m khosravanian - Biotechnology Group, Department of Chemical Engineering, Tarbiat Modares University,Tehran, Iran, P. O. Box: ۱۴۱۱۵-۱۱۴
s hashemi najafabadi - Biotechnology Group, Department of Chemical Engineering, Tarbiat Modares University,Tehran, Iran, P. O. Box: ۱۴۱۱۵-۱۱۴
m erfani moghadam - Biophysics Group, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran

Recently, crystallization has emerged as a suitable process for preparing the biocatalysts in the form of crystals or for the recovery of proteins from the fermentation broth. In both instances, it is essential to define the suitable conditions to control the crystal size and weight and also a reliable recovery of the active protein. In this study, we described a simple procedure that allows determining the effect of four factors; protein concentration, salt concentration, rotation rate and pH; on crystallization process for albumin. The experiments indicated that in milli-scale batch crystallization of albumin, the best recovery of 94% can be obtained at protein concentration 61.25 mg/mL, salt concentration 62.5 mg/mL, pH 4.5 and rotation rate 112 rpm.

Agitated milli-scale vessels, Batch crystallization, Albumin, CCD