Manners D J, Wilson G
Biochem J. 1973 Sep;135(1):11-8. doi: 10.1042/bj1350011.
A commercial enzyme preparation, originally obtained from a Flavobacterium(Cytophaga), was fractionated by continuous electrophoresis, giving a protein fraction which hydrolysed laminarin, carboxymethylpachyman, barley beta-glucan, lichenin and cellodextrin in random fashion. This enzymic activity was not very stable. Ion-exchange chromatography and molecular-sieve chromatography on Bio-Gel P-60 showed that this activity was due to two specific beta-glucanases, an endo-beta-(1-->3)-glucanase and an endo-beta-(1-->4)-glucanase. The two enzymes occur in both high- and low-molecular-weight forms, the latter endo-beta-(1-->3)-glucanase having a molecular weight of about 16000.
一种最初从黄杆菌(噬细胞菌属)获得的商业酶制剂,通过连续电泳进行分级分离,得到一种能以随机方式水解海带多糖、羧甲基茯苓聚糖、大麦β-葡聚糖、地衣多糖和纤维糊精的蛋白质级分。这种酶活性不是很稳定。在Bio-Gel P-60上进行离子交换色谱和分子筛色谱分析表明,这种活性是由两种特异性β-葡聚糖酶引起的,一种是内切β-(1→3)-葡聚糖酶,另一种是内切β-(1→4)-葡聚糖酶。这两种酶都有高分子量和低分子量形式,后者的内切β-(1→3)-葡聚糖酶分子量约为16000。