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Purification of L-asparaginase II by crystallization

Content Provider	Springer Nature Link
Author	Liu, Y. Pietzsch, M. Ulrich, J.
Copyright Year	2013
Abstract	Here a case study of L-asparaginase II out of a recombinant Escherichia coli is presented. The target protein was obtained by simple cell disintegration and acetone precipitation. The L-asparaginase II has been crystallized in three different forms in the following microbatch crystallization. The rod-shaped crystals (∼400 μm edge length) were obtained at either 8°C or 22°C after 17 h by addition of PEG$_{6000}$. The rectangular-shaped crystals were obtained after further recrystallization of the rod-shaped crystals. The rhombic-shaped crystals formed at 8°C after 12 days when cold ethanol was used instead of PEG$_{6000}$. All crystallizations were performed in tris-acetate buffer (50 mmol·L$^{−1}$, pH 5.1). By crystallization, the specific activity of L-asparaginase II has increased 5-fold. The protein content and the purity of the crystals were evaluated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The more concentrated L-asparaginase II out of an extract mixture and the presence of only less minor proteins after crystallization demonstrates that crystallization is an effective and mild method to purify the target protein. The single crystal X-ray diffraction pattern reveals that the crystals are proteins and the X-ray powder diffraction (XRPD) pattern shows clearly that the crystals forming in PEG$_{6000}$ and ethanol have different crystal structures.
Starting Page	37
Ending Page	42
Page Count	6
File Format	PDF
ISSN	20950179
Journal	Frontiers of Chemical Engineering in China
Volume Number	7
Issue Number	1
e-ISSN	20950187
Language	English
Publisher	SP Higher Education Press
Publisher Date	2012-12-28
Publisher Institution	Chinese Universities
Publisher Place	Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	protein crystallization L-asparaginase II purification Industrial Chemistry/Chemical Engineering Nanotechnology
Content Type	Text
Resource Type	Article
Subject	Chemical Engineering

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