Kobayashi M, Matsuda K
Biochim Biophys Acta. 1980 Jul 10;614(1):46-62. doi: 10.1016/0005-2744(80)90166-7.
Multiple forms of dextransucrase (sucrose:1.6-alpha-D-glucan 6-alpha-D-glucosyltransferae EC 2.4.1.5) from Leuconostoc mesenteroides NRRL B-512F strain were shown by gel filtraton and electrophoretic analyses. Two components of enzyme, having different affinities for dextran gel, were separated by a column of Sephadex G-100. The major component voided from the Sephadex column was treated with dextranase and purified to an electrophoretically homogeneous state. The ]urified enzyme had a molecular weight of 64 000-65 000, pI value of 4.1, and 17% of carbohydrate in a molecule. EDTA showed a characteristic inhibition on the enzyme while stimulative effects were observed by the addition of exogenous dextran to the incubation mixture. The enzyme activity was stimulated by various dextrans and its Km value was decreased with increasing concentration of dextran. The purified enzyme showed no affinity for a Sephadex G-100 gel, and readily aggregated after the preservation at 4 degrees C in a concentrated solution.
通过凝胶过滤和电泳分析表明，肠系膜明串珠菌NRRL B - 512F菌株存在多种形式的葡聚糖蔗糖酶（蔗糖：1,6-α-D-葡聚糖6-α-D-葡糖基转移酶，EC 2.4.1.5）。用Sephadex G - 100柱分离出对葡聚糖凝胶具有不同亲和力的两种酶组分。从Sephadex柱中最先流出的主要组分用葡聚糖酶处理并纯化至电泳纯状态。纯化后的酶分子量为64000 - 65000，pI值为4.1，分子中碳水化合物含量为17%。EDTA对该酶表现出特异性抑制作用，而向孵育混合物中添加外源葡聚糖则观察到刺激作用。各种葡聚糖可刺激该酶活性，其Km值随葡聚糖浓度增加而降低。纯化后的酶对Sephadex G - 100凝胶无亲和力，在4℃浓缩溶液中保存后容易聚集。
