2010Science and Technology of Food IndustryRequires access

Study on partial characteristics of polyphenol oxidase in lily bulb

Qun Shen

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Abstract

The activity of PPO was determined by spectrophotometer at 420nm using pyrocatechol as substrate. The effects of temperature,pH and inhibitors were studied. The results showed that the activity of PPO could be inhibited at a temperature higher than 25℃ and the optimum storage temperature was below 10℃. There were two optimum pH,4.0 and 6.0. Inhibitors such as cysteine,ascorbic acid and sodium isoascorbate could inhibit the enzyme activity effectively. But EDTA and citric acid had less effect on inhibiting enzyme activity.

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The activity of PPO was determined by spectrophotometer at 420nm using pyrocatechol as substrate. The effects of temperature,pH and inhibitors were studied. The results showed that the activity of PPO could be inhibited at a temperature higher than 25℃ and the optimum storage temperature was below 10℃. There were two optimum pH,4.0 and 6.0. Inhibitors such as cysteine,ascorbic acid and sodium isoascorbate could inhibit the enzyme activity effectively. But EDTA and citric acid had less effect on inhibiting enzyme activity.

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Available abstract

The activity of PPO was determined by spectrophotometer at 420nm using pyrocatechol as substrate. The effects of temperature,pH and inhibitors were studied. The results showed that the activity of PPO could be inhibited at a temperature higher than 25℃ and the optimum storage temperature was below 10℃. There were two optimum pH,4.0 and 6.0. Inhibitors such as cysteine,ascorbic acid and sodium isoascorbate could inhibit the enzyme activity effectively. But EDTA and citric acid had less effect on inhibiting enzyme activity.

Key concepts: Polyphenol oxidase, Chemistry, Citric acid, Ascorbic acid, Bulb, Substrate (aquarium), Enzyme assay, Enzyme

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