CARBOXYMETHYL-CELLULASE FROM ERWINIA-CHRYSANTHEMI .2. PURIFICATION AND PARTIAL CHARACTERIZATION OF AN ENDO-BETA-1,4-GLUCANASE
CARBOXYMETHYL-CELLULASE FROM ERWINIA-CHRYSANTHEMI .2. PURIFICATION AND PARTIAL CHARACTERIZATION OF AN ENDO-BETA-1,4-GLUCANASE
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DOI：
10.1016/0168-1656(84)90009-9
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发表时间：
1984-01-01
影响因子：
4.1
通讯作者：
CATTANEO, J
中科院分区：
文献类型：
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作者：
BOYER, MH;CHAMBOST, JP;CATTANEO, J
E.当培养物上清液的浓度和/或储存时间增加时，菌株3665具有形成聚集体的显著趋势。在将未浓缩的甘油培养物上清液进行离子交换色谱时，1个主要的内-β-葡聚糖酶被抑制。1，4-葡聚糖酶可以分离与高纯度和部分特征。分子大小为45千道尔顿。等电点为4.3。该酶迅速降低了CM-纤维素的粘度，同时产生的还原糖缓慢增加。它在pH 6.2-7.5之间显示出对CM-纤维素的最高活性。它对磷酸溶胀纤维素等无定形纤维素有显著的水解能力。降解产物主要为纤维二糖和纤维三糖。它对微晶纤维素表现出非常低的活性。葡萄糖和纤维二糖对其抗CM-纤维素活性影响不显著。
The extracellular CM-cellulase of E. chrysanthemi, strain 3665, had a marked tendency to form aggregates when concentration and/or storage time of culture supernatant were increased. In submitting an unconcentrated glycerol culture supernatant to ion exchange chromatography, 1 major endo-.beta.-1,4-glucanase could be isolated with a high degree of purity and partially characterized. The molecular size was 45 kilodaltons. The isoelectric point was 4.3. The enzyme rapidly decreased the viscosity of CM-cellulose with a slow increase in the reducing sugars produced. It displayed its highest activity towards CM-cellulose at a pH between 6.2-7.5. It had a significant capacity to hydrolyze amorphous cellulose such as phosphoric acid-swollen cellulose. The major products of this degradation were cellobiose and cellotriose. It exhibited a very low activity on microcrystalline cellulose. Glucose and cellobiose did not affect significantly its activity against CM-cellulose.