用于有机溶剂中的丝氨酸蛋白酶的溶胶-凝胶固定化。

Sol-gel immobilization of serine proteases for application in organic solvents.

作者信息

van Unen D J, Engbersen J F, Reinhoudt D N

机构信息

Laboratory of Supramolecular Chemistry and Technology, MESA Research Institute, University of Twente, P.O. Box 217, 7500 AE Enschede, The Netherlands.

出版信息

Biotechnol Bioeng. 2001 Oct 20;75(2):154-8. doi: 10.1002/bit.1173.

DOI:10.1002/bit.1173

PMID:11536137

Abstract

The serine proteases alpha-chymotrypsin, trypsin, and subtilisin Carlsberg were immobilized in a sol-gel matrix and the effects on the enzyme activity in organic media are evaluated. The percentage of immobilized enzyme is 90% in the case of alpha-chymotrypsin and the resulting specific enzyme activity in the transesterification of N-acetyl-L-phenylalanine ethyl ester with 1-propanol in cyclohexane is 43 times higher than that of a nonimmobilized lyophilized alpha-chymotrypsin. The activities of trypsin and subtilisin Carlsberg are enhanced with 437 and 31 times, respectively. The effect of immobilization on the enzyme activity is highest in hydrophobic solvents.

摘要

将丝氨酸蛋白酶α-胰凝乳蛋白酶、胰蛋白酶和枯草杆菌蛋白酶固定在溶胶-凝胶基质中，并评估其对有机介质中酶活性的影响。对于α-胰凝乳蛋白酶，固定化酶的百分比为90%，在环己烷中N-乙酰-L-苯丙氨酸乙酯与1-丙醇的酯交换反应中，所得的比酶活性比未固定化的冻干α-胰凝乳蛋白酶高43倍。胰蛋白酶和枯草杆菌蛋白酶的活性分别提高了437倍和31倍。在疏水溶剂中，固定化对酶活性的影响最大。