摘要
为实现不溶性酵母β-1,3-葡聚糖的酶法改性增溶,对源于木霉TP-24的β-1,3-葡聚糖酶分离纯化进行研究。结果表明,用含有2%CaCl2的pH5.0醋酸缓冲液浸提固态发酵曲180min,所得粗酶液经2%活性炭脱色、(NH4)2SO4分段盐析、透析浓缩、Sephadex G-100层析分离,获得了高酶活的蛋白峰I和杂蛋白峰II。浓缩含酶组分进行SDS-PAGE电泳分析,酶蛋白呈单一谱带,分子量近似为54.56ku,酶比活力为342.95U/mg,相对于粗酶液纯化了28.67倍,酶的回收率为45.15%。
Crude enzyme solution was precipitated with ammonium sulfate fraction, dialyses, and Sephadex G-100 chromatographic column. The recovery of β-glucanase was almost 45.15%, the specific activity was increased from 11.96 U/mg to 342.95 U/mg. SDS-PAGE of the purified β-Glucanase gave a single stained band at approximately 54.56 ku.
出处
《食品科技》
CAS
北大核心
2008年第7期169-172,共4页
Food Science and Technology