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Alpha-Glucosidase Enzyme Immobilized Dextran-Co Metal Nanoparticle Cryogel Composite Systems as Dual Catalyst with Enhanced Stability and Catalytic Activity
Journal article   Peer reviewed

Alpha-Glucosidase Enzyme Immobilized Dextran-Co Metal Nanoparticle Cryogel Composite Systems as Dual Catalyst with Enhanced Stability and Catalytic Activity

Sahin Demirci and Nurettin Sahiner
ChemCatChem, Vol.15(11), p.n/a
06-09-2023

Abstract

Chemistry Chemistry, Physical Physical Sciences Science & Technology
Here, dextran (Dex) cryogels were prepared and used for the immobilization of alpha-Glu enzyme via two different techniques of entrapment and covalent linking. The entrapment of alpha-Glu enzyme within Dex cryogels (alpha-GluE@Dex) during the synthesis process caused almost 70% activity loss. On the other hand, the Dex cryogels with alpha-Glu enzyme immobilized via covalent linking (alpha-GluC@Dex) maintained 91. 1.1% activity and afforded 10 consecutive usages and could be stored at 25 degrees C for 10 days with more than 50% activity. Moreover, we prepared Cobalt (Co) metal nanoparticle containing Dex-Co cryogel composite to be used to immobilize the alpha-Glu enzyme via covalent linking to attain an alpha-GluC@Dex-Co catalyst system with dual catalytic performance e. g., enzymatic and chemical reduction of the substrate and its' by-product for the first time. The prepared alpha-GluC@Dex-Co cryogels system was used for enzymatic hydrolysis of 4-nitrophenyl-alpha-D-glucopyranoside to glucose and 4-nitrophenol, and then the reduction of 4-nitrophenol to 4-aminophenol catalyzed by the Co metal nanoparticles present as co-catalyst within the cryogel network. The enzymatic activity of alpha-GluC@Dex-Co cryogels was calculated as 72. 3.1% and the cryogel reduced the enzymatic reaction by-product of 4-nitrophenol to 4-aminophenol in 7 min in the presence of NaBH4.

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