Partial Purification and Characterization of Polyphenol Oxidase from Banana (Musa sapientum L.) Peel
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- 作者：Chang-Peng Yang ; Shuji Fujita ; Koei Kohno ; Akiko Kusubayashi ; MD. Ashrafuzzaman ; and Nobuyuki Hayashi
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：2001
- 出版时间：March 2001
- 年：2001
- 卷：49
- 期：3
- 页码：1446 - 1449
- 全文大小：64K
- 年卷期：v.49,no.3(March 2001)
- ISSN：1520-5118
文摘
Polyphenol oxidase (EC 1.10.3.1, o-diphenol: oxygen oxidoreductase, PPO) of banana (Musasapientum L.) peel was partially purified about 460-fold with a recovery of 2.2% using dopamine assubstrate. The enzyme showed a single peak on Toyopearl HW55-S chromatography. However, twobands were detected by staining with Coomassie brilliant blue on PAGE: one was very clear, andthe other was faint. Molecular weight for purified PPO was estimated to be about 41 000 by gelfiltration. The enzyme quickly oxidized dopamine, and its Km value (Michaelis constant) for dopaminewas 3.9 mM. Optimum pH was 6.5 and the PPO activity was quite stable in the range of pH 5-11for 48 h. The enzyme had an optimum temperature at 30 
C and was stable up to 60 C after heattreatment for 30 min. The enzyme activity was strongly inhibited by sodium diethyldithiocarbamate,potassium cyanide, L-ascorbic acid, and cysteine at 1 mM. Under a low buffer capacity, the enzymewas also strongly inhibited by citric acid and acetic acid at 10 mM.Keywords: Banana (Musa sapientum L.) peel; enzymatic browning; polyphenol oxidase; purification;characterization
C and was stable up to 60 C after heattreatment for 30 min. The enzyme activity was strongly inhibited by sodium diethyldithiocarbamate,potassium cyanide, L-ascorbic acid, and cysteine at 1 mM. Under a low buffer capacity, the enzymewas also strongly inhibited by citric acid and acetic acid at 10 mM.Keywords: Banana (Musa sapientum L.) peel; enzymatic browning; polyphenol oxidase; purification;characterization