Sustainable Synthesis of Zeolitic Imidazolate Frameworks at Room Temperature in Water with Exact Zn/Linker Stoichiometry.

Zeolitic imidazolate frameworks (ZIFs) are widely used MOFs because of certain characteristics, but also because they can be prepared at room temperature using water as the unique solvent. However, these a priori sustainable conditions inevitably entail a huge and somehow unusable excess of linker. Here, we present the formation of ZIFs at room temperature in water, starting from mixtures with a linker/metal ratio of two, that is, coinciding with the stoichiometry found in the final MOFs, in the presence of amines. ZIF-8 can be prepared with triethylamine (TEA), giving a yield of Zn of 96.6%. Other bases, like NaOH, tetraethylammonium hydroxide or ammonium hydroxide, do not lead to ZIF-8 under the same conditions. The so-obtained ZIF-8 contains TEA inside its cavities, making it less porous than its conventionally prepared counterparts. Amine can be removed by mild thermal treatments (200-250 °C). Such thermal treatments induce the generation of g-C3N4-like species which could give added value to these materials as potential photocatalysts, increasing their affinity to CO2, as proved in this work. This methodology can be successfully extended to other amines, like N,N-dicyclohexylmethylamine, as well as to other prepared ZIFs, like Co-based ZIF-67, isostructural to ZIF-8.

Metal-organic frameworks for enzyme immobilization and nanozymes: A laccase-focused review.

Laccases are natural catalysts with remarkable catalytic activity. However, their application is limited by their lack of stability. Metal-organic frameworks (MOFs) have emerged as a promising alternative for enzyme immobilization. Enzymes can be immobilized in MOFs via two approaches: postsynthetic immobilization and in situ immobilization. In postsynthetic immobilization, an enzyme is embedded after MOF formation by covalent interactions or adsorption. In contrast, in in situ immobilization, a MOF is formed in the presence of an enzyme. Additionally, MOFs have exhibited intrinsic enzyme-like activity. These materials, known as nanozymes when they have the ability to replace enzymes in certain catalytic processes, have multiple key advantages, such as low cost, easy preparation, and large surface areas. This review presents a general overview of the most recent advances in both enzyme@MOF biocatalysts and MOF-based nanozymes in different applications, with a focus on laccase, which is one of the most widely investigated enzymes with excellent industrial potential.

Oriented Coimmobilization of Oxidase and Catalase on Tailor-Made Ordered Mesoporous Silica.

Mesoporous silica materials are promising carriers for enzyme immobilization in heterogeneous biocatalysis applications. By tailoring their pore structural framework, these materials are designable for appropriate enzyme binding capacity and internal diffusivity. To supply O2 efficiently to solid-supported immobilized enzymes represents a core problem of heterogeneously catalyzed oxidative biotransformations. In this study, therefore, we synthesized and compared three internally well-ordered and two amorphous silica materials as enzyme carriers, each of those with pore sizes of ≥10 nm, to enable the coimmobilization of d-amino-acid oxidase (79 kDa) and catalase (217 kDa). Both enzymes were fused to the silica-binding module Zbasic2 to facilitate their selective and oriented immobilization directly from crude protein mixtures on native silica materials. Analyzing the effects of varied pore architecture and internal surface area on the performance of the immobilized bienzymatic system, we showed that a uniform pore structural framework was beneficial for enzyme loading (≥70 mg protein/g carrier), immobilization yield (≥90%), surface and pore volume filling without hindered adsorption, and catalytic effectiveness (≥60%) of the coimmobilizate. Using the best carrier LP-SBA-15, we obtained a solid oxidase-catalase preparation with an activity of 2000 µmol/(min g_material) that was recyclable and stable during oxidation of d-methionine. These results affirm a strategy of optimizing immobilized O2-dependent enzymes via tunable internal structuring of the silica material used as carrier. They thus make a significant advance toward the molecular design of heterogeneous oxidation biocatalysts on mesoporous silica supports.

Mesoporous silicas with tunable morphology for the immobilization of laccase.

Siliceous ordered mesoporous materials (OMM) are gaining interest as supports for enzyme immobilization due to their uniform pore size, large surface area, tunable pore network and the introduction of organic components to mesoporous structure. We used SBA-15 type silica materials, which exhibit a regular 2D hexagonal packing of cylindrical mesopores of uniform size, for non-covalent immobilization of laccase. Synthesis conditions were adjusted in order to obtain supports with different particle shape, where those with shorter channels had higher loading capacity. Despite the similar isoelectric points of silica and laccase and the close match between the size of laccase and the pore dimensions of these SBA-15 materials, immobilization was achieved with very low leaching. Surface modification of macro-/mesoporous amorphous silica by grafting of amine moieties was proved to significantly increase the isoelectric point of this support and improve the immobilization yield.