One-pot synthesis of microporous nanoscale metal organic frameworks conjugated with laccase as a promising biocatalyst

Samui, Arpita; Sahu, Sumanta Kumar

doi:10.1039/c7nj03619a

Cited by 79 publications

(27 citation statements)

References 51 publications

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“…345 Enzymes immobilized in MOFs for biocatalysis are commonly reported in terms of their relative activity at each cycle by repeated initial rate measurements. 44,402,403 In batch processes, the reaction time typically is adjusted to reach a defined product concentration (e.g. maximum conversion).…”

Section: Structural Analysis and Localization Of Enzymes Immobilized ...mentioning

confidence: 99%

Metal–Organic Framework-Based Enzyme Biocomposites

et al. 2021

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Due to their efficiency, selectivity, and environmental sustainability, there are significant opportunities for enzymes in chemical synthesis and biotechnology. However, as the three-dimensional active structure of enzymes is predominantly maintained by weaker non-covalent interactions, thermal, pH and chemical stressors can modify or eliminate activity. Metal-organic Frameworks (MOFs), which are extended porous network materials assembled by a bottom-up building block approach from metal-based nodes and organic linkers, can be used to afford protection to enzymes. The self-assembled structures of MOFs can be used to encase an enzyme in a process called encapsulation when the MOF is synthesized in the presence of the biomolecule. Alternatively, enzymes can be infiltrated into mesoporous MOF structures or surface bound via covalent or non-covalent processes. Integration of MOF materials and enzymes in this way affords protection and allows the enzyme to maintain activity in challenge conditions (e.g. denaturing agents, elevated temperature, non-native pH and organic solvents). In addition to forming simple enzyme/MOF biocomposites, other materials can be introduced to the composites to improve recovery or facilitate advanced applications in sensing and fuel cell technology. This review canvasses enzyme protection via encapsulation, pore infiltration and surface adsorption and summarizes strategies to form multi-component composites. Also, given that enzyme/MOF biocomposites straddle materials chemistry and enzymology, this review provides an assessment of the characterization methodologies used for MOF-immobilized enzymes and identifies some key parameters to facilitate development of the field. CONTENTSMOF-based enzyme biocomposite compositions and the concept of encapsulation 3.MOF-based enzyme biocomposites formed via encapsulation 3.1.Templating methods 3.2.One-pot embedding (non-templated) 3.3.Parameters influencing the chemistry of enzyme@MOF biocomposites 3.3.1. Additives 3.3.2.Enzyme suface chemistry 3.3.3.MOF precusors and structures 3.4.Alternative synthesis strategies 4.Infiltration (post insertion of enzymes in preformed MOFs) 4.1.Early results and the advantages of MOFs for infiltration 4.2.Tuning the framework structure in infiltrated enzyme@MOF biocomposites 4.3.Towards applications of infiltrated enzyme@MOFs 5.Surface bound enzymes 5.1. Immobilization via physical adsorption 5.2. Immobilization via coordinate bonds 5.3. Immobilization via covalent bonding 5.4. Enzymatic activity upon surface-immobilization 6. Multicomponent biocomposites 7. Characterization of MOF immobilized enzymes 7.1. Overview 7.2. Key immobilization parameters 7.3. One-pot enzyme MOF formation 7.4. Highlights of MOF-immobilized enzyme performance 7.4.1. Experimental determination of key immobilization parameters 7.4.1.1. Determination of protein concentrations 7.4.1.2. Activity determination 7.4.2. Advanced characterization of immobilized enzymes 7.4.2.1. Apparent enzyme kinetics 7.4.2.2. Structural analysis and localization o...

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Section: Structural Analysis and Localization Of Enzymes Immobilized ...mentioning

confidence: 99%

Metal–Organic Framework-Based Enzyme Biocomposites

et al. 2021

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“…In this study, the validity of this in situ one-step methodology for enzyme immobilization onto NH 2 -MIL-53(Al) is extended to lipase CaLB (from Candida antarctica), which indeed is one of the most widely investigated enzymes in different immobilization processes [34][35][36]. Apart from our own studies using nanocrystalline NH 2 -MIL-53(Al) supports for enzymes [20,21], the MIL-53(Al) family has proved to be efficient in the immobilization of: (i) Laccase on NH 2 -MIL-53(Al), using our one-step room-temperature methodology [37]; (ii) laccase on meso-MIL-53(Al) by post-synthesis methods [38]; and (iii) luciferase on non-functionalized MIL-53(Al), also by post-synthesis methodology [39]. We also found excellent results for lipase in situ immobilization on the semi-crystalline support Fe-BTC [23], suggesting that this enzyme could be easily immobilized onto MOF supports.…”

