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.
出处
《中国医药工业杂志》
CAS
CSCD
北大核心
2012年第10期821-823,841,共4页
Chinese Journal of Pharmaceuticals
