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1.
J Biomech Eng ; 145(9)2023 09 01.
Article in English | MEDLINE | ID: mdl-37144887

ABSTRACT

Porous cages with lower global stiffness induce more bone ingrowth and enhance bone-implant anchorage. However, it's dangerous for spinal fusion cages, which usually act as stabilizers, to sacrifice global stiffness for bone ingrowth. Intentional design on internal mechanical environment might be a promising approach to promote osseointegration without undermining global stiffness excessively. In this study, three porous cages with different architectures were designed to provide distinct internal mechanical environments for bone remodeling during spinal fusion process. A design space optimization-topology optimization based algorithm was utilized to numerically reproduce the mechano-driven bone ingrowth process under three daily load cases, and the fusion outcomes were analyzed in terms of bone morphological parameters and bone-cage stability. Simulation results show that the uniform cage with higher compliance induces deeper bone ingrowth than the optimized graded cage. Whereas, the optimized graded cage with the lowest compliance exhibits the lowest stress at the bone-cage interface and better mechanical stability. Combining the advantages of both, the strain-enhanced cage with locally weakened struts offers extra mechanical stimulus while keeping relatively low compliance, leading to more bone formation and the best mechanical stability. Thus, the internal mechanical environment can be well-designed via tailoring architectures to promote bone ingrowth and achieve a long-term bone-scaffold stability.


Subject(s)
Osseointegration , Spinal Fusion , Porosity , Osteogenesis , Prostheses and Implants , Spinal Fusion/methods , Titanium
2.
J Biomech ; 136: 111078, 2022 05.
Article in English | MEDLINE | ID: mdl-35405418

ABSTRACT

Reliable and accurate predictions of bone remodeling provide essential assistance for personalized implant design and orthopedic diagnosis. However, the bone remodeling simulations fail to accurately mimic the sophisticated architecture of trabecular bone so far, due to the neglection of the stochastic behaviors of bone remodeling. In this study, we coupled the Physiological Stochasticity in Bone Remodeling into the conventional Topology Optimization algorithm (named PSBR-TO method) to predict the cancellous structure of human femur. The sensitivity function of topology optimization was amended according to the bone remodeling rules from in vivo study (Razi et al., 2015) to reflect the stochastic process of bone remodeling in various physiological conditions. To demonstrate the algorithm, the bone structures of adults and the elderly were simulated by adopting the corresponding remodeling rules. The results showed that PSBR-TO gives rise to highly similar morphological features with the natural femur bone, in terms of the trabecular orientations and bone content distribution. The predicted femurs for adults and the elderly showed that the region-dependent variations in trabecular structural parameters during aging, including BV/TV, Tb.Th, and Tb.Sp, were consistent with the natural bone. Additionally, a loading collection of thirteen activities was employed in the algorithm and succeeded in driving the femur model to reproduce cancellous structure without extra constraint of structure perimeter or local density. By means of PSBR-TO, the trabecular structure in diverse physiological conditions can be accurately predicted, showing the valuable contribution on the clinical diagnosis and patient-specific design of bone implants.


Subject(s)
Bone Remodeling , Femur , Adult , Aged , Algorithms , Bone Density , Bone and Bones , Computer Simulation , Femur/anatomy & histology , Humans
3.
J Agric Food Chem ; 70(12): 3785-3794, 2022 Mar 30.
Article in English | MEDLINE | ID: mdl-35302358

