Enzyme–Iron Oxide Nanoassemblies: A Review of Immobilization and Biocatalytic Applications
Abstract
:1. Introduction
2. Iron Oxide Magnetic Nanoplatforms
2.1. Stability and Coating Strategies
2.2. Coated versus Non-Coated Magnetic Nanoparticles and Their Comparative Performance in Biocatalytic Applications
3. Enzyme Immobilization Process: A Thermodynamic and Kinetic Viewpoint
3.1. Enzyme Immobilization Strategies
3.2. Thermodynamic Considerations in the Enzyme Adsorption Process
- Only a monolayer is formed, i.e., only one molecule is bound per binding site.
- The surface is homogeneous, so all binding centers are identical.
- The binding sites are independent, i.e., the adsorption of one molecule does not affect the adsorption of the next molecule.
- There is no competition for binding sites.
- Adsorption is reversible.
3.3. Kinetic and Thermodynamic Parameters of Immobilized Enzymes
4. Enzyme–Magnetite Nanohybrids for Catalytic Biotechnology
5. Enzyme–Magnetite Nanohybrids for Cancer Therapy
6. Conclusions
Author Contributions
Funding
Data Availability Statement
Conflicts of Interest
References
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Enzyme/Protein | Support | Isotherm Adjust | Kd (µM) | qmax (mg g−1) | Ref. |
---|---|---|---|---|---|
Cellulase | Langmuir | 370 | [92] | ||
430 | |||||
Bovine hemoglobin | Cu2+-EDTA-Fe3O4 | Langmuir and Freundlich (better fit results with Langmuir model) | - | 1277 | [114] |
(BHb) | |||||
Bovine serum albumin (BSA) | 311 | ||||
Lysozyme (Lyz) | 192 | ||||
Bovine hemoglobin | Fe3O4@ytterbium silicate microspheres | Langmuir and Freundlich (better fit results with Langmuir model) | - | 304.4 | [115] |
(BHb) | |||||
β-Lactoglobulin | ~75 | ||||
(β-Lac) | |||||
Lysozyme | ~60 | ||||
(Lyz) | |||||
α-Lactalbumin | ~50 | ||||
(α-Lac) | |||||
Bovine serum albumin (BSA) | ~45 | ||||
Fetuin | ~32 | ||||
Lysozyme | Fe3O4 | Langmuir and Freundlich (better fit results with Langmuir model) | 17.9 | 370.4 | [116] |
[C4MIM]-Fe3O4 | 3.8 | 400.0 | |||
[C6MIM]-Fe3O4 | 3.0 | 500.0 | |||
[C8MIM]-Fe3O4 | 6.0 | 526.3 | |||
Mms6 (magnetosome membrane specific protein) | SP35 (spherical magnetite nanoparticle) | Langmuir | 9.52 | 11.1 | [117] |
Lipase (BSA as standard protein) | Bare Fe3O4 | Langmuir | - | 19.3 | [118] |
Bovine serum albumin (BSA) | Nickel ferrite nanoparticles | Langmuir | - | 916 | [119] |
Lysozyme | Poly(sodium 4-styrenesulfonte) PSS@Fe3O4 | Langmuir and | - | 476.2 | [120] |
Ovalbumin | Freundlich | 4.5 | |||
Conalbumin | (better fit results with Langmuir model) | 1.8 | |||
α-amylase | Cellulose(28 wt.%)@Fe3O4 | Langmuir | - | 18.2 | [121] |
Ureasa | Fe3O4/SiO2/APTES | Langmuir | 0.12 | ~300 | [122] |
Fe3O4/SiO2/APTES/MTES | 0.063 | ~450 | |||
Fe3O4/SiO2/APTES/PTES | 0.08 | ~1000 | |||
Fe3O4/SiO2/TMPED | 5.0 | ~500 |
Enthalpy Contributions | |
---|---|
Electrostatic interaction | ΔH negligible vs. −TΔS |
Hydrophobic interaction | ΔH > 0 (unfavorable to a.p.) |
Entropy Contributions | |
