Regeneration of immobilized Candida antarctica lipase for transesterification
Regeneration of immobilized Candida antarctica lipase for transesterification
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DOI：
10.1263/jbb.95.466
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发表时间：
2003-05-01
影响因子：
2.8
通讯作者：
Wu, WT
中科院分区：
文献类型：
--
作者：
Chen, JW;Wu, WT
采用固定化脂肪酶催化甘油三酸酯转化为生物柴油。固定化脂肪酶经常被低级醇失活，其中失活是由甘油三酯与甲醇或乙醇之间的不相容性引起的。当低级醇被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。具有三个或更多个碳原子的醇，优选2-丁醇或叔丁醇，可以再生失活的固定化酶。本工作建立了固定化脂肪酶的活力可以显着提高时，这些醇用于浸渍预处理的酶。市售固定化酶Novozyme 435的活性与未进行任何预处理的酶相比增加约10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，并分别使其恢复到其原始活性水平的约56%和75%。
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.