Isocyanide-based multi-component reactions for carrier-free and carrier-bound covalent immobilization of enzymes

Mehdi Mohammadi, Mansour Shahedi, Faezeh Ahrari, Mostafa Mostafavi, Zohreh Habibi, Maryam Yousefi

Published: 2023-02-28 DOI: 10.1038/s41596-023-00812-z

Isocyanide-based reactions

Enzyme immobilization

Covalent coupling

Multi-component reactions

Functional groups

AI 解读

Efficient and safe single-cell cloning of human pluripotent stem cells using the CEPT cocktail

Profiling native pulmonary basement membrane stiffness using atomic force microscopy

Genetic circuit design automation with Cello 2.0

Synthesis of siRNA nanoparticles to silence plaque-destabilizing gene in atherosclerotic lesional macrophages

Scalable dual-omics profiling with single-nucleus chromatin accessibility and mRNA expression sequencing 2 (SNARE-seq2)

A practical guide to scanning light-field microscopy with digital adaptive optics

Effective high-throughput isolation of fully human antibodies targeting infectious pathogens

Improved sampling and DNA extraction procedures for microbiome analysis in food-processing environments

MOF-derived nanoporous carbons with diverse tunable nanoarchitectures

Tutorial: a statistical genetics guide to identifying HLA alleles driving complex disease

查看全部

Sections

Figures

References

Strategies for the covalent immobilization of enzymes depend on the type of functional group selected to perform the coupling reaction, and on the relative importance of selectivity, loading capacity, immobilization time and activity/stability of the resu
Introduction
Materials
Procedure
Troubleshooting
Anticipated results
References
ACKNOWLEDGMENTS

Bolivar, J. M., Woodley, J. M. & Fernandez-Lafuente, R. Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization. Chem. Soc. Rev. 51, 6251–6290 (2022).
Souza, P. M. P. et al. Enzyme-support interactions and inactivation conditions determine Thermomyces lanuginosus lipase inactivation pathways: functional and florescence studies. Int. J. Biol. Macromol. 191, 79–91 (2021).
Sheldon, R. A. & van Pelt, S. Enzyme immobilisation in biocatalysis: why, what and how. Chem. Soc. Rev. 42, 6223–6235 (2013).
Rodrigues, R. C. et al. Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions. Biotechnol. Adv. 37, 746–770 (2019).
Guzik, U., Hupert-Kocurek, K. & Wojcieszyńska, D. Immobilization as a strategy for improving enzyme properties—application to oxidoreductases. Molecules 19, 8995–9018 (2014).
da Fonseca, A. M. et al. Synthesis, biological activity, and in silico study of bioesters derived from bixin by the CALB enzyme. Biointerface Res. Appl. Chem. 12, 5901–5917 (2022).
Sheldon, R. A., Basso, A. & Brady, D. New frontiers in enzyme immobilisation: robust biocatalysts for a circular bio-based economy. Chem. Soc. Rev. 50, 5850–5862 (2021).
Cao, L. Carrier-Bound Immobilized Enzymes: Principles, Application and Design (John Wiley & Sons, 2006).
Monteiro, R. R. et al. Improvement of enzymatic activity and stability of lipase A from Candida antartica onto halloysite nanotubes with Taguchi method for optimized immobilization. Appl. Clay Sci. 228, 106634 (2022).
Pierre, S. J. et al. Covalent enzyme immobilization onto photopolymerized highly porous monoliths. Adv. Mater. 18, 1822–1826 (2006).
Silva, A. R. et al. The chemistry and applications of metal–organic frameworks (MOFs) as industrial enzyme immobilization systems. Molecules 27, 4529 (2022).
Nunes, Y. L. et al. Chemical and physical chitosan modification for designing enzymatic industrial biocatalysts: how to choose the best strategy? Int. J. Biol. Macromol. 181, 1124–1170 (2021).
Mohammadi, M. et al. Rapid and high-density covalent immobilization of Rhizomucor miehei lipase using a multi component reaction: application in biodiesel production. RSC Adv. 5, 32698–32705 (2015).
Mohammadi, M., Gandomkar, S., Habibi, Z. & Yousefi, M. One pot three-component reaction for covalent immobilization of enzymes: application of immobilized lipases for kinetic resolution of rac-ibuprofen. RSC Adv. 6, 