作　　者： ; ; ; ; ;

机构地区： 华南农业大学食品学院

出　　处： 《食品工业科技》 2011年第10期353-357,共5页

摘　　要： 以菠萝茎为原料,利用微滤除杂、超滤浓缩分离得菠萝蛋白酶浓缩液,再通过硫酸铵法进行沉淀,最后进行真空冷冻干燥制取菠萝蛋白粗酶;而为了验证其酶学性质,采用SephadexG-100柱层析和DEAE-52离子交换层析制得纯度较高的菠萝蛋白酶。结果表明:菠萝茎打浆后原液通过微滤除杂、超滤浓缩,再采用90%硫酸铵沉淀等工序后,纯化倍数达1.44,是目前工厂制酶的1.19倍,酶活收率与原液相比只降低9%,具有工业化生产的优越性;经SephadexG-100柱层析和DEAE-52柱层析后,达到电泳纯,可满足医药用酶所需,存在很好的市场应用价值;且该菠萝蛋白酶的酶学性质与有关报道基本一致,最适反应pH在5～6之间,最适温度60℃,重金属离子如Cu2+、Fe2+、Pb2+等对菠萝茎蛋白酶活抑制较大,而Na+、K+、Ca2+则表现出不同程度的激活作用。 A industrial production process for extraction of bromelain was studied. First,the concentrate of bromelain was enriched from the pineapple stalks by the ways of microfiltration and ultrafiltration. And then,the enzyme extracts were precipitated by the ammonium sulfate precipitation. Last,the bromelain was dehydrated by the vacuum freeze drying. On the basis of these,the high purity of bromelain was produced by the Sephadex G-100 and DEAE-52 ion column chromatography and its characterization was studied. The results showed that after the front process,1.44-fold purified bromelain was achieved,which purity than the old process was 1.19 times. The high purity of bromelain that was produced by the Sephadex G-100 and DEAE-52 ion column chromatography could reach the electrophoresis pure. This purified bromelain can satisfy the demand in medical treatment field,so it had higher market value. And the result of the characterization of this bromelain was consistent with earlier reports. The optimum pH and temperature of the purified enzyme were 5-6 and 60℃. The purified enzyme was inhibition by heavy metal ions such as Cu^2＋,Fe^2＋,Pb^2＋,and activation by the Na^＋,K^＋,Ca^2＋.

关 键 词： 菠萝茎蛋白酶 提取 纯化 酶学性质

领　　域： [轻工技术与工程] [轻工技术与工程]