囊状青霉菊粉酶的分离纯化  

Isolation and Purification of Inulinase from Eladia saccula

作　　者：王兴娜[1] 赵洁[1] 朱启忠[1] 

机构地区：[1]山东大学(威海)海洋学院,山东威海264209

出　　处：《资源开发与市场》2014年第7期769-770,774,共3页Resource Development & Market

基　　金：国家科技支撑计划项目(编号:2011BAC02B04)

摘　　要：利用盐析、分子筛和阴离子交换层析处理囊状青霉发酵液,得到菊粉酶Ⅰ、菊粉酶Ⅱ和菊粉酶Ⅲ。经纯化,菊粉酶Ⅰ纯化倍数达4.47倍,酶比活力179.15U/mg;菊粉酶Ⅱ纯化倍数达9.63倍,酶比活力385.45U/mg;菊粉酶Ⅲ纯化倍数达3.72倍,酶比活力149.10U/mg。纯化后的菊粉酶经SDS-PAGE检测,显示均为单一条带,相对分子质量确定为菊粉酶Ⅰ4.08×104、菊粉酶Ⅱ6.08×104、菊粉酶Ⅲ4.13×104,表明囊状青霉产胞外菊粉酶具有三种同工酶成分。Inulinase Ⅰ Ⅱ andⅢwere purified by annonium sulfate precipitation, molecular sieve and ion exchange from fermentation broth of Eladia saccula SA1201. The obtained enzyme Inulinase I was purified 4.47 folds with specific activity of 179.15 U/mg while Inulinase 11 was puri- fied 9.63 folds with specific activity of 385.45 U/mg and Inulinase m was purified 3.72 folds with specific activity of 149.10 U/mg. The purified enzyme was identified with a molecular mass were4.08×104 ,6.08 × 104 and 4.13 × 104 respectively.

关 键 词：囊状青霉 菊粉酶 分离纯化 

分 类 号：Q556.2[生物学—生物化学]