Recent Progress and Future Prospects of Laccase Immobilization on MOF Supports for Industrial Applications.

Laccase is a multicopper oxidoreductase enzyme that can oxidize organics such as phenolic compounds. Laccases appear to be unstable at room temperature, and their conformation often changes in a strongly acidic or alkaline environment, making them less effective. Therefore, rationally linking enzymes with supports can effectively improve the stability and reusability of native enzymes and add important industrial value. However, in the process of immobilization, many factors may lead to a decrease in enzymatic activity. Therefore, the selection of a suitable support can ensure the activity and economic utilization of immobilized catalysts. Metal-organic frameworks (MOFs) are porous and simple hybrid support materials. Moreover, the characteristics of the metal ion ligand of MOFs can enable a potential synergistic effect with the metal ions of the active center of metalloenzymes, enhancing the catalytic activity of such enzymes. Therefore, in addition to summarizing the biological characteristics and enzymatic properties of laccase, this article reviews laccase immobilization using MOF supports, as well as the application prospects of immobilized laccase in many fields.

Improvement in the stability and bioavailability of pumpkin lutein using ß-cyclodextrin microcapsules.

Growing concerns about food nutrition and food supplies have encouraged the development of effective constituents. Lutein is an important nutrient element, and its health benefits are gradually being recognized. Lutein, as a carotenoid antioxidant, can protect cells and organs from damage caused by free radicals. However, in processing, storage, and usage, lutein is unstable and often undergoes isomerization and oxidative decomposition, which limits its wide range of applications. ß-Cyclodextrin is an ideal substrate to prepare microcapsule structures, which are highly biocompatible and nontoxic. During the lutein encapsulation process, ideal ß-cyclodextrin microcapsules were used to form inclusion compounds. The results reveal that the encapsulation efficiency of the microcapsules reached 53%. Moreover, using ultrasonic-assisted extraction can easily and efficiently purify lutein. In addition, the capability of the ß-cyclodextrin composite shell can enhance the bioactive molecules' activity and stability.

Research Status and Application Prospects of the Medicinal Mushroom Armillaria mellea.

Armillaria is one of the most common diseases underlying chronic root rot in woody plants. Although there is no particularly effective way to prevent it, soil disinfection is a common effective protective measure. However, Armillaria itself has important medicinal value and is a symbiotic fungus in the cultivation of Gastrodia elata and Polyporus umbellatus. Therefore, researching Armillaria is of great practical significance. In this review, the biological characteristics, cultivation methods, chemical components, food and medicinal value and efficacy of Armillaria were all reviewed, and its development and utilization direction were analyzed and discussed.

Enzymatic characteristics of immobilized carbonic anhydrase and its applications in CO2 conversion.

Native carbonic anhydrase (CA) has been widely used in several different applications due to its catalytic function in the interconversion of carbon dioxide (CO2) and carbonic acid. However, subject to its stability and recyclability, native CA often deactivates when in harsh environments, which restricts its applications in the commercial market. Maintaining the stability and high catalytic activity of CA is challenging. Immobilization provides an effective route that can improve enzymatic stability. Through the interaction of covalent bonds and van der Waals forces, water-soluble CA can be combined with various insoluble supports to form water-insoluble immobilized CA so that CA stability and utilization can be greatly improved. However, if the immobilization method or immobilization condition is not suitable, it often leads to a decrease in CA activity, reducing the application effects on CO2 conversion. In this review, we discuss existing immobilization methods and applications of immobilized CA in the environmental field, such as the mineralization of carbon dioxide and multienzyme cascade catalysis based on CA. Additionally, prospects in current development are outlined. Because of the many outstanding and superior properties after immobilization, CA is likely to be used in a wide variety of scientific and technical areas in the future.

Co-immobilization multienzyme nanoreactor with co-factor regeneration for conversion of CO2.

Multienzymatic conversion of carbon dioxide (CO2) into chemicals has been extensively studied. However, regeneration and reuse of co-factor are still the main problems for the efficient conversion of CO2. In this study, a nanoscale multienzyme reactor was constructed by encapsulating simultaneously carbonic anhydrase (CA), formate dehydrogenase (FateDH), co-factor (NADH), and glutamate dehydrogenases (GDH) into ZIF-8. In the multienzyme reactors, cationic polyelectrolyte (polyethyleneimine, PEI) was doped in the ZIF-8 by dissolving it in the precursors of ZIF-8. Co-factor (NADH) was anchored in ZIF-8 by ion exchange between PEI (positive charge) and co-factor (negative charge), and regenerated through GDH embedded in the ZIF-8, thus keeping high activity of FateDH. Activity recovery of FateDH in the multienzyme reactors reached 50%. Furthermore, the dissolution of CO2 in the reaction solution was increased significantly by the combination of CA and ZIF-8. As a result, the nanoscale multienzyme reactor exhibited superior capacity for conversion of CO2 to formate. Compared with free multienzyme system, formate yield was increased 4.6-fold by using the nanoscale multienzyme reactor. Furthermore, the nanoscale multienzyme reactor still retained 50% of its original productivity after 8 cycles, indicating excellent reusability.

Carbonic Anhydrase@ZIF-8 Hydrogel Composite Membrane with Improved Recycling and Stability for Efficient CO2 Capture.

In this study, carbonic anhydrase (CA, EC 4.2.1.1) molecules were embedded into metal-organic frameworks (MOFs) via co-precipitation (CA@ZIF-8), and then these CA@ZIF-8 nanocomposites were encapsulated in the poly(vinyl alcohol) (PVA)-chitosan (CS) hydrogel networks to prepare CA@ZIF-8-PVA-CS composite hydrogels (PVA/CS/CA@ZIF-8) with high activity, stability, and reusability. The immobilization efficiency of CA was greater than 70%, suggesting the high immobilization efficiency. The prepared PVA/CS/CA@ZIF-8 composite membranes displayed excellent higher stability against a high temperature, denaturants, and acid than free CA and CA@ZIF-8. Furthermore, these membranes exhibited an excellent performance for CO2 capture. The amount of calcium carbonate obtained by PVA/CS/CA@ZIF-8 hydrogel membranes was 20- and 1.63-fold than free CA and CA@ZIF-8 composites, respectively. Furthermore, the hydrogel membranes exhibited superior reusability and mechanical strength. The hydrogel membrane maitained 50% of its original activity after 11 cycles. However, CA@ZIF-8 completely lost activity. These results indicated that the PVA/CS/CA@ZIF-8 membranes can be efficiently applied to capture CO2 sequestration.

Bienzyme Magnetic Nanobiocatalyst with Fe3+-Tannic Acid Film for One-Pot Starch Hydrolysis.

In this study, a novel co-immobilization biocatalyst for one-pot starch hydrolysis was prepared through shielding enzymes on the Fe3O4/SiO2 core-shell nanospheres by a Fe3+-tannic acid (TA) film. In brief, α-amylase and glucoamylase were covalently immobilized on amino-modified Fe3O4/SiO2 core-shell nanospheres using glutarldehyde as a linker. Then, a Fe3+-TA protective film was formed through the self-assembly of the Fe3+ and TA coordination complex (Fe3+-TA@Fe3O4/SiO2-enzymes). The film acts a "coating" to prevent the enzyme from denaturation and detachment, thus significantly improving its structural and operational stability. Furthermore, the immobilization efficiency reached 90%, and the maximum activity recovery of α-amylase and glucoamylase was 87 and 85%, respectively. More importantly, the bienzyme magnetic nanobiocatalyst with Fe3+-TA film could be simply recovered by a magnet. The Fe3+-TA@Fe3O4/SiO2-enzymes kept 55% of the original activity after reuse for 9 cycles, indicating outstanding reusability. However, the bienzyme magnetic nanobiocatalyst without Fe3+-TA film maintained 28% of the initial activity.

Immobilized carbonic anhydrase on mesoporous cruciate flower-like metal organic framework for promoting CO2 sequestration.

CO2 capture by immobilized carbonic anhydrase (CA) has become an alternative and environmental friendly approach in CO2 sequestration technology. However, the immobilized CA usually exhibits low CO2 sequestration efficiency due to no gas adsorption function for the conventional CA supports. Metal organic frameworks (MOFs) are an excellent material for gas adsorption and enzyme immobilization. Herein, a combined immobilization system of CA and ZIF-8 with cruciate flower-like morphology for CO2 adsorption was prepared for the first time by adsorbing CA onto ZIF-8. The immobilization efficiency was greater than 95%, and the maximum activity recovery reached 75%, indicating the highly efficient immobilization process. The resultant CA@ZIF-8 composites exhibited outstanding thermostability, the tolerance against denaturants, and reusability compared with free CA. Furthermore, we demonstrated for the first time that the shape of ZIF-8 could be controlled by adjusting concentrations of Zn2+ ions at the high concentration of 2-methylimidazole (1 M). More importantly, we also demonstrated the applicability of the CA@ZIF-8 composites to the sequestration of CO2 in carbonate minerals. The yields of the CaCO3 obtained by using CA@ZIF-8 composites were 22-folds compared to free CA. Thus, this CA@ZIF-8 composite can be successfully used as a robust biocatalyst for sequestration of CO2.