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机构地区:[1]西南大学生命科学学院淡水鱼类资源与生殖发育教育部重点实验室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》2016年第5期126-131,共6页Food Science
基 金:重庆市科委重点攻关项目(CSTC2011AB1027)
摘 要:将新鲜牛肾匀浆后,经由缓冲液提取,正丁醇除脂,硫酸铵分级沉淀,CM-Sepharose阳离子交换层析,Superdex-200凝胶过滤层析后得到电泳纯的牛肾溶菌酶。结果表明:该酶比活力为15 145.63 U/mg,回收率为29.13%,纯化倍数为231.05;分子质量约12.66 k D,为单亚基酶。最适反应温度为65℃,在65℃以下较稳定;最适p H 9.0,p H值在3.0~9.0范围内稳定性较好;测得最适条件下牛肾溶菌酶对溶壁微球菌的Km值为0.399μg/m L;甲醇、乙醇、异丙醇和硫氰化钾(KSCN)对该酶有激活作用;十二烷基硫酸钠、Pb2+、Ag+对该酶有明显抑制作用。Electrophoretically pure lysozyme from bovine kidney was obtained through homogenization, buffer extraction, butanol degreasing, ammonium sulfate fractionation precipitation, CM-Sepharose ion-exchange chromatography and Superdex-200 gel filtration chromatography. Results showed that the specific activity of the purified lysozyme was 15 145.63 U/mg with a recovery rate of 29.13% and the enzyme was purified 231.05 folds. The molecular weight of the lysozyme was approximately 12.66 k D, which consisted of a single subunit. The optimum temperature of the enzyme was 65 ℃ and it was stable at temperatures below 65 ℃; the optimum p H of this enzyme was 9.0 and it was stable in the range of p H 3.0–9.0. Its Km towards micrococcus lysodeikticus was 0.399 μg/m L. The enzyme activity was enhanced by methanol, ethanol, isopropanol and KSCN, and inhibited by SDS, Pb2+, and Ag+.
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