PURIFICATION AND CHARACTERIZATION OF A NOVEL BETA-AGARASE FROM VIBRIO SP AP-2
PURIFICATION AND CHARACTERIZATION OF A NOVEL BETA-AGARASE FROM VIBRIO SP AP-2
复制标题
DOI：
10.1111/j.1432-1033.1990.tb15326.x
复制
发表时间：
1990-01-26
期刊：
影响因子：
--
通讯作者：
KITAMIKADO, M
中科院分区：
文献类型：
--
作者：
AOKI, T;ARAKI, T;KITAMIKADO, M
β-的从一株卟啉分解菌AP-2的培养液中，经硫酸铵沉淀、柱层析、DNase和RNase处理，得到一种琼脂糖酶。最终的酶制剂在聚丙烯酰胺凝胶电泳上似乎是均匀的。该酶的分子量为20 kDa，最适pH为5.5，在pH 4.0-9.0和低于45 ℃的温度下稳定。C.β-琼胶酶是一种新的内切型酶，其水解新琼胶四糖、较大的新琼胶低聚糖和琼脂以产生新琼胶二糖[3，6-脱水-α- L-吡喃半乳糖基-（1 →3）-D-半乳糖]作为主要产物。该酶对K-卡拉胶不起作用。根据《Bergey’s Manual of Systematic Bacteriology》的分类标准，将该菌株归属于弧菌属（Vibrio）。
.beta.-Agarase was purified from the culture fluid of a porphyran-decomposing marine bacterium (strain AP-2) by ammonium sulfate precipitation, successive column chromatography and DNase and RNase treatment. The final enzyme preparation appeared to be homogeneous on polyacrylamide gel electrophoresis. The enzyme had a molecular mass of 20 kDa, a pH optimum of 5.5, and was stable in the pH region 4.0-9.0 and at temperatures below 45.degree. C. The .beta.-agarase was a novel endo-type enzyme which hydrolyzed neoagarotetraose, larger neoagarooligosaccharides and agar to give neoagarobiose [3,6-anhydro-.alpha.-L-galactopyranosyl-(1 .fwdarw. 3)-D-galactose] as the predominant product. The enzyme did not act on K-carrageenan. According to the criteria of Bergey''s Manual of Systematic Bacteriology, the strain was assigned to the genus Vibrio.