作者: Estrella Núñez-Delicado , Marta Serrano-Megías , Antonio José Pérez-López , José Manuel López-Nicolás
DOI: 10.1016/J.FOODCHEM.2005.09.027
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摘要: Abstract Polyphenol oxidase (PPO) from Napoleon grape was isolated using a two-phase partitioning approach with Triton X-114. The enzyme purified in latent form and could be optimally activated by the presence of 0.2% sodium dodecyl sulphate (SDS) at pH 6.0. In absence SDS, showed maximum activity acid (3.0). kinetically characterized 3.0 6.0 4-tert-butylcatechol (TBC) as substrate. Vm/KM ratio that PPO presents greater affinity for TBC (0.1 min−1) SDS (0.02 min−1). highly heat stable, 80% remaining 70 °C. Selected inhibitors were also studied, tropolone being most active Ki value 27 μM SDS.