Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, China.
Molecules. 2013 Jan 16;18(1):1138-49. doi: 10.3390/molecules18011138.
The enzymatic performance of trypsin in hydrolysis of N-α-benzoyl-DL-arginine-4-nitroanilide (BAPNA) was improved by adsorption on Santa Barbara Amorphous (SBA)-15 mesoporous silica. The optimal immobilization conditions were screened and the properties of immobilized enzyme have also been studied. Under the optimal conditions, the immobilized trypsin displays maximum specific activity (49.8 μmol/min/g). The results also indicate that the immobilized trypsin exhibits better storage stability.
通过吸附在 Santa Barbara Amorphous (SBA)-15 介孔硅上，胰蛋白酶在 N-α-苯甲酰-DL-精氨酸-4-硝基苯胺（BAPNA）水解中的酶催化性能得到了提高。筛选了最佳固定化条件，并研究了固定化酶的性质。在最佳条件下，固定化胰蛋白酶显示出最大的比活性（49.8 μmol/min/g）。结果还表明，固定化胰蛋白酶具有更好的储存稳定性。
