Immobilized lipase is a cost-effective biocatalyst for a wide variety of industrial applications, mainly in food, cosmetics, and pharmaceutics due to the huge number of so-called chemically catalyzed reactions of industrial interest that can be replaced by immobilized-enzyme catalysis. In this scenario, there is a growing demand to develop new products, supports, and immobilization protocols, as well as to elucidate the reaction mechanism aiming to cross the barrier imposed by the cost of immobilized lipases. As a large number of researchers have focused their efforts in order to find new applications taking into account new products emerging continuously, it is important to clarify the traditional and alternative process routes using immobilized lipases. In the past decade, almost 5000 research endeavors were reported, and this number continues to rise. This review reports the past 10 years of research work on the techniques used for lipase immobilization proposing a brief introduction about traditional immobilization techniques and an overview of the reactions catalyzed by immobilized lipases with a focus on applications and some products obtained by each pathway.

Understanding the complex behavior and dynamics of cellular membranes is integral to gain insight into cellular division and fusion processes. Bottom-up synthetic cells are as a platform for replicating and probing cellular behavior. Giant polymer vesicles are more robust than liposomal counterparts, as well as having a broad range of chemical functionalities. However, the stability of the membrane can prohibit dynamic processes such as membrane phase separation and division. Here, we present a method for manipulating the membrane of giant polymersomes using a temperature responsive polymer. Upon elevation of temperature deformation and phase separation of the membrane was observed. Upon cooling, the membrane relaxed and became homogeneous again, with infrequent division of the synthetic cells.

1,2-Limonene oxide was synthesized for the first time via epoxidation reactions of (R)-(+)-limonene mediated by a new immobilized preparation with low-cost material from Candida antarctica lipase fraction B (NS 88011). Parameters affecting this reaction were studied, such as enzyme amount, acyl donor concentration, oxidant concentration, (R)-(+)-limonene concentration, reaction time, and temperature. The synthesis was maximized in fed-batch reactors, considering 40 mM (R)-(+)-limonene, 70 mM octanoic acid, and 250 mM H2O2 (35% aqueous solution). NS 88011 and Novozym 435 led to similar results, which makes NS 88011 a promising and low-cost alternative in epoxidation reactions mediated by lipase. The best result in the 1,2-limonene oxide synthesis was 74.92 ± 1.12% of yield at 40 min. In addition, both NS 88011 and Novozym 435 can be used for up to three cycles. Therefore, NS 88011 had a good and viable performance in the epoxidation reactions of the (R)-(+)-limonene and after purification led to a final product with purity >95%.

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