Key Laboratory of Molecular Biophysics, The Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China.
Bioresour Technol. 2013 Mar;131:179-87. doi: 10.1016/j.biortech.2012.12.092. Epub 2012 Dec 20.
An immobilization strategy was employed to improve activity and operational stability of Yarrowia lipolytica lipase LIP2 (YlLIP2) by using macroporous resins as carrier. D152H, a cation-exchange resin, was the best support. Under the optimized conditions, the immobilization efficiency was 89.81% and the specific activity was 809,751 U/g, being 2.1-fold higher than that of the free lipase. Bioimprinting and interfacial activation were used to further boost the catalytic activity of YlLIP2, respectively enhanced 21.5-fold, 231.2% and 107.2% compared to the free, non-bioimprinted and non-interfacial-activated lipases. The immobilized lipase exhibited much better thermal and pH stability and broader substrate specificity; when used to enrich docosahexaenoic acid (DHA) from Chlorella protothecoides oil, it could increase 1.66-fold of DHA content and show good operational stability. These indicate that the immobilized YlLIP2 offers a promising approach for the enrichment of DHA.
采用固定化策略，使用大孔树脂作为载体，提高解脂耶氏酵母脂肪酶 LIP2(YlLIP2)的活性和操作稳定性。D152H 是一种阳离子交换树脂，是最佳的载体。在优化条件下，固定化效率为 89.81%，比游离脂肪酶的比活提高了 2.1 倍，达到 809751U/g。生物印迹和界面激活分别将 YlLIP2 的催化活性提高了 21.5 倍、231.2%和 107.2%，与游离、非生物印迹和非界面激活的脂肪酶相比。固定化脂肪酶具有更好的热稳定性和 pH 稳定性以及更广泛的底物特异性；用于从小球藻油中富集二十二碳六烯酸（DHA）时，DHA 含量可提高 1.66 倍，且具有良好的操作稳定性。这些表明，固定化的 YlLIP2 为 DHA 的富集提供了一种很有前途的方法。
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