Operational stability of high initial activity protease catalysts in organic solvents
Operational stability of high initial activity protease catalysts in organic solvents
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DOI：
10.1021/bp020098g
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发表时间：
2002-11-01
影响因子：
2.9
通讯作者：
Halling, PJ
中科院分区：
文献类型：
--
作者：
Fernandes, JFA;Halling, PJ
首次研究了交联酶晶体（CLECs）在有机介质中的操作稳定性。虽然这些催化剂显示出高的初始比活性，但它们在连续流动下在最初的4小时内迅速地失活，损失超过50%的初始活性。此外，当返回到水性介质时，失活是不可逆的。同样的快速失活发生在吸附的蛋白酶制剂中，这些蛋白酶制剂显示出类似的高初始比活性（枯草杆菌蛋白酶和α-胰凝乳蛋白酶的丙醇冲洗的酶制剂（PREP））。
The first studies on the operational stability of cross-linked enzyme crystals (CLECs) in organic media are described. Although these catalysts display high initial specific activity, they inactivate rapidly, losing more than 50% of the initial activity within the first 4 h under continuous flow. Furthermore, the inactivation is not reversible when returned to an aqueous medium. The same rapid inactivation occurs with adsorbed protease preparations that show similar high initial specific activity (propanol-rinsed enzyme preparations (PREPs) of subtilisin and alpha-chymotrypsin).