Enzyme-loaded water-in-oil Pickering emulsion is a promising system for biphasic catalytic reactions. In this paper, we report on oriented enzyme immobilization at the oil/water interface in a Pickering emulsion, in which CHO-Janus silica nanoparticles (CHO-JNPs) are utilized as a stabilizer of the emulsion and support for the enzyme to enhance both catalytic activity and recyclability. The catalytic performance of this immobilized enzyme (lipase from Candida sp.) was evaluated by esterification of hexanoic acid and 1-hexanol in a water/heptane biphasic medium. The results show that the specific catalytic activity of the immobilized enzyme (33.2 U mL^–1) was 6.5 and 1.4 times higher than that of free enzyme (5.1 U mL^–1) and encapsulated enzyme in the liquid core (23.3 U mL^–1), respectively. Moreover, the immobilized enzyme demonstrated good stability and recyclability, retaining 75% of its activity after 9 cycles. We expect that oriented enzyme immobilization at the oil/water interface will be an important strategy for enhancing catalytic performance in Pickering emulsions.

中文翻译：

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定向固定在油/水界面的酶增强了Pickering乳液的催化活性和可回收性

负载酶的油包水皮克林乳液是用于双相催化反应的有前途的系统。在本文中，我们报道了在Pickering乳液中油/水界面处定向酶的固定化，其中CHO-Janus二氧化硅纳米颗粒（CHO-JNPs）被用作乳液的稳定剂和酶的支持物，以增强催化作用。活性和可回收性。通过在水/庚烷双相介质中己酸和1-己醇的酯化来评价该固定化酶（来自假丝酵母的脂肪酶）的催化性能。结果表明，固定化酶（33.2 U mL ^–1）的比催化活性分别是游离酶（5.1 U mL ^–1）的6.5和1.4倍。）和包埋在液芯中的酶（分别为23.3 U mL ^–1）。此外，固定化酶表现出良好的稳定性和可回收性，在9个循环后仍保留了其活性的75％。我们期望将取向的酶固定在油/水界面将是提高Pickering乳液催化性能的重要策略。