The adhesion forces of liquid drops on superhydrophobic surfaces are typically in the nano-Newton range which presents problems in their dispensation from pipettes. Furthermore, since the liquid adheres more strongly to the pipette tip, some portion of the liquid will tend to remain on the tip, causing inaccuracy in the volume dispensed. We advance a novel approach here, in which the spray from an acoustic nebulizer is sent to a superhydrophobic receptacle and the volume ascertained precisely using a weighing scale. The superhydrophobic surface was identified to develop via a galvanic displacement mechanism in an electroless deposition process. A time dependent morphology change from granular to dendritic with longer immersion into the silver nitrate solution was found which indicated that granular growth beyond a certain size was not feasible, although granular structures were more preferentially formed just after nucleation. The dendritic structure formation was likely due to the natural tendency of the process to maintain or increase the surface area to volume ratio in order not to limit the rate of deposition. An immersion for at least 7 seconds into the silver nitrate solution, when the granular structures were predominant, was all that was needed to ensure superhydrophobicity of the surfaces. Also, the superhydrophobic state required not just significant numbers of the granular structures to be present but also interrupted coverage on the surface. On using the technique, a single drop was created by subsequently covering the receptacle with a lid and shaking it gently. The volume dispensed was found to vary linearly with the operation time of the nebulizer. We elucidated the observed increased ability of drops to reside on inclines using wetting mechanics and presented an elementary mathematical description of the extent of aerosol coverage on the surface, which has implications for the mechanics of aerosol growth into drops. The structural changes in enhanced green fluorescent protein (EGFP) observed after acoustic dispensation necessitated all samples in a fluorimetric assay to involve equal nebulized volumes of the fluorescent protein marker for measurement consistency.

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The effects of hydrogen peroxide on enterokinase catalysis were studied using several fusion proteins recombinantly produced from E. coli. It was demonstrated that hydrogen peroxide enhanced the rate of enterokinase cleavage reaction, leading to a faster release of the target peptide as discussed in patent WO07149053. Among the conditions tested, we observed that hydrogen peroxide could exert its effect on the cleavage of fusion proteins over a wide range of pH and temperature. This finding might provide a simple solution for the accelerated enterokinase cleavage of thermolabile fusion proteins at low temperature.