Protein-supported transition metal catalysts: Preparation, catalytic applications, and prospects

Chen, Tianyou; Yan, Ping; Qiu, Meishuang; Yi, Changfeng; Xu, Zushun

doi:10.1016/j.ijbiomac.2023.123206

Cited by 4 publications

(2 citation statements)

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“…Silk/metal composites with catalytic activity also have been studied [236,237]. The advantages of SF for constructing catalytic components are attributed to its elemental composition and molecular structure [238].…”

Section: Carbon-based Electrocatalytic Compositesmentioning

confidence: 99%

Novel Applications of Silk Proteins Based on Their Interactions with Metal Ions

Wen,

Zhang,

Chen

et al. 2023

Sustainability

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Silk secreted by Bombyx mori L. silkworm has become one of the most important biomaterials, due to its excellent biocompatibility, controllable biodegradability, superior processability, and unique mechanical properties. Silk fibroin and sericin, as the two components of silk, contain abundant polar functional groups, and thus can bind metal ions through electrostatic interaction and chelation. Based on this binding, silk proteins not only can be used to fabricate ecofriendly and efficient adsorbents to remove heavy metals from waterbodies, but also can synthesize metal nanostructures (nanoparticles or nanoclusters) to form silk/metal composites with amazing optical or electrochemical characteristics. This binding also can be manipulated to optimize silk’s performance. This review focuses on discussing and summarizing advances in the use of silk fibroin and sericin for heavy metal ion-contaminated water remediation, biosensing materials, and electrochemical materials from the perspective of the interaction between silk proteins and metal ions. The performance enhancement of silk using metal ions is also analyzed. Moreover, the silk proteins’ interactions with metal ions and related structural features that contribute to the above sustainable applications are illustrated to lay a theoretical foundation. This review will favor the expansion of the applications of silk in both the traditional textile field and new biomaterials.

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Section: Carbon-based Electrocatalytic Compositesmentioning

confidence: 99%

Novel Applications of Silk Proteins Based on Their Interactions with Metal Ions

Wen,

Zhang,

Chen

et al. 2023

Sustainability

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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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