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Abstract
Magnetic porous corn starch was prepared as an affinity adsorbent for the efficient and simple scale-up procedure for one-step purification of cyclodextrin glucanotransferase (CGTase) from Bacillus circulans. Magnetic affinity separation enabled isolation of CGTase from cultivation media (volumes between 10 and 400 mL) with ca 60–70% recovery after elution with alkaline buffers containing soluble starch; the enzyme purification factor was 19–25 in different batches. The majority of ballast proteins were removed during the purification process, which shows high selectivity of the affinity material used.
Acknowledgements
This research was supported by the Ministry of Education, Youth and Sports of the Czech Republic (Projects OC 157–COST 868 and OC 09052–COST MP0701), and by the Ministry of Industry and Trade of the Czech Republic (Project 2A-1TP1/094). The authors also express their gratitude to SEPMAG Tecnologies, SL, Barcelona, Spain for providing R&D grant and SEPMAG Q500 mL 2042, precision magnetophoresis system.
Declaration of interest: The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper.