Abstract
AbstractAccurate equilibrium solubility data is important when studying the crystallization behavior of a compound. Measurements of solubility can be hindered by the length periods encountered during the approach to equilibrium. This is especially true for proteins and other compounds with relatively slow crystal growth rates. A new model curve fitting technique is developed and applied, which is equally applicable to crystallizing and dissolving systems. The curve fitting inputs are: (i) measurements of solute concentration as a function of time, taken during the dynamic approach to equilibrium; and (ii) the order of crystal growth or dissolution kinetics. The equilibrium solubility is an output parameter of the curve fitting. Where properly used, this curve fitting technique can give a more precise estimate of solubility equilibrium. The technique is applied to the measurement of solubility for glucose isomerase, an industrial enzyme.
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