Purification and some properties of polyphenoloxidase in eggplant (Solanum melongena)
Purification and some properties of polyphenoloxidase in eggplant (Solanum melongena)
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茄子中多酚氧化酶的纯化及其一些性质
DOI：
10.1002/jsfa.2740460111
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发表时间：
1988
影响因子：
4.1
通讯作者：
T. Tono
中科院分区：
文献类型：
--
作者：
S. Fujita;T. Tono
茄子多酚氧化酶（EC 1.10.3.1）经硫酸铵分级、DEAE-Cellulofine和DEAE-Toyopolymer层析和SephadexG-100凝胶过滤纯化。酶纯化了约110倍，回收率为5%。纯化的酶更快地氧化绿原酸（5-caffeoylquinic酸，IUPAC）比其他10种底物使用。发现该酶的Km值相对于绿原酸为0·50 mM;该酶的最适pH为约4，酶稳定性在pH 5和8之间。在75°C热处理30 min或80°C热处理5 min后，酶完全失活。焦亚硫酸钠、氰化钾和氟化钠对酶活性有明显的抑制作用。
Polyphenoloxidase (EC 1.10.3.1) in eggplant (Solatium melongena L) was purified by ammonium sulphate fractionation, DEAE-Cellulofine and DEAE-Toyopearl chromatography and Sephadex G-100 gel filtration. The enzyme was purified about 110-fold with a recovery of 5%. The purified enzyme more quickly oxidised chlorogenic acid (5-caffeoylquinic acid, IUPAC) than 10 other substrates used. The Km value for the enzyme was found to be 0·50 mM with respect to chlorogenic acid; the optimum pH of the enzyme was about 4 with enzyme stability between pH 5 and 8. The enzyme was completely inactivated after heat treatment at 75°C for 30 min or 80°C for 5 min. Sodium metabisulphite, potassium cyanide and sodium fluoride markedly inhibited the enzyme activity.