Enzyme in nonaqueous solutions

Enzyme molecules are rigid enough to preserve their native structures and some of the essential water, performing as molecular lubricant for conformational flexibility of enzyme, remains bound even in organic solvents containing little or no water. Altering the bulk water by organic solvents is conducive to improvement of substrate solubility, increase thermal stability (i.e. operational stability), suppression of side reaction generated by water and rational control on enzymatic selectivity.

Related publications:

Langmuir, 2010, 26 (11), pp 9076–9081

Chem. Commun., 2009, 535-537

Bioelectrochemistry, 2009, 76, 63–69

Anal. Chem., 2005, 77 (6), pp 1647–1654

Langmuir, 2003, 19 (4), pp 1282–1286

Chem. Commun., 2002, 816-817

Biotechnology and Bioengineering, 1995, 46, 175–179

>>>A biofuel cell working in non-aqueous solution

In our recent publication (Chem. Commun., 2015,51, 13478-13480), We report the first example of a biofuel cell operating in organic solvents. The cell utilises glucose oxidase and bilirubin oxidase immobilised on nanoporous gold. The power output of the cell decreases with increasing solvent hydrophobicity in the alcohols, methanol (MeOH), ethanol (EtOH), 1-propanol (PrOH), 1-butanol (BuOH) and 1-pentanol (PeOH).