2005Gansu Nongye Daxue xuebaoRequires access

Properties of polyphenol oxidase extracted from potato

Min Li, Lei Liu, Guo Yurong, Chen Derong, Yongcai Li

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Abstract

The discoloration of fresh-cut potato was mainly due to its PPO. The processed potato cultivar Atlantic was used to study its PPO property by spectrocolorimetry. The results showed that the substrate of PPO was o-diphenol, but not hydroquinone, m-diphenol, and mono-phenol. The optimum pH value was 5.5 and the optimum temperature was 5 ℃ for PPO with o-diphenol as a substrate. The chosen inhibitors at 0.01mol/L restrained PPO except NaCl2 and EDTA.

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The discoloration of fresh-cut potato was mainly due to its PPO. The processed potato cultivar Atlantic was used to study its PPO property by spectrocolorimetry. The results showed that the substrate of PPO was o-diphenol, but not hydroquinone, m-diphenol, and mono-phenol. The optimum pH value was 5.5 and the optimum temperature was 5 ℃ for PPO with o-diphenol as a substrate. The chosen inhibitors at 0.01mol/L restrained PPO except NaCl2 and EDTA.

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Available abstract

The discoloration of fresh-cut potato was mainly due to its PPO. The processed potato cultivar Atlantic was used to study its PPO property by spectrocolorimetry. The results showed that the substrate of PPO was o-diphenol, but not hydroquinone, m-diphenol, and mono-phenol. The optimum pH value was 5.5 and the optimum temperature was 5 ℃ for PPO with o-diphenol as a substrate. The chosen inhibitors at 0.01mol/L restrained PPO except NaCl2 and EDTA.

Key concepts: Polyphenol oxidase, Hydroquinone, Phenol, Substrate (aquarium), Cultivar, Chemistry, Catechol, Polyphenol

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