Enzymes are useful tools for biotransformations in the food and bioprocessing industries; however, their instability to extreme environments, and inability to be reused has hindered their widespread implementation. Hierarchical structures have been researched to stabilize enzymes, but recovery remains a challenge. Lipase is an enzyme of interest for stabilization because of its potential to replace inorganic processes, such as biofuel production and natural surfactant synthesis. A high internal phase emulsion (HIPE) template, using dicyclopentadiene (DCPD) as a monomer, was polymerized in the presence of lipase, forming a highly ordered structure of both macro- and microscale features. Additionally, polyHIPEs were synthesized in the absence of lipase as a control. The hierarchical structure of the polyHIPEs was observed using scanning electron microscopy (SEM). Lipase polyHIPEs were tested for activity after immobilization using resorufin butyrate as a substrate. The polyHIPEs (19 µg lipase/g material) were sectioned into pieces to an equivalent amount of protein as native lipase prior to activity testing. Lipase incorporated into polyHIPEs exhibited an increase in activity after immobilization, compared to native lipase. On average, lipase polyHIPEs displayed a 63.3±8.7% increase in activity over native lipase. Previous research stabilizing lipase in polymerized DCPD emulsions showed enhanced stability in extreme environments, including extreme pH values (pH 3, 7, 10), and greener solvents at elevated temperatures (50 °C and 60 °C). PolyHIPEs take advantage of a hierarchical structure to increase surface area available to participate in enzymatic reactions, while retaining a macroscale catalyst, supporting reuse. Enzyme stabilization within hierarchical structures shows potential for application in extreme environments present in bioprocessing, while considering ease of handling.

Stabilization of lipase in polymerized high internal phase emulsions through interfacial assembly

254th National Meeting (2017)

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