Decrease in the translational, rotational and vibrational entropy | ΔSconfig < 0 (unfavorable to a.p.) |
Reduction in conformational stability of the adsorbed enzyme | ΔSconform > 0 (favorable to a.p.) |
Release of a large number of water molecules solvating both the nanoparticle surface and the residues exposed to the solvent by the enzyme | ΔShydrat > 0 (most favorable factor to a.p.) |
Enzyme/Protein | Support | Method of Determination | Kd (µM) | ΔH (kJ mol−1) | ΔS (kJ K−1 mol−1) | ΔG (kJ mol−1) | N | Ref. |
---|---|---|---|---|---|---|---|---|
Lysozyme | Fe3O4 | From adsorption isotherm at different temperatures | 17.9 | −12.3 | −0.036 | 1.72 | - | [116] |
[C4MIM]-Fe3O4 | 3.8 | 31.0 | 0.129 | −7.38 | ||||
[C6MIM]-Fe3O4 | 3.0 | 11.5 | 0.053 | −4.26 | ||||
[C8MIM]-Fe3O4 | 6.0 | 16.6 | 0.071 | −4.60 | ||||
BSA Lysozyme | DEAPA-Fe3O4 | ITC | - | ~0 | - | - | - | [124] |
PAA-Fe3O4 | - | ~2 kcal mol−1 | - | - | - | |||
DEAPA-Fe3O4 | - | ~0 | - | - | - | |||
PAA-Fe3O4 | 1p: 0.14 | 1p: −2.2 | 1p: 0.12 | 1p: −39.2 | 14.6 | |||
2p: 29.4 | 2p: −27.2 | 2p: −0.004 | 2p: −25.9 | 69.5 | ||||
HSA Human IgG | 5_Fe3O4-PAOZ | ITC | 3.1 | −320 | −1.0 | −31.6 | 2.2 | [125] |
8_Fe3O4-PAOZ | 34 | −240 | −0.7 | −25.6 | 7.0 | |||
5_Fe3O4-PAOZ | 1.6 | −340 | −1.0 | −34.1 | 1.1 | |||
8_Fe3O4-PAOZ | 0.4 | −110 | −0.26 | −36.5 | 0.9 | |||
Trypsin | PVPr-co-P4VP/Fe3O4 hydrogel | From adsorption isotherm at different temperatures | 316.4 (a) | 20.4 | 0.116 | −14.26 | - | [126] |
Enzyme/ Protein | Support | Method Immo. | Ed (kJ mol−1) | ΔH (kJ mol−1) | ΔS (kJ K−1 mol−1) | ΔG (kJ mol−1) | Km (mg/mL) | Vmax (µmol ml−1 min−1) | Reference | ||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
f | i | f | i | f | i | f | i | f | i | f | i | ||||
Catalase | Fe3O4/SiO2 | Covalent | - | - | - | - | - | - | - | - | 15.3 (mM) | 16.6 | 4.02 | 3.47 | [104] |
mSiO2@Fe3O4/SiO2 | 21.2 | 2.36 | |||||||||||||
α-amylase | CSM-Fe3O4 | Adsorption | 15.3 | 18.8 | 12.7 | 16.2 | −0.28 | −0.28 | 101.7 | 104.2 | 0.45 | 1.03 | 34.48 * | 15.4 * | [129] |
CSM-GLY-Fe3O4 | Covalent | 35.4 | 32.8 | −0.24 | 106.8 | 0.53 | 25.0 * | ||||||||
CSM-GLA-Fe3O4 | Covalent | 28.3 | 25.7 | −0.26 | 106.4 | 0.57 | 19.6 * | ||||||||
CSM-CSM-Fe3O4 | Covalent | 23.6 | 21.0 | −0.27 | 104.8 | 0.65 | 16.4 * | ||||||||
Candida rugosa lipase (CRL) | AP-SiO2-Fe3O4 | Covalent | 93.3 | 112.9 | 87.7 | 110.3 | 233.7 | 293.2 | 14.6 | 17.0 | 6000 | 583 | 3330 | 833.3 | [130] |
Inulinase | GSH-Au-Fe3O4 | Covalent | - | - | - | - | - | - | - | - | 5.4 | 6.8 | 3.55 | 3.03 | [131] |
α-amylase | GO-Fe3O4 | Covalent | 85.4 | 79.0 | 74.2 | 79.1 | −0.17 | −0.14 | 114.3 | 106.2 | 0.6 | 0.9 | 450 | 333.3 | [132] |
β-Glucosidase | Bare Fe3O4 | Covalent | - | - | - | - | - | - | - | - | 3.5 (mM) | 4.3 (mM) | 0.72 | 0.89 | [133] |
Candida rugosa lipase (CRL) | A-SiO2-Fe3O4 | Covalent | 113.9 (ag.) | 128.5 | 111.2 (ag.) | 122.8 | 0.29 (ag.) | 0.32 | 16.8 (ag.) | 18.3 | 13.8 (mM) | 18.0 (mM) | 0.30 | 0.28 | [134] |
Laccase | Fe3O4-SiO2-AP | Covalent | - | - | - | - | - | - | - | - | 0.0015 (mM) | 0.0062 (mM) | 0.32 | 0.062 | [135] |
