Nanomaterials‐based artificial enzymes (AEs) have flourished for more than a decade. However, it is still challenging to further enhance their biocatalytic performances due to the limited strategies ...to tune the electronic structures of active centers. Here, a new path is reported for the de novo design of the d electrons of active centers by modulating the electron transfer in vanadium‐based AEs (VOx‐AE) via a unique Zn–O–V bridge for efficient reactive oxygen species (ROS)‐catalysis. Benefiting from the electron transfer from Zn to V, the V site in VOx‐AE exhibits a lower valence state than that in V2O5, which results in charge‐filled V‐dyz orbital near the Fermi level to interfere with the formation of sigma bonds between the V‐dz2 and O‐pz orbitals in H2O2. The VOx‐AE exhibits a twofold Vmax and threefold turnover number than V2O5 when catalyzing H2O2. Meanwhile, the VOx‐AE shows enhanced catalytic eradication of drug‐resistant bacteria and achieves comparable wound‐treatment indexes to vancomycin. This modulating charge‐filling of d electrons provides a new direction for the de novo design of nanomaterials‐based AEs and deepens the understanding of ROS‐catalysis.
A new vanadium‐based artificial enzyme (VOx‐AE) for efficient reactive oxygen species (ROS)‐catalysis is synthesized by modulating the d electrons in the active centers via a unique Zn–O–V bridge structure. Experimental and theoretical results demonstrate that the VOx‐AE exhibits optimal adsorption/dissociation of oxygen‐intermediates, thus showing enhanced ROS catalytic activity and augmented eradication of drug‐resistant bacteria and comparable wound‐treatment indexes to antibiotics.
Artificial multienzyme scaffolds are being developed for in vitro cascaded biocatalytic activity and, in particular, accessing substrate channeling. This review covers progress in this field over the ...last ∼5 years with a specific focus on the scaffold materials themselves and the benefits they can provide for assembling multienzyme cascades in vitro. These benefits include improving biocatalytic efficiency, bypassing potential cellular toxicity, directed catalysis, modularity, incorporating enzymes from different prokaryotic and eukaryotic sources, and potentially the ability to create de novo designer cascades. We begin with an overview of the strongest impetus currently driving the rapid development of this field, namely, biomanufacturing and cell-free synthetic biology. We then discuss in detail pertinent mechanisms responsible for the benefits of artificial multienzyme scaffolds. In particular, we focus on substrate channeling, including the evolving debate about what leads to substrate channeling in artificial systemsproximity, confinement, or bothand whether sequential enzyme order is really needed. How different scaffold materials/chemistries can in turn affect enzyme activity is also discussed. The bulk of the review then details progress in the development of different biotic (e.g., cells) and abiotic (e.g., nanoparticles) scaffolding materials and is divided up by class and subtype as needed. Within each material class of scaffolds, attention is given to their inherent chemical diversity, how they are engineered, how they allow for enzymatic attachment, their ease of use, their benefits (e.g., inherent three-dimensional architecture) and liabilities where appropriate, and other relevant issues. For each scaffolding material, a detailed overview of current progress is provided using examples of multienzyme cascades and data/schematics reproduced from the literature. Special attention is also given to the use of DNA scaffolds, as they can potentially provide the most versatile designer three-dimensional scaffold architectures. Finally, a short perspective on how this rapidly moving field will evolve in the near and long terms is provided.
Soil biota has a crucial impact on soil ecology, global climate changes, and effective crop management and studying the diverse ecological roles of dipteran larvae deepens the understanding of soil ...food webs. A multi-omics study of Pseudolycoriella hygida comb. nov. (Diptera: Sciaroidea: Sciaridae) aimed to characterize carbohydrate-active enzymes (CAZymes) for litter degradation in this species. Manual curation of 17,881 predicted proteins in the Psl. hygida genome identified 137 secreted CAZymes, of which 33 are present in the saliva proteome, and broadly confirmed by saliva CAZyme catalytic profiling against plant cell wall polysaccharides and pNP-glycosyl substrates. Comparisons with two other sciarid species and the outgroup Lucilia cuprina (Diptera: Calliphoridae) identified 42 CAZyme families defining a sciarid CAZyme profile. The litter-degrading potential of sciarids corroborates their significant role as decomposers, yields insights to the evolution of insect feeding habits, and highlights the importance of insects as a source of biotechnologically relevant enzymes.
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•The Pseudolycoriella genome (609 Mb) encodes 17881 genes and 1022 CAZymes•The saliva proteome includes 33 of the 137 predicted secreted CAZymes•Diverse saliva CAZyme activities detected on polysaccharides and synthetic substrates•Comparison with other sciarids shows a rich conserved repertoire of secreted CAZymes
Mycology; Biocatalysis; Plant biology
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•We reviewed materials and functionalization strategies to engineer nanobiocatalysts.•Coordination between materials and enzymes play a critical role in developing ...nanobiocatalysts.•The characteristic properties rendering materials interesting matrices for immobilization.•Functionalized constructs can be used as immobilization carriers for enzymes.
Suitable coordination between the new wave of nanostructured materials and catalyst of interests play a critical role in developing nanobiocatalysts with new or improved functionalities. In this context, enzymes with natural origin are versatile biocatalysts with multifunctional characteristics and have been widely utilized in various sectors such as environmental, energy, biomedical, pharmaceutical, cosmeceutical, nutraceutical, fine chemicals, agro-industrial, and food industry, etc. The deployment of enzymes in a non-natural environment has limited boundaries such as the high production cost, challenging separation, purification, and liability to deactivation under non-ambient conditions. These drawbacks can be overcome by the design and fabrication of novel hybrid and functionalized nanobiocatalyst. However, appropriate coordination at chemical, physical, and the biological level is highly requisite to engineer such nanobiocatalysts of supreme interests. Currently, the generation and development of diverse nanomaterials along with new strategies have been established from the nanotechnology perspectives, where the integration of naturally occurring biocatalysts with suitable nanomaterials offer an exceptional corridor to upgrade the catalytic performances of pristine enzymes. Recent innovations in nano-biotechnology furnished numerous opportunities to integrate natural biocatalysts to a range of nanostructured materials with unique attributes. These newly introduced nanomaterials show/impart additional characteristics which enzyme in their pristine form fails to demonstrate on their own. Manipulation of these nanomaterials for enzyme delivery or recovery, remote access for activation or deactivation of enzymatic activity, and new catalytic entities with harmonizing functionalities has taken this field to a new horizon with pronounced biotechnological applications in the coming years. The present review emphases on the recent developments along with the exploitation of nanostructured materials including nanofibers, hybrid nanoflowers, mesoporous/nanoporous carriers, carbon nanotubes, magnetic or non-magnetic nanoparticles, and nanocomposites as support carriers for the immobilization of different enzymes to develop nanobiocatalysts with potential activity and stability characteristics. In addition, strategies for the synthesis and various types of new functionalization approaches, particularly the chemical method for its capability to modify nanomaterials with enormous functionalities are discussed. Towards the end, challenges related to the use of nanobiocatalysts and their possible solution are summarized.
Lignin is a crucial component of plant matter; however, it is also largely responsible for the recalcitrance of lignocellulosic biomass when subjected to pretreatment processes. Lignin is generated ...in large volumes as a waste product from paper and pulping industry as well as cellulosic biorefineries. As a result, lignin valorization is critical to the successful implementation of cellulosic biofuels. To this end, we investigated interactions between three ionic liquids (ILs) and the lignolytic enzyme laccase toward biocatalytic lignin conversion to aromatic monomers. Laccase exhibited minimal loss of activity in 10% diethylamine hydrogensulfate (DEAHSO4). Changes in V max and K m of laccase with respect to IL concentration indicate that DEAHSO4 is a noncompetitive inhibitor, whereas cholinium lysinate (ChLys) and C2C1ImOAc are mixed inhibitors. Docking simulations suggested that ChLys and C2C1ImOAc disrupt residues leading to the active site. Experiments with a β-O-4′ linked model dimer revealed that laccase in C2C1ImOAc and ChLys requires the presence of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) to oxidize the β-O-4′ linkage, leading to polymerization of the model dimer. Alkaline lignin treated with laccase, ABTS, and the aqueous ILs (AILs) showed few structural changes, although the lignin was partially solubilized and converted to degradation products. The major products obtained from alkaline lignin were vanillin, acetosyringone, syringaldehyde, and acetovanillone. The results of this study provide, for the first time, an in-depth explanation of the interactions between laccase and AILs for the purpose of lignin valorization.
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