富士苹果多酚氧化酶特性研究  

Studies on Properties of Polyphenoloxidase from Fuji Apple

作　　者：于佳[1] 袁翠美[1] 马文秀[1] 周培根 

机构地区：[1]南京林业大学,南京210037

出　　处：《中国野生植物资源》1999年第4期13-16,共4页Chinese Wild Plant Resources

摘　　要：本文从富士苹果中提取和部分纯化多酚氧化酶,并对其特性进行研究。以邻苯二酚为作用底物,该酶最适pH为50,在pH50～80范围内有较高的稳定性。最适温度为30℃,在60℃以上迅速失活。该酶对不同的酚类物质表现出不同的底物专一性,由高至低的趋势依次为邻苯二酚、焦性没食子酸、DL-多巴、酪氨酸,其中对酪氨酸的活力为零。浓度为04mmol/L的VC、L-半胱氨酸及浓度为03mmol/L的亚硫酸氢钠,可完全抑制该酶活性。Polyphenoloxidase was extracted and partially purified from Fuji apple,and some properties were studied.pH optimum was 5.0 with catechol.The enzyme exhibited a rather broad pH stability range from 5.0 to 8.0.Observed optimum temperature from the PPO catechol reaction was 30℃.It was rapidly inactivated above 60℃.The enzyme had different substrate specificities for different phenolic compounds,a maxium activity was shown with catechol,followed by pyrogallol,DL DOPA.The activity with tyrosine was not detected.V C and L cysteine can completely inhibit PPO by the concentration of 0.4mmol/L,but sodium bisulfite only needs 0.3mmol/L.

关 键 词：富士苹果 多酚氧化酶 特性 PH值 温度 苹果 

分 类 号：S661.101[农业科学—果树学] Q946.541[农业科学—园艺学]