(314e) Bioinspired Membrane Pores Containing Phospholipid Bilayer for Immobilized Enzymatic Catalysis

Enzymes, immobilized within membrane pores, offer improved kinetics due to pressure-driven convective flow. On the other hand, phospholipid bilayer (PLB), owing to its fluidity and native “cell-membrane” environment, facilitates the activity and stability of enzymes. We reported integration of the biomimetic characteristics of PLB and convective flow through porous membrane within the same configuration (1). Novel bioinspired membranes were developed by incorporating PLB within membrane pores using two different approaches – (i) direct deposition of lipid bilayer within bare membrane pores, and (ii) immobilization of a polymer cushion prior to lipid bilayer within membrane pores. PLB-functionalized membrane pores were examined for enzymatic catalysis by electrostatically immobilizing glucose oxidase (GOx) enzyme. In-depth activity study revealed that the bioinspired membrane with polymer cushion supported PLB and with convective mode of flow exhibited benefits in terms of activity, stability and operating range of pH. Besides, we reported the reusability of the membrane matrix as well as the PLB by exploiting the reversible attachment-detachment sequence of the functional moieties (2). Characterization of the detached phospholipid confirmed retention of the original structural and functional properties as exhibited before attachment. The study was further extended for the development of immobilized bi-enzymatic (GOX-HRP) and multi-enzymatic (Glucoamylase-GOX-HRP) systems. Development of the bioinspired membrane, characterization and in-depth performance analysis (activity, stability and reusability) studies will be discussed in the presentation.

References: 1. A. Kumari, S. Datta^*, Phospholipid bilayer functionalized membrane pores for enhanced efficiency of immobilized glucose oxidase enzyme, J. Mem. Sci., 539 (2017) 43-51

2. A. Kumari, L. Rekhie, S. Datta^*, Reversibly attached phospholipid bilayer functionalized membrane pores, Langmuir, 34 (2018) 14395-14401