Co-immobilization of enzymes and chemocatalysts for one-pot chemoenzymatic cascades: Scaffold engineering toward more efficient catalysis

Chen, Tianyou; Lu, Yizhuo; Xiong, Xiaorong; Xu, Zushun

doi:10.1016/j.checat.2023.100894

Cited by 1 publication

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“…The combination of enzymes and metal nanoparticles (MNPs) expands the spectrum of reaction types to meet the growing need to produce new chemicals. − More importantly, the combination provides access to one-pot chemoenzymatic cascade reactions, − which possess several advantages, including producing less waste, avoiding the isolation and purification of intermediates, improving the overall synthetic efficiency and yields, and requiring less operating time and production costs. Because of their distinct operating conditions and potential mutual deactivation, the direct use of enzymes and MNPs in a vessel may not afford efficient cascades .…”

Section: Introductionmentioning

confidence: 99%

Hyperbranched Polymer-Cross-Linked Enzyme Aggregates for the Compartmentalized Coimmobilization of Enzymes and Metal Nanoparticles

Qiu,

Peng,

et al. 2024

ACS Appl. Polym. Mater.

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The coimmobilization of enzymes and metal nanoparticles (MNPs) is an effective strategy for improving the efficiency of chemoenzymatic cascades. Cross-linked enzyme aggregates (CLEAs), as catalytic scaffolds, have been utilized as scaffolds for coimmobilization, leading to relatively high volumetric and space–time yields. However, it is still a challenge to achieve compartmentalization of enzymes and MNPs in CLEAs, likely due to the poor affinity between cross-linkers and MNPs. To overcome this shortcoming, here we have developed a void-adaptive cross-linking strategy for the preparation of hyperbranched polymer-cross-linked enzyme aggregates (HPCLEAs) that could be used as scaffolds for the immobilization of MNPs. Hyperbranched polymers were in situ-synthesized and could void-adaptively cross-link enzyme aggregates. They could also complex with metal precursors and then template the formation of MNPs via the in situ reduction of metal precursors, leading to the compartmentalization of several combinations of lipase and glucose oxidase (GOx) with MNPs, including Pd, Pt, Au, PdPt, AuPd, and AuPt. The physicochemical and catalytic properties of these chemoenzymatic catalysts were systematically studied to gain a deeper insight into structure–activity relationships. This strategy is promising for the development of more efficient chemoenzymatic cascades and can be extended for the compartmentalized coimmobilization of other enzymes and MNPs.

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