Easily handling penicillin G acylase magnetic cross-linked enzymes aggregates: Catalytic and morphological studies

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• 作者：Willian Kopp ; Taciane P. da Costa ; S ; ra C. Pereira ; Miguel Jafelicci Jr ; Roberto C. Giordano ; Rodrigo F.C. Marques ; Fern ; o M. Ara煤jo-Moreira ; Raquel L.C. Giordano
• 关键词：Cross-linked enzymes aggregates ; Superparamagnetic nanoparticles ; Supramolecular complex ; Magnetic recovery of enzymes ; Penicillin hydrolysis
• 刊名：Process Biochemistry
• 出版年：January, 2014
• 年：2014
• 卷：49
• 期：1
• 页码：38-46
• 全文大小：1781 K

文摘

Biomolecules labeled with superparamagnetic nanoparticles can be selectively removed from complex reaction mixtures using an external magnetic field. Amino-functionalized superparamagnetic iron oxide nanoparticles (amino-SPION) were co-aggregated with penicillin G acylase and then cross-linked, generating magnetic cross-linked enzymes aggregates (M-CLEAs) that were quickly and efficiently recovered from the reaction medium by applying an external magnetic field. M-CLEAs and cross-linked enzymes aggregates (CLEAs) prepared under the same reaction conditions were characterized and compared. The best recovered activities were obtained for M-CLEAs prepared using polyethylene glycol 600 as precipitant and the most stable M-CLEA were obtained using tert-butanol. Successive penicillin G hydrolysis reactions were carried out using the same M-CLEA in a 50 mL reactor (3 reaction cycles), after the reactions the derivate was magnetically recovered without loss of activity demonstrating a total magnetic recovery. Line-scan energy dispersive X-ray spectroscopy showed that the amino-SPIONs were homogeneously dispersed within the structure of the M-CLEA.