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Bulk Crystallization of Proteins by Low‐Pressure Water Evaporation
Author(s) -
Groß Michael,
Kind Matthias
Publication year - 2016
Publication title -
chemical engineering and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.403
H-Index - 81
eISSN - 1521-4125
pISSN - 0930-7516
DOI - 10.1002/ceat.201500582
Subject(s) - crystallization , protein crystallization , orthorhombic crystal system , evaporation , tetragonal crystal system , boiling , solubility , lysozyme , aqueous solution , chemical engineering , chemistry , yield (engineering) , solvent , materials science , boiling point , salt (chemistry) , crystallography , crystal structure , thermodynamics , organic chemistry , metallurgy , biochemistry , engineering , physics
An advanced technique for bulk protein crystallization based on solvent evaporation is introduced. Hen egg white lysozyme is crystallized from its buffered aqueous solution in a stirred tank at low pressure and, thus, moderate boiling temperatures. No crystallizing agent to reduce the solubility is needed for crystallization. The biological activity of the enzyme remains unchanged during the process and a high crystal yield is achieved. Tetragonal and rod‐like lysozyme crystals, presumably of orthorhombic type, are crystallized at different boiling temperatures. This crystallization technique is proposed as a promising option to crystallize proteins economically, controllably, and gently. This method may replace standard salt‐out steps in existing production processes.