Biocatalytic protein membranes fabricated by electrospinning

In this study, a protein-based catalytic membrane was produced by electrospinning. Membrane activity was characterised in terms of response current for various glucose concentrations. We focused on the preparation of a scaffold by converting a globular protein to other structural forms using catastrophic solvents. A scaffolding protein, bovine serum albumin, and an enzyme, glucose oxidase (GOD), were selected as a model natural carrier matrix and a biologically active agent, respectively. Beta-mercaptoethanol (β-ME) was used to convert the globular protein to an amyloid-like form. A structural stabilising agent, 2,2,2-triflouroethanol (TFE), was used to maintain the final α-helical structure of the amyloid-like protein. The TFE:PBS (phosphate-buffered saline) ratio and various electrospinning parameters were analysed to minimise activity loss. Using this approach, we applied electrospinning to an active enzyme to obtain biocatalytic nanofibrous membranes. After optimising the protein electrospinning process, the activities of the protein nanofibrous membranes were monitored. GOD remained active in the new membrane structure. The highest enzyme activity was observed for the membranes prepared with a 1.5:1 (v:v) TFE:PBS solvent ratio. In that particular case, the immobilized enzyme created a current of 0.7 μA and the apparent activity was 2547 ± 132 U/m2.