α-amylase | ZnO-Fe3O4 | Adsorption | 18.9 | 21.6 | 15.5 | 18.8 | −0.28 | −0.28 | 108.3 | 110.9 | 0.61 | 0.65 | 18.7 mg ml−1 min−1 | 18.2 mg ml−1 min−1 | [136] |
Candida rugosa lipase (CRL) | SiO2/Fe3O4/GO | Covalent | 27.6 | 32.3 | 25.0 | 29.7 | 0.035 | 0.048 | 13.8 | 14.5 | - | - | - | - | [137] |
Enzyme | Coating Reagent | Fe3O4 Preparation Method | Immobilization Method | Application Field | Specific Applications | Ref. |
---|---|---|---|---|---|---|
Lipase A | Chitosan | Co-precipitation | Covalent (Glutaraldehyde) | Industry | Biolubricants production | [3] |
Lipase A Lipase B | APTES | Co-precipitation | Covalent (Glutaraldehyde) | Industry | Ethyl butyrate production | [20] |
Catalase | Silica (TMOS, APTES) | Solvothermal | Covalent (Glutaraldehyde) | Scientific purpose | Enzyme shielding | [104] |
Lipase | Silica magnetic nanoparticles on (3-glycidoxypropyl) trimethoxylsilane (GPTMS) | Co-precipitation | Covalently (Epoxy groups/nucleophilic groups on the surface of enzyme) | Industry | Biodiesel production | [141] |
Pectinase | Polyethilene glycole (PEG) | Co-precipitation | Covalent (trichlorotriazine Cyanuric chloride) | Industry | Fruit juice clarification | [142] |
Tissue plasminogen activator (tPA) | Silica (TEOS, PEG, TREG) | Oxidation-precipitation | Covalent (NHSS-EDC and tresyl chloride) | Medicine | Treatment of thrombosis in coronary arteries | [143] |
Fibrinolytic protease (FP) | Polyaniline | Precipitation | Covalent (Glutaraldehyde) | Medicine | Treatment of cardiovascular diseases (degradation of the γ chain of human fibrinogen) | [144] |
Glucose oxidase (GOx) | - | Co-precipitation | Adsorption | Industry | Removal of acid yellow 12 | [145] |
Glucose oxidase (GOx) | Magnetic nanoparticles (EM1-100/40) | Purchased from Merck Co. | Covalent | Scientific purpose | Study of enzyme inactivation | [146] |
Lipase | Polymer-coating (Gum Arabic) | Co-precipitation | Covalent (Glutaraldehyde) | Industry | Biocatalyst a flavor ester, production | [147] |
Lipase | AGMNP-Co2+ | Co-precipitation | Metal chelate affinity | Industry | Biodiesel production | [148] |
Lipase | Polyaniline (Pani) | Co-precipitation | Adsorption | Scientific purpose | Enzyme adsorption | [149] |
β-fructofuranosidase | Chitosan | Co-precipitation | Adsorption | Industry | Produce fructooligosaccharides (growth of desirable gut microflora) | [150] |
Tripsin | Gallic acid (GA) | Co-precipitation | Adsorption | Industry | Hydrolysis of bovine milk | [151] |
L-Asparaginase | Amine-functionalized silane modifier, APTES | Co-precipitation | Covalent | Industry | Reduce acrylamide content in the food system (carcinogen and neurotoxin) | [152] |
β-agarase | Tannic acid (TA) | Co-precipitation | Adsorption | Industry | Bioactive neogaro-oligosaccharide (varying antioxidant activities) | [153] |
D-allullose-3-epimerase | ZIF67 (MOF) | Solvothermal | Encapsulation into ZIF67 (Chemical bonds Co2+) | Industry | Preparation of D-allulose (rare low-calorie sugar) | [154] |