ABSTRACT

The hybrid coupling of biocatalysts and chemical catalysts plays a vital role in the fields of catalysis, sensing, and medical treatment due to the integrated advantages in the high activity of natural enzymes and the excellent stability of nanozymes. Herein, a new nanozyme/natural enzyme hybrid biosensor was established for ultrasensitive glutamate detection. The MIL-88B(Fe)-NH2 material with remarkable peroxidase mimic activity and stability was used as a nanozyme and carrier for immobilizing glutamate oxidase (GLOX) through Schiff base reaction to construct a chem-enzyme cascade detector (MIL-88B(Fe)-NH2@GLOX). The resultant MIL-88B(Fe)-NH2@GLOX exhibited a wide linear range (1-100 µM), with a low detection limit of 2.5 µM for glutamate detection. Furthermore, the MIL-88B(Fe)-NH2@GLOX displayed excellent reusability and storage stability. After repeated seven cycles, MIL-88B(Fe)-NH2-GLOX (GLOX was adsorbed on MIL-88B(Fe)-NH2) lost most of its activity, whereas MIL-88B(Fe)-NH2@GLOX still retained 69% of its initial activity. Meanwhile, MIL-88B(Fe)-NH2@GLOX maintained 60% of its initial activity after storage for 90 days, while free GLOX only retained 30% of its initial activity. This strategy of integrating MOF mimics and natural enzymes for cascade catalysis makes it possible to design an efficient and stable chemo-enzyme composite catalysts, which are promising for applications in biosensing and biomimetic catalysis.


Subject(s)
Biosensing Techniques , Metal-Organic Frameworks , Biomimetics , Catalysis , Glutamic Acid
4.
J Colloid Interface Sci ; 610: 709-718, 2022 Mar 15.
Article in English | MEDLINE | ID: mdl-34863543

ABSTRACT

Metal-organic frameworks (MOFs), with large specific surface area and tunable porosity, have gained lots of attention for immobilizing enzymes. However, the intrinsic open channels of most reported MOFs are generally smaller than 2 nm, which significantly prevents the passage of enzymes, and the diffusion efficiency of substrates and products. Here we report a new hierarchical micro-mesoporous zeolitic imidazolate framework-8 (ZIF-8) with core-shell superstructure (HZIF-8) using colloidal hydrated zinc sulfate (ZnSO4·7H2O) as a soft template for enzyme immobilization. The ZnSO4·7H2O forms an aggregation of colloids due to the self-conglobation effect in methanol, which affords a soft template for the formation of HZIF-8. Cytochrome C (Cyt C) was immobilized in interior of HZIF-8 through entrapment during the formation of HZIF-8. The resultant immobilized Cyt C (Cyt C@HZIF-8) exhibited 4-fold and 3-fold higher activity than free Cyt C and Cyt C encapsulated in conventional microporous ZIF-8 (Cyt C@ZIF-8), respectively. Meanwhile, the Km value of Cyt C@HZIF-8 significantly decreased due to the presence of mesopores compared with Cyt C@ZIF-8, indicating enhanced substrate affinity. After 7 cycles, Cyt C@HZIF-8 still maintained 70% of its initial activity whereas Cyt C@ZIF-8 only retained 10% of its initial activity. Moreover, the obtained HZIF-8 showed outstanding performance in co-immobilization of multi-enzyme for the detection of glucose.


Subject(s)
Metal-Organic Frameworks , Zeolites , Enzymes, Immobilized , Porosity , Sulfates
5.
J Colloid Interface Sci ; 602: 426-436, 2021 Nov 15.
Article in English | MEDLINE | ID: mdl-34144301

ABSTRACT

Inspired by the interfacial catalysis of lipase, Herein, the hydrophobic ZIF-L coated with polydimethylsiloxane (PDMS) were prepared by chemical vapor deposition (CVD) and used to immobilize lipase from Aspergillus oryzae (AOL) for biodiesel production. The results showed that the PDMS coating enhanced the stability of ZIF-8 and ZIF-L in PBS. Immobilization efficiency of AOL on PDMS-modified ZIF-L was 96% under optimized conditions. The resultant immobilized lipase (AOL@PDMS-ZIF-L) exhibited higher activity recovery (430%) than AOL@ZIF-L. Meanwhile, compared with free lipase, the AOL@PDMS-ZIF-L exhibited better storage stability and thermal stability. After 150 days of storage, the free lipase retained only 20% of its original activity of hydrolyzing p-NPP, while the AOL@PDMS-ZIF-L still retained 90% of its original activity. The biodiesel yield catalyzed from soybean oil by free lipase was only 69%, However, the biodiesel yield by AOL@PDMS-ZIF-L reached 94%, and could still be maintained at 85% even after 5 consecutive cycles. It is believed that this convenient and versatile strategy has great promise in the important fields of immobilized lipase on MOF for biodiesel production.


