catechol Oxidase