Chen Jech-Wei, Wu Wen-Teng
Department of Chemical Engineering, National Tsing Hua University, Hsinchu 30043, Taiwan, ROC.
J Biosci Bioeng. 2003;95(5):466-9. doi: 10.1016/s1389-1723(03)80046-4.
Immobilized lipase from Candida antarctica was employed to convert triglycerides to biodiesel using alcohol. Immobilized lipase is frequently deactivated by lower alcohols with deactivation being caused by the immiscibility between triglycerides and methanol or ethanol. When the lower alcohol is adsorbed to the immobilized enzyme, the entry of triglycerides is blocked, which causes the reaction to stop. An alcohol with three or more carbon atoms, preferably 2-butanol or tert-butanol, can regenerate the deactivated immobilized enzyme. The present work established that the activity of immobilized lipase could be significantly increased when such alcohols were used for an immersion pretreatment of the enzyme. The activity of the commercially available immobilized enzyme, Novozyme 435, increased about tenfold in comparison to the enzyme not subjected to any pretreatment. Following complete deactivation of the enzyme by methanol, washing with 2-butanol and tert-butanol successfully regenerated the enzyme and restored it to about 56% and 75% of its original activity level, respectively.
利用南极假丝酵母固定化脂肪酶，通过醇将甘油三酯转化为生物柴油。固定化脂肪酶常被低级醇失活，失活是由甘油三酯与甲醇或乙醇之间的不混溶性引起的。当低级醇吸附到固定化酶上时，甘油三酯的进入被阻断，这导致反应停止。具有三个或更多碳原子的醇，优选2-丁醇或叔丁醇，可以使失活的固定化酶再生。目前的工作表明，当使用这些醇对酶进行浸泡预处理时，固定化脂肪酶的活性可以显著提高。与未进行任何预处理的酶相比，市售固定化酶Novozyme 435的活性提高了约十倍。在用甲醇使酶完全失活后，用2-丁醇和叔丁醇洗涤成功地使酶再生，其活性分别恢复到原始活性水平的约56%和75%。
