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鸭卵清溶菌酶的分离纯化及性质
引用本文:成丽丽,邓玉,赵芯,敬海明,唐云明.鸭卵清溶菌酶的分离纯化及性质[J].食品科学,2012,33(17):198-202.
作者姓名:成丽丽  邓玉  赵芯  敬海明  唐云明
作者单位: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
基金项目: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。

关 键 词:鸭卵清  溶菌酶  分离纯化  性质  
收稿时间:2011-07-29

Isolation, Purification and Characterization of Lysozyme from Duck Egg White
CHENG Li-li,DENG Yu,ZHAO Xin,JING Hai-ming,TANG Yun-ming.Isolation, Purification and Characterization of Lysozyme from Duck Egg White[J].Food Science,2012,33(17):198-202.
Authors:CHENG Li-li  DENG Yu  ZHAO Xin  JING Hai-ming  TANG Yun-ming
Affiliation:(Key Laboratory of the Three Gorges Reservoir Region’s Eco-Environment,Ministry of Education,Chongqing Sweet-potato Engineering Research Center,School of Life Science,Southwest University,Chongqing 400715,China)
Abstract: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 Km 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+.
Keywords:duck egg white  lysozyme  isolation and purification  characterization  
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