重组微小毛霉凝乳酶的分离与纯化  

Separation and purification of recombinant Mucor pusillus rennet

作　　者：李玉秋[1] 王景会[1] 李铁柱[1] 李倬林[1] 杨贞耐[1] 

机构地区：[1]吉林省农业科学院农产品加工研究中心,吉林长春130033

出　　处：《中国酿造》2010年第10期19-22,共4页China Brewing

基　　金：国家高技术研究与发展计划‘863计划’(2006AA10Z306);现代农业产业技术体系建设专项资金资助(nycytx-0502)

摘　　要：用硫酸铵分级沉淀分离提取重组微小毛霉凝乳酶(GS115/pPICZαA-Mucor pusillus rennet),经过Sephadex G-75分子筛和DEAE-52离子交换2次柱层析纯化,酶的比活力由2078U/mg提高为10526U/mg,纯化倍数超过5倍,纯化的重组凝乳酶经SDS-PAGE电泳分析纯化的重组凝乳酶分子质量约为46kDa。Recombinant rennet expressed in Pichia pastoris （GS115/pPIC ZαA-Mucor pusillus rennet） was partially purified and characterized. Recombinant rennet was obtained by fractional precipitation with ammonia sulfate, followed by the chromatography of DEAE-52 and Sephadex G-75. It was purified over five fold and the specific activity of the enzyme preparation increased from 2078 U/mg to 10526 U/mg. The purified enzyme had a molecular mass of 46 kDa as showed by SDS-PAGE.

关 键 词：重组微小毛霉凝乳酶 分离 纯化 

分 类 号：Q814.3[生物学—生物工程]