Subject(s)
Lipase , Metal-Organic Frameworks , Biofuels , Enzyme Stability , Enzymes, Immobilized/metabolism , Hydrophobic and Hydrophilic Interactions , Lipase/metabolism
6.
J Colloid Interface Sci ; 590: 436-445, 2021 May 15.
Article in English | MEDLINE | ID: mdl-33561593

ABSTRACT

Metal-organic frameworks (MOFs) have been emerged as a promising support for immobilizing enzymes owing to the tunable porosity, high surface area, and structural diversity. However, most of these possess nanometer size and small pores, which are difficult to recover them from the reaction medium and present low immobilization efficiency and protein loading capacity, and high substrate diffusion limitations. Herein, a novel magnetic amino-functionalized zeolitic imidazolate framework-8 (ZIF-8) with 3D highly ordered macroporous structure was synthesized using the assembled polystyrene (PS) nanosphere monoliths as a template. Subsequently, catalase (CAT) molecules were immobilized on the surface of macroporous magnetic ZIF-8 and inside the macropores by precipitation, covalent binding and cross-linking. The resultant immobilized CAT showed high immobilization efficiency (58%) and protein loading capacity (29%), leading to 500% higher activity than the immobilized CAT on ZIF-8 (CAT/ZIF-8). Meanwhile, the immobilized CAT could be easily recovered with a magnet without obvious activity loss. The traditional CAT/ZIF-8 lost its activity after 6 cycles, whereas, the immobilized CAT retained 90% activity of its initial activity after reusing for 8 cycles, indicating excellent reusability. In conclusion, this study provides a facile and efficient approach to immobilize enzymes on/in MOFs with enhanced activity and excellent recyclability.


Subject(s)
Metal-Organic Frameworks , Zeolites , Catalase , Enzymes, Immobilized , Magnetic Phenomena
7.
Int J Biol Macromol ; 155: 110-118, 2020 Jul 15.
Article in English | MEDLINE | ID: mdl-32220640

ABSTRACT

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.


Subject(s)
Bioreactors , Carbon Dioxide/chemistry , Enzymes, Immobilized/metabolism , Catalysis , Polyethyleneimine/chemistry
8.
Int J Biol Macromol ; 152: 207-222, 2020 Jun 01.
Article in English | MEDLINE | ID: mdl-32109471

ABSTRACT

As a highly efficient and environmentally friendly biocatalyst, immobilized lipase has received incredible interest among the biotechnology community for the production of biodiesel. Nanomaterials possess high enzyme loading, low mass transfer limitation, and good dispersibility, making them suitable biocatalytic supports for biodiesel production. In addition to traditional nanomaterials such as nano­silicon, magnetic nanoparticles and nano metal particles, novel nanostructured forms such as nanoflowers, carbon nanotubes, nanofibers and metal-organic frameworks (MOFs) have also been studied for biodiesel production in the recent years. However, some problems still exist that need to be overcome in achieving large-scale biodiesel production using immobilized lipase on/in nanomaterials. This article mainly presents an overview of the current and state-of-the-art research on biodiesel production by immobilized lipases in/on nanomaterials. Various immobilization strategies of lipase on various advanced nanomaterial supports and its applications in biodiesel production are highlighted. Influential factors such as source of lipase, immobilization methods, feedstocks, and production process are also critically discussed. Finally, the current challenges and future directions in developing immobilized lipase-based biocatalytic systems for high-level production of biodiesel from waste resources are also recommended.


