鸭卵清溶菌酶的分离纯化及性质  

Isolation, Purification and Characterization of Lysozyme from Duck Egg White

作　　者：成丽丽[1] 邓玉[1] 赵芯[1] 敬海明[1] 唐云明[1] 

机构地区：[1]西南大学生命科学学院,重庆市甘薯工程研究中心,三峡库区生态环境教育部重点实验室,重庆400715

出　　处：《食品科学》2012年第17期198-202,共5页Food Science

基　　金：重庆市科委重点攻关项目(CSTC2011AB1027)

摘　　要：通过硫酸铵的分级沉淀、CM-Sepharose阳离子交换层析、Superdex-200凝胶过滤层析等步骤,从鸭卵清中获得电泳纯的溶菌酶,该酶的比活力达到33687.26U/mg,纯化倍数为109.44,回收率为28.00%。测得该酶分子质量约为14.82kD,对溶壁微球菌的最适反应温度为50℃,最适pH值为7,且在50℃以下及pH5～9有较好的稳定性,同时在最适条件下测得其Km值为0.0864mg/mL。Fe2+、Mg2+、Mn2+等金属离子对该酶有较强的抑制作用,而Zn2+、Cu2+、Co2+对该酶有一定的激活作用。Lysozyme was purified from duck egg white by ammonium sulfate precipitation, CM-Sepharose chromatography and Superdex-200 gel filtration chromatography. The specific activity, yield and purification fold of lysozyme were 33687.26 U/mg, 28.00% and 109.44, respectively. The molecular weight of lysozyme was estimated as approximately 14.82 kD. The optimal pH and temperature against Micrococcus lysodlekticus were 7.0 and 50 ℃, respectively. The enzyme was stable at temperatures below 50 ℃ and pH 5.0--9.0. The apparent K＋ determined by Lineweaver-Burk method under the optimum conditions was 0.0864 mg/mL. The activity of lysozyme was inhibited by Mg2＋, Mn2＋, or Fe2＋, and enhanced by Zn2＋, Cu2＋ or Co2＋.

关 键 词：鸭卵清 溶菌酶 分离纯化 性质 

分 类 号：Q814.1[生物学—生物工程]