Bioreactor for the Continuous Purification of Simvastatin by Lovastatin Esterase. (September 2017)

• Record Type: Journal Article
• Authors: Kurek, Waldermar; Koszelewski, Dominik; Ostaszewski, Ryszard; Żądło-Dobrowolska, Anna
• Is Part Of: Process biochemistry. Volume 60(2017)
• Page Start: 92
• Page End: 97
• Publication Date: 2017-09
• Subjects: bioreactor -- continuous flow reactor -- lovastatin esterase -- simvastatin -- immobilization; Biochemical engineering -- Periodicals; Biotechnology -- Periodicals; Biochemistry -- periodicals; Biotechnology -- periodicals; Chemical Engineering -- periodicals; Génie biochimique -- Périodiques; Biotechnologie -- Périodiques; Biochemical engineering; Biotechnology; Periodicals; 660.63
• DOI: 10.1016/j.procbio.2017.05.026
• Languages: English
• ISSNs: 1359-5113

Abstract

Graphical abstract: An efficient separation of simvastatin ammonium salt from residual lovastatin ammonium salt, based on immobilized lovastatin esterase employed in a packed-bed bioreactor is now reported. Highlights: Purification of simvastatin from the residual amounts of lovastatin is reported. Immobilized lovastatin esterase was applied as a bed in a flow reactor. Chromogenic substrates were used for determination the enzyme specific activity. Abstract: This work investigates an efficient method for purification of simvastatin ammonium salt from the residual amounts of lovastatin ammonium salt. Lovastatin esterase produced by the fungus Clonostachys compactiuscula was chosen as a biocatalyst for selective hydrolysis of lovastatin ammonium salt. Based on specific activities, determined by a spectrophotometric assay, two enzyme preparations were chosen as suitable candidates for this transformation: lovastatin esterase immobilized on Sepharose 4 B or immobilized on diethylaminoethylcellulose. Immobilized enzyme was packed into the inner space of the steel column and examined as a bioreactor in a continuous flow process. Both reactors indicated excellent selectivity (> 100) and stability.