Section: Introductionmentioning

confidence: 95%

Efficient One-Step Immobilization of CaLB Lipase over MOF Support NH2-MIL-53(Al)

et al. 2020

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Metal-organic framework (MOF) materials possess the widest versatility in structure, composition, and synthesis procedures amongst the known families of materials. On the other hand, the extraordinary affinity between MOFs and enzymes has led to widely investigating these materials as platforms to support these catalytic proteins in recent years. In this work, the MOF material NH2-MIL-53(Al) has been tested as a support to immobilize by one-step methodology (in situ) the enzyme lipase CaLB from Candida antarctica by employing conditions that are compatible with its enzymatic activity (room temperature, aqueous solution, and moderate pH values). Once the nature of the linker deprotonating agent or the synthesis time were optimized, the MOF material resulted in quite efficient entrapping of the lipase CaLB through this in situ approach (>85% of the present enzyme in the synthesis media) while the supported enzyme retained acceptable activity (29% compared to the free enzyme) and had scarce enzyme leaching. The equivalent post-synthetic method led to biocatalysts with lower enzyme loading values. These results make clear that the formation of MOF support in the presence of the enzyme to be immobilized substantially improves the efficiency of the biocatalysts support for retaining the enzyme and limits their leaching.

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“…The soluble enzyme completely loses activity after incubation for 1 h, whereas the immobilized BGL reserves its initial activity nearly 70% after incubation for 3 h and approximately 50% for 5 h. It has been proved that enzyme immobilized by CLEAs caused it more stable and catalyzed efficiently at high temperature [30]. Stable support-bound BGL could be applied for the enzyme immobilization with economical matrix [31]. Glutaraldehyde can cross-link proteins both inter-and intramolecularly, thereby the covalent cross-linking between the amino groups of the enzyme is provided, which is beneficial to the rigidification of its tertiary structure and, thus, higher stability [32].…”

Section: Thermostability and Reusabilitymentioning

confidence: 99%

Enhanced biochemical characteristics of β-glucosidase via adsorption and cross-linked enzyme aggregate for rapid cellobiose hydrolysis

Deng

et al. 2020

Bioprocess Biosyst Eng

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With proper design, immobilization can be useful tool to improve the stability of enzymes, and in certain cases even their activity, selectivity, productivity and economic viability. An immobilized β-glucosidase (BGL, EC 3.2.1.21) through matrix adsorption and cross-linked enzyme aggregate (ad-CLEA) technology is presented in this work. After adsorption and precipitation, BGL was immobilized to poly(glycidyl methacrylate-co-ethylenedimethacrylate) (P GMA/EDMA ) microparticles using glutaraldehyde as the cross-linker. Immobilized BGL exhibits lower apparent K m but much higher V max than that of the soluble enzyme, suggesting greater enzyme-substrate affinity and rapid velocity. Besides, ad-CLEA-BGL presents better thermostability retaining activity nearly 70% for 3 h and approximately 50% for 5 h at 70 °C, high operational reusability remaining more than 90% activity after nine uses and excellent storage stability holding about 95% activity after 45 days. Furthermore, the cellobiose is completely hydrolyzed within 1 h with ad-CLEA-BGL, which is significantly more efficient than soluble enzyme (about 4 h). Therefore, BGL was successfully immobilized on P GMA/EDMA microparticles with an ad-CLEA technology and the immobilization greatly enhances the biochemical characteristics. This work indicates promising application for ad-CLEA-BGL in utilizing agricultural remnants, bio-converting cellobiose to fermentable reducing sugar and ethanol production.

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One-pot synthesis of microporous nanoscale metal organic frameworks conjugated with laccase as a promising biocatalyst

Abstract: Fabrication of amine-functionalized NMOFs followed by immobilization of laccase, a multicopper oxidase,viaa one-pot synthetic procedure.

Cited by 79 publications

References 51 publications

Metal–Organic Framework-Based Enzyme Biocomposites

Metal–Organic Framework-Based Enzyme Biocomposites

Efficient One-Step Immobilization of CaLB Lipase over MOF Support NH2-MIL-53(Al)

Enhanced biochemical characteristics of β-glucosidase via adsorption and cross-linked enzyme aggregate for rapid cellobiose hydrolysis

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