Immobilization of invertase on silica monoliths with hierarchical pore structure to obtain continuous flow enzymatic microreactors of high performance

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• 作者：Katarzyna Szyma¨½ska^a ; ^{Katarzyna.Szymanska@polsl.pl} ; Wojciech Pud?o^a ; Julita Mrowiec-Bia?o¨½^a ; ^b ; Agata Czardybon^c ; Jacek Kocurek^a ; Andrzej B. Jarz?bski^a ; ^b
• 关键词：Hierarchically structured monoliths ; Monoliths in biocatalysis ; Enzymatic microreactor ; Immobilized invertase ; Sucrose hydrolysis
• 刊名：Microporous and Mesoporous Materials
• 出版年：2013
• 出版时间：April, 2013
• 年：2013
• 卷：170
• 期：Complete
• 页码：75-82
• 全文大小：896 K

文摘

Monolithic silica rods of 4 mm diameter and 2-5 cm length, exhibiting very open and uniform 3D hierarchical pore structure of 35 ¦Ìm flow-through macropores and ca. 20 nm mesopores were synthesized using the sol-gel processing combined with pore templating and phase separation. These monoliths were successfully converted into miniaturized multichannel continuous-flow reactors which (for a single rod) could operate at flow rates up to about 20 mL/min at backpressure not exceeding 2.5 bar. After covalent attachment of invertase, considered as a model enzyme, their potentials were tested in reaction of sucrose hydrolysis and the results were compared, using Michaelis-Menten kinetics, with the performance of mesoporous cellular foam (MCF)-bound invertase immobilized in the same way. The hydrolysis of sucrose appeared to proceed with maximum velocity over 1000 times faster in the monolithic bioreactor than in MCF-based slurry system, and invertase embedded in the mesopores of silica monoliths showed notably larger affinity (lower K_M) to substrate than the native enzyme. The reactors stored at 4 ¡ãC retained initial activity for at least 6 week and no change in the microreactor performance was seen for at least 2 week of continuous operation.