Horseradish peroxidase (HRP) | Polymethil methacrylate (PMMA) | Purchased from Sigma-Aldrich | Encapsulation | Industry | Removal of wastewater aromatic pollutants | [155] |
Ene-reductase | Non-functionalized MNP (After add (HR)4tag) | Co-precipitation | Adsorption | Scientific purpose | Study enzyme immobilization | [156] |
Sortase A | Peptide | Co-precipitation | Covalent | Scientific purpose | Produce and bioquemically characterize immobilized proteins (single-molecule FRET) | [157] |
β-D-galactosidase (lactase) | Fe3O4–chitosan (Fe3O4–CS) | Co-precipitation | Covalent (Glutaraldehyde) | Industry | Galactooligosaccharides (GOS) production | [158] |
Tyrosinase | Magnetic beads poly(GMA–MMA) | Co-precipitation | Covalent ((Glutaraldehyde) | Industry | L-Dopa (1-3,4-dihydroxy phenylalanine) | [159] |
Enzyme | Coating Reagent | Fe3O4 Preparation Method | Immobilization Method | Specific Applications | Ref. |
---|---|---|---|---|---|
Glucose oxidase (GOx) | Silica (TEOS, EPTES) | Co-precipitation | Covalent (Glutaraldehyde) | Cytotoxic study for biomedical applications | [176] |
Choline-binding domain of N-acetylmuramoyl-L-alanine amidase–D-amino acid oxidase (CLytA-DAAO) | Diethilaminoethanol (DEAE) | Purchased from Chemicell GmbH (Berlin, Germany) | Adsorption (between CLytA domain and DEAE) | Anticancer therapy for pancreatic and colorectal carcinoma and glioblastoma | [177] |
LDHA (isoenzyme of Lactate Dehidrogenase, LDH) | Amino groups (APTES) | Co-precipitation | Covalent (Glutaraldehyde) | Cancer treatment (identification of LDH inhibitors) | [178] |
β-Glucosidase | Polyethylene glycol, PEG (by hydroxysuccinimide chemistry) | Purchased from Chemicell GmbH (Berlin, Germany) | Covalent (Glutaraldehyde) | Enzyme/Prodrug therapy in cancer | [179] |
L-Asparaginase | Poly(2-vinyl-4,4-dimethylazlactone | Co-precipitation | Covalent | Construct an efficient enzyme reactor (potential application in leukemia treatment) | [180] |
L-Asparaginase | Poly(HEMA-GMA) | Purchased from Sigma-Aldrich (St. Louis, MO, USA) | Covalent | Lymphoblastic leukemia (Remove L-Asparagine, an essential factor of protein synthesis) | [181] |
Glucose oxidase (GOx) | Fe3O4@PDA | Purchased from Sigma-Aldrich St. Louis, MO, USA) | Adsorption | Cancer treatment | [182] |
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Valls-Chivas, Á.; Gómez, J.; Garcia-Peiro, J.I.; Hornos, F.; Hueso, J.L. Enzyme–Iron Oxide Nanoassemblies: A Review of Immobilization and Biocatalytic Applications. Catalysts 2023, 13, 980. https://doi.org/10.3390/catal13060980
Valls-Chivas Á, Gómez J, Garcia-Peiro JI, Hornos F, Hueso JL. Enzyme–Iron Oxide Nanoassemblies: A Review of Immobilization and Biocatalytic Applications. Catalysts. 2023; 13(6):980. https://doi.org/10.3390/catal13060980
Chicago/Turabian StyleValls-Chivas, Ángeles, Javier Gómez, Jose I. Garcia-Peiro, Felipe Hornos, and Jose L. Hueso. 2023. "Enzyme–Iron Oxide Nanoassemblies: A Review of Immobilization and Biocatalytic Applications" Catalysts 13, no. 6: 980. https://doi.org/10.3390/catal13060980