文献类型：期刊文献

中文题名：固定化唾液酸酶催化多唾液酸神经节苷脂制备GM1

英文题名：Application of Immobilized Sialidase to Preparation of GM1 from Gangliosides

作者：沈丹虹[1];彭彦峰[1];王学东[1];魏东芝[1]

机构：[1]华东理工大学生物反应器工程国家重点实验室,上海200237

年份：2012

卷号：43

期号：10

起止页码：821

中文期刊名：中国医药工业杂志

外文期刊名：Chinese Journal of Pharmaceuticals

收录：CSTPCD;;北大核心:【北大核心2011】；CSCD:【CSCD2011_2012】；

语种：中文

中文关键词：乳酪短杆菌;唾液酸酶;固定化;单唾液酸四己糖神经节苷脂

外文关键词：Brevibacterium casei; sialidase; immobilization; monosialotetrahexosylganglioside

摘要：对一种来源于乳酪短杆菌的唾液酸酶进行固定化并考察其催化性质。使用HZ841大孔吸附树脂固定化唾液酸酶,确定固定化条件:15～25℃,pH 5.4,每克载体以酶液15 ml(30 u/ml)固定化16 h。固定化唾液酸酶在pH 5～9范围内活性良好,40℃时酶活力半衰期由30 min延长至2 h以上,其pH稳定性和热稳定性较游离酶均有所提高。利用固定化唾液酸酶转化多唾液酸神经节苷脂为单唾液酸四己糖神经节苷脂(GM1),TLC法测得催化前后GM1在神经节苷脂混合物中的相对含量由9%提高到60%。
Immobilization and the catalytic properties of sialidase from Brevibacterium casei were investigated. Macroporous adsorption resin HZ841 was adopted for the immobilization of sialidase. The optimal immobilized condition was determined as follows： load of sialidase 450 u/g support, at 15 - 25 ℃, pH 5.4 and the immobilization time of 16 h. The pH stability and thermostability of the immobilized sialidase were improved. After biotransformation of gangliosides into monosialotetrahexosylganglioside （GM1） via immobilized sialidase, the relative content of GM 1 was increased from 9 % to 60 % in the crude gangliosides.