Department of Bioengineering, School of Chemical Engineering, Hebei University of Technology, Tianjin 300130, China.
N Biotechnol. 2010 Feb 28;27(1):53-8. doi: 10.1016/j.nbt.2009.12.001. Epub 2009 Dec 11.
Candida antarctica lipase B (CALB) was immobilized on the macroporous resin by physical adsorption in organic medium. The immobilization was performed in 5 mL isooctane, and the immobilization conditions were optimized. The results were achieved with the mass ratio of lipase to support 1:80, the buffer of pH 6.0, initial addition of PBS 75 microL, and immobilization time of two hours at 30 degrees C. Under the optimal conditions, the activity recovery was 83.3%. IM-CALB presented enhanced pH and thermal stability compared to the free lipase, and showed comparable stability with the commercial Novozym 435, after 7 times repeated use for catalyzing the synthesis of ethyl lactate, 56.9% of its initial activity was retained, and only 24.7% was retained when used for catalyzing the hydrolysis of olive oil.
南极假丝酵母脂肪酶 B(CALB)通过物理吸附在有机介质中固定在大孔树脂上。在 5 毫升异辛烷中进行固定化,优化了固定化条件。在脂肪酶与载体质量比为 1:80、缓冲液 pH 值 6.0、初始 PBS 添加量为 75 微升、30°C 下固定化 2 小时的条件下,获得了最佳结果。在最佳条件下,活性回收率为 83.3%。与游离脂肪酶相比,IM-CALB 表现出增强的 pH 值和热稳定性,并且在重复使用 7 次催化合成乳酸乙酯后,其稳定性与商业 Novozym 435 相当,保留了其初始活性的 56.9%,而用于催化橄榄油水解时仅保留了 24.7%。