MOFs as Potential Matrices in Cyclodextrin Glycosyltransferase Immobilization
Abstract
:1. Introduction
2. Cyclodextrin Glycosyltransferase
Sources and Properties
3. CGTase Immobilization
3.1. Supports Used for CGTase Immobilization
Support | Source of CGTase | Optimum pH | Optimum Temperature (°C) | Activity of Immobilized Enzyme (U/g-Support) | Maximum Yield of CD (%) | Reusability Studies (% of Initial Activity Retained after Cycles) | Ref. |
---|---|---|---|---|---|---|---|
Physical Adsorption | |||||||
Polyvinylidene difluoride hollow fiber | Bacillus lincheniformis | 7.0 | 25 | n.r | 69.37 | n.r | [43] |
Covalent Attachment | |||||||
Cellulose nanofiber | Bacillus macerans | n.r. | 70 | 159.34 | 69 (α) | 68% after 10 cycles | [44] |
Trisoperl (activated porous glass) | 5.1 | 48 | 3.0 | ~85 (β) | 68% after 20 cycles | [36] | |
Aminated polyvinylchloride (PVC) | 6 | 75 | 121 | 15.6 | 85% after 14 cycles | [37] | |
Fe3O4@PEI-PDA | Bacillus pseudalcaliphilus | 6.0 | 55 | 300 | 88.9 (β) | 19% after 9 cycles | [13] |
Resin (FE 4611) | 6–8 | ~58 | ≤ 2 | 14 | n.r. | [38] | |
Glutaraldehyde-pre-activated silica | Thermoanaerobacter sp. | 4.0–8.0 | n.r. | 101.73 | n.r. | n.r. | [35] |
Glyoxyl-agarose | 6.0 | 85 | 27.38 | 85.4 (β) | [40] | ||
Functionalized magnetic double mesoporous core-shell silica | Amphibacillus sp. | 8.5 | 55 | n.r. | n.r. | 56% after 10 cycles | [45] |
Entrapment | |||||||
Calcium alginate beads | Bacillus maceran | 7.5 | 60 | n.r. | n.r. | 75% after 7 cycles | [46] |
Aspergillus oryzae | 4.0 | 40 | 2760.4 U/mL | n.r. | 57% after 12 cycles | [39] |
3.2. Immobilization Technique
4. Metal-Organic Frameworks
Types and Properties
5. Conclusions
Funding
Conflicts of Interest
References
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Bacteria | Type of CGTase | Optimum Condition | Reference |
---|---|---|---|
Bacillus licheniformis | α-CGTase | 40 °C, pH 6.0–8.0 | [14] |
Bacillus circulans | β-CGTase | 56 °C, pH 6.4 | [1] |
Bacillus sp. | β-CGTase | 55 °C, pH 5.0 | [15] |
Bacillus agaradhaerens | β-CGTase | 55 °C, pH 9.0 | [16] |
Bacillus megaterium | β-CGTase | 60 °C, pH 7.2 | [17] |
Bacillus subtilis | γ-CGTase | 65 °C, pH 8.0 | [18] |
Bacillus firmus strain 290-3 | β/γ-CGTase | 60 °C, pH 6–8 | [19] |
Paenibacillus macerans | α-CGTase | 45 °C, pH 6.0–10 | [20] |
Thermoanaerobacterium thermosulfurigenes | α-CGTase | 80–85 °C, pH 4.5–7.0 | [21] |
Geobacillus thermoglucosidans | β-CGTase | 65–70 °C, pH 5.5 | [10] |
Brevibacillus brevis strain CD162 | β/γ-CGTase | 55 °C, pH 8.0 | [22] |
B. macorous strain WSH02–06 | γ-CGTase | 50 °C, pH 6.5 | [23] |
Brevibacterium sp. strain 9605 | γ-CGTase | 45 °C, pH 10 | [24] |
Immobilization Method | Binding Characteristics | Advantages | Disadvantages |
---|---|---|---|
Physical adsorption [59,60] | Weak bonds by either van der Waals or ionic interactions |
|
|
Covalent binding [61] | Chemical attachment between functional groups on support and enzyme |
|
|
Entrapment/encapsulation [62,63] | Inclusion of enzyme within the supports structure |
|
|
Cross-linking [64,65] | Aggregate/cluster of enzyme cross-linked by a functional reactant |
|
|
Synthesis Method | Advantages | Disadvantages | Examples of MOFs |
---|---|---|---|
Solvothermal |
|
| ZIF-95 [93] ZIF-78 [94] |
Microwave-assisted |
|
| VSB-1, VSB-5 [95] IRMOF-1, IRMOF-2, IRMOF-3 [96] Zr-UiO-66 [97] Hf-UiO-66 |
Sonochemical/Ultrasonic |
|
| TMU-46, TMU-47, TMU-48 [98] |
Mechanochemical |
|
| Copper isonicotinate Cu(INA)2 [99] Copper benzenetricarboxylate Cu3(BTC)2 [100] Cd(II)-based MOFs [87] |
Electrochemical |
|
| UiO-66 [101] Cu3(BTC)2 [102] |
Slow diffusion |
|
| Zn3(BDC)3.6CH3OH [103] |
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Ogunbadejo, B.; Al-Zuhair, S. MOFs as Potential Matrices in Cyclodextrin Glycosyltransferase Immobilization. Molecules 2021, 26, 680. https://doi.org/10.3390/molecules26030680
Ogunbadejo B, Al-Zuhair S. MOFs as Potential Matrices in Cyclodextrin Glycosyltransferase Immobilization. Molecules. 2021; 26(3):680. https://doi.org/10.3390/molecules26030680
Chicago/Turabian StyleOgunbadejo, Babatunde, and Sulaiman Al-Zuhair. 2021. "MOFs as Potential Matrices in Cyclodextrin Glycosyltransferase Immobilization" Molecules 26, no. 3: 680. https://doi.org/10.3390/molecules26030680