Batch crystallization of hen egg white lysozyme was carried out in sodium acetate buffer at pH 4.5 and 18°C. Different amounts of saturated sodium chloride solution (precipitant) were used for the crystallization of lysozyme. It could be shown that with faster addition of the precipitant (0.58 ml/min) the crystals were smaller than with an addition rate of 0.2 ml/min. However, the unexpected result in this work was that the slower addition reduced the specific activity of lysozyme by 21% compared to the starting material. The rate of addition of 0.58 ml/min resulted in the contrary in no significant loss in the specific activity.
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