A new method is presented to precipitate proteins and amino acids from reverse micelles by dehydrating the micelles with molecular sieves. Nearly complete precipitation is demonstrated for alpha-chymotrypsin, cytochrome-c, and tryptophan from 2-ethylhexyl sodium sulfosuccinate (AOT)/isooctane/water reverse micelle solutions. The products precipitate as a solid powder, which is relatively free of surfactant. The method does not require any manipulation of pH, ionic strength, temperature, pressure, or solvent composition, and is applicable over a broad range of these properties. This general approach is compared with other techniques for the recovery of biomolecules from reverse micelles.