Subject(s)
Biofuels , Enzymes, Immobilized/chemistry , Lipase/chemistry , Nanostructures/chemistry , Animals , Biocatalysis/drug effects , Biotechnology/methods , Metal-Organic Frameworks/chemistry , Nanotubes, Carbon/chemistry
9.
J Biotechnol ; 306: 54-61, 2019 Dec 20.
Article in English | MEDLINE | ID: mdl-31550490

ABSTRACT

Zeolitic imidazole frameworks (ZIFs) with tunable pore sizes and high surface areas have recently used as an effective support for immobilizing enzymes. However, the instability in the aqueous acidic environment has limited their practical applications in some cases. In this work, we develop a novel catalase/ZIFs composite with mesoporous silica shell (mSiO2@CAT/ZIFs) via co-precipitation, and controlled self-assembly of silanes. During preparation, the cetyltrimethylammonium bromide induced the formation of the mesostructured silica layer on the outer surface of CAT/ZIFs. The resultant mSiO2@CAT/ZIFs exhibited high activity recovery (92%). Compared with the conventional CAT/ZIFs and free CAT, mSiO2@CAT/ZIFs exhibited excellent acid resistance. For example, after 30 min in acetate buffer solution (pH 3.0), the CAT/ZIFs and free CAT almost lost activity whereas the mSiO2@CAT/ZIFs still retained 35% of original activity. Meanwhile, the thermostability of the mSiO2@CAT/ZIFs was enhanced significantly compared with conventional CAT/ZIFs. In addition, the mSiO2@CAT/ZIFs displayed excellent storage stability, and retained 60% of its initial activity after 15 days storage period. Furthermore, the mSiO2@CAT/ZIFs could maintain 70% of its initial activity after 8 continuous uses, demonstrating superior reusability than the free CAT and CAT/ZIFs. These results demonstrated that the mSiO2@CAT/ZIFs are potential for practical applications even in the acidic environment.


Subject(s)
Acids/chemistry , Enzymes, Immobilized/chemistry , Nanocomposites/chemistry , Silicon Dioxide/chemistry , Catalase/chemistry , Catalase/metabolism , Enzyme Stability , Enzymes, Immobilized/metabolism , Imidazoles/chemistry , Metal-Organic Frameworks/chemistry , Metal-Organic Frameworks/metabolism , Porosity , Silanes/chemistry
10.
J Agric Food Chem ; 66(33): 8753-8760, 2018 Aug 22.
Article in English | MEDLINE | ID: mdl-30052438

ABSTRACT

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.


Subject(s)
Starch/chemistry , Tannins/chemistry , Biocatalysis , Enzyme Stability , Enzymes, Immobilized/chemistry , Glucan 1,4-alpha-Glucosidase/chemistry , Hydrolysis , Magnetite Nanoparticles/chemistry , alpha-Amylases/chemistry
11.
Int J Biol Macromol ; 117: 673-682, 2018 Oct 01.
Article in English | MEDLINE | ID: mdl-29859841

ABSTRACT

Enzyme immobilization on the external surface of solid supports is a commonly adopted method to improve stability and reuse for continuous operations, which, however, is prone to cause the enzyme denaturation due to no carriers protection. Herein, we describe enzyme-shielding strategy to prepare hybrid organic/inorganic nanobiocatalysts; it exploits the self-assembly of silane building blocks at the surface of immobilized enzymes on Fe3O4/silica core-shell nanospheres to grow a protective silica layer. The silica shell around the immobilized enzyme particles provides a "shield" to protect from biological, thermal and chemical degradation for enzyme. As a result, the recycling of the immobilized catalase with a protective silica layer was improved remarkably compared with immobilized catalase without a protective silica layer. The immobilized catalase with a protective silica layer still remained 70% of their original activity after 9 cycles, whereas the immobilized catalase without a protective silica layer only retained 20% of their original activity. Moreover, the immobilized catalase with a protective silica layer exhibited significantly enhanced resistance to denaturing stresses (such as proteolytic agent, denaturants, and heat). Therefore, the enzyme-shielding strategy showed promising applications for preparing obtain stable and recycled nanobiocatalyst.


