National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, PR China.
Bioresour Technol. 2013 Aug;142:415-9. doi: 10.1016/j.biortech.2013.05.045. Epub 2013 May 22.
Yarrowia lipolytica lipase (YLL) demonstrated an (R)-enantiopreference for efficient resolution of (R,S)-2-octanol. The activity, enantioselectivity, the ratio of substrate to enzyme, acetaldehyde tolerance, and operational stability of YLL were improved by an integrated strategy of interfacial activation, bioimprinting, and immobilization. In comparison with the control, both the enzymatic activity and enantioselectivity increased by a factor of 8.85 and 2.75 by the integrated strategy, respectively. Fifty-one percentage of conversion with 220 of enantioselectivity was obtained using the immobilized YLL prepared by the integrated strategy at a ratio of 104 of substrate to enzyme loaded. The immobilized YLL retained 97% of its initial activity without a decrease in enantioselectivity after 10 successive reuse cycles. Together these results will result in a promising strategy with the YYL for efficient resolution of (R,S)-2-octanol in practice.
解脂耶氏酵母脂肪酶（YLL）对（R，S）-2-辛醇表现出（R）-对映体选择性，有利于高效拆分。通过界面激活、生物印迹和固定化的集成策略，提高了 YLL 的活性、对映体选择性、底物与酶的比例、乙醛耐受性和操作稳定性。与对照相比，通过集成策略，酶活性和对映体选择性分别提高了 8.85 倍和 2.75 倍。在底物与酶的比例为 104 的情况下，采用集成策略制备的固定化 YLL 可获得 51%的转化率和 220 的对映体选择性。固定化 YLL 在 10 次连续重复使用后，初始活性保留了 97%，对映体选择性没有下降。这些结果将为在实际中高效拆分（R，S）-2-辛醇提供一种有前途的策略。
