Abstract
Two fast and efficient purification methods for the preparation of large amounts of proline-specific endopeptidase (PSE) [EC 3.4.21.26] fromFlavobacterium meningosepticum heterologously expressed inEscherichia coli are described. Overproduction and accumulation of PSE in the periplasmic space ofE. coli means that a single gel chromatography step or ion exchange chromatography step was sufficient to obtain homogenously pure PSE preparations. With these procedures, up to 490 μg of purified enzyme per gE. coli cells were obtained. The different purification methods are discussed.
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