Subject(s)
Catalase/chemistry , Enzymes, Immobilized/chemistry , Nanospheres/chemistry , Silicon Dioxide/pharmacology , Biocatalysis , Enzyme Stability/drug effects , Ferric Compounds/chemistry , Ferric Compounds/pharmacology , Kinetics , Proteolysis/drug effects , Silicon Dioxide/chemistry
12.
Int J Biol Macromol ; 117: 189-198, 2018 Oct 01.
Article in English | MEDLINE | ID: mdl-29803747

ABSTRACT

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.


Subject(s)
Carbon Dioxide/chemistry , Carbon Dioxide/isolation & purification , Carbonic Anhydrases/chemistry , Enzymes, Immobilized/chemistry , Metal-Organic Frameworks/chemistry , Adsorption , Biocatalysis , Carbonic Anhydrases/metabolism , Enzymes, Immobilized/metabolism , Imidazoles/chemistry , Kinetics , Nanoparticles/chemistry , Porosity
13.
Polymers (Basel) ; 11(1)2018 Dec 25.
Article in English | MEDLINE | ID: mdl-30960011

ABSTRACT

Zeolitic imidazole framework-8 (ZIF-8) with tunable pore sizes and high surface areas have recently emerged as a promising support for immobilizing enzymes. However, the instability in the aqueous acidic environment and difficulty of recovery has limited their practical applications in some cases. In this study, catalase/ZIF-8 composites with a protective nanocoating were prepared by the controlled self-assembly of silanes or coordination complexes (tannic acid (TA) and Fe3+). The properties of the catalase (CAT)/ZIF-8 composites with a protective nanocoating were also determined. The recovered activity of CAT/ZIF-8 and CAT/ZIF-8 with protective nanocoating was 70% and 65%, respectively. Compared with the conventional CAT/ZIF-8 composites, CAT/ZIF-8 with protective nanocoating exhibited excellent acid resistance. For example, after treatment for 60 min in phosphate buffer solution (pH 3.0), CAT/ZIF-8 composites only maintained 20% of their initial activity (about 12 U/mg). However, CAT/ZIF-8 with a protective nanocoating could still retain about 50% of its initial activity (about 10 U/mg). Meanwhile, the thermostability and storage stability of the CAT/ZIF-8 composites was enhanced significantly due to the presence of nanocoating compared with conventional CAT/ZIF-8. More importantly, the CAT/ZIF-8 with a protective nanocoating retained 40% of its initial activity after 7 cycles, whereas CAT/ZIF-8 only retained 8% of the initial activity. The approach in this study could be an efficient strategy to prepare enzyme/ZIF-8 composites with both high acid resistance and excellent recyclability.

14.
ACS Appl Mater Interfaces ; 9(12): 10587-10594, 2017 Mar 29.
Article in English | MEDLINE | ID: mdl-28281743

ABSTRACT

Metal-organic frameworks (MOFs) have recently emerged as a promising candidates for the immobilization of enzymes due to their diversified structures and porosity. However, a lack of good size and morphological control over the as-prepared MOFs has limited their practical applications in some cases. Herein, instead of zeolitic imidazolate framework-8 (ZIF-8) with the standard rhombic dodecahedral morphology, we successfully synthesize a novel mesoporous catalase@ZIF composite with cruciate flower-like morphology by embedding catalase molecules into uniformly sized ZIF crystals. With extraordinarily large mesopore size and high protein loading capacity, the catalase@ZIF composites with cruciate flower-like morphology exhibit 400% higher activity than that of catalase@ZIF composites with conventional rhombic dodecahedral morphology, and show higher reusability than conventional rhombic dodecahedral morphology. More importantly, we demonstrate for the first time that the biomacromolecules (proteins) can not directly regulate the crystal size, morphology, and crystallinity of ZIF-8. Moreover, the crystal morphology of ZIF has primary dependence on concentrations of 2-methylimidazole and Zn2+ ions, and can be directly controlled by adjusting concentrations of Zn2+ ions while keeping the high concentration of 2-methylimidazole.


Subject(s)
Metal-Organic Frameworks/chemistry , Catalase , Enzymes, Immobilized , Porosity , Zeolites
15.
J Agric Food Chem ; 65(3): 618-625, 2017 Jan 25.
Article in English | MEDLINE | ID: mdl-28054483

ABSTRACT

Cross-linked enzyme aggregates (CLEAs) have recently emerged as a promising tool for enzyme immobilization because of their simplicity and low cost. However, a lack of good size and morphological control over the as-prepared CLEAs has limited their practical applications. For example, the prepared CLEAs exhibit amorphous large clusters that would cause significant mass-transfer limitations, which lead to a low catalytic efficiency. Here, inspired by biomineralized core-shell structures in nature, we develop a novel mesoporous spherical CLEA with a biosilica shell by using phenylalanine ammonia lyase based on CaCO3 microtemplates and biomimetic mineralization. The resultant CLEAs exhibited a spherical structure with good monodispersity instead of the amorphous clusters of conventional CLEAs and showed activity higher than that of conventional CLEAs. Moreover, the thermostability, tolerance against denaturants, and mechanical stability of the spherical CLEAs with a biosilica shell were enhanced significantly compared with those of conventional CLEAs. In particular, the spherical CLEAs with a biosilica shell retained 70% of their original activity after 13 cycles, whereas the conventional CLEAs retained only 35% of their original activity. This approach could be an efficient strategy for improving the catalytic properties of CLEAs.


Subject(s)
Fungal Proteins/chemistry , Phenylalanine Ammonia-Lyase/chemistry , Rhodotorula/enzymology , Silicon Dioxide/chemistry , Biocatalysis , Cross-Linking Reagents/chemistry , Enzyme Stability , Enzymes, Immobilized/chemistry , Hydrogen-Ion Concentration , Kinetics , Rhodotorula/chemistry
16.
Sci Rep ; 5: 14203, 2015 Sep 16.
Article in English | MEDLINE | ID: mdl-26374188

ABSTRACT

A novel enzyme immobilization approach was used to generate mesoporous enzymes-silica composite microparticles by co-entrapping gelatinized starch and cross-linked phenylalanine ammonia lyase (PAL) aggregates (CLEAs) containing gelatinized starch into biomemitic silica and subsequently removing the starch by α-amylase treatment. During the preparation process, the gelatinzed starch served as a pore-forming agent to create pores in CLEAs and biomimetic silica. The resulting mesoporous CLEAs-silica composite microparticles exhibited higher activity and stability than native PAL, conventional CLEAs, and PAL encapsulated in biomimetic silica. Furthermore, the mesoporous CLEAs-silica composite microparticles displayed good reusability due to its suitable size and mechanical properties, and had excellent stability for storage. The superior catalytic performances were attributed to the combinational unique structure from the intra-cross-linking among enzyme aggregates and hard mesoporous silica shell, which not only decreased the enzyme-support negative interaction and mass-transfer limitations, but also improved the mechanical properties and monodispersity. This approach will be highly beneficial for preparing various bioactive mesoporous composites with excellent catalytic performance.


Subject(s)
Enzymes, Immobilized , Nanoparticles , Phenylalanine Ammonia-Lyase , Silicon Dioxide , Enzyme Activation , Enzyme Stability , Kinetics , Nanoparticles/chemistry , Nanoparticles/ultrastructure , Phenylalanine Ammonia-Lyase/metabolism , Porosity , Silicon Dioxide/chemistry , Thermodynamics
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