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When a solute is present in an aqueous droplet, the water activity in the droplet and the rate of droplet dissolution are both decreased (as compared to a pure water droplet). One of the main parameters that controls this effect is the dynamically changing solute concentration, and therefore water activity and chemical potential, at the droplet interface. This work addresses the importance of understanding how water activity changes during solution droplet dissolution. A model for dissolution rate is presented that accounts for the kinetic effects of changing water activity at the droplet interface during the dissolution of an aqueous salt solution microdroplet into a second immiscible liquid phase. The important underlying question in this model is whether the dissolving component can be considered in local equilibrium on both sides of the droplet interface and whether this assumption is sufficient to account for the kinetics of dissolution. The dissolution model is based on the Epstein-Plesset equation, which has previously been applied to pure gas (bubble) and liquid (droplet) dissolution into liquid phases, but not to salt solutions. The model is tested by using the micropipet technique to form and observe the dehydration of single NaCl solution microdroplets in octanol or butyl acetate. The model successfully predicts the droplet diameter as a function of time in both organic solvents. The NaCl concentration in water is measured well into the supersaturated area >5.4 M, and the supersaturation limit at which NaCl nucleation happens is reported to be 10.24 ± 0.31 M. [ABSTRACT FROM AUTHOR]

Controlled enzyme dehydration using a new processing technique of Microglassification™ has been investigated. Aqueous solution microdroplets of lysozyme, α-chymotrypsin, catalase, and horseradish peroxidase were dehydrated in n-pentanol, n-octanol, n-decanol, triacetin, or butyl lactate, and changes in their structure and function were analyzed upon rehydration. Water solubility and microdroplet dissolution rate in each solvent decreased in the order: butyl lactate > n-pentanol > triacetin > n-octanol > n-decanol. Enzymes Microglassified™ in n-pentanol retained higher activity (93%-98%) than n-octanol (78%-85%) or n-decanol (75%-89%), whereas those Microglassified™ in triacetin (36%-75%) and butyl lactate (48%-79%) retained markedly lower activity. FTIR spectroscopy analyses showed α-helix to β-sheet transformation for all enzymes upon Microglassification™, reflecting a loss of bound water in the dried state; however, the enzymes reverted to native-like conformation upon rehydration. Accelerated stressed-storage tests using Microglassified™ lysozyme showed a significant ( p < 0.01) decrease in enzymatic activity from 46,560 ± 2736 to 31,060 ± 4327 units/mg after 3 months of incubation; however, it was comparable to the activity of the lyophilized formulation throughout the test period. These results establish Microglassification™ as a viable technique for enzyme preservation without affecting its structure or function. © 2014 Wiley Periodicals, Inc. and the American Pharmacists Association J Pharm Sci 104:640-651, 2015 [ABSTRACT FROM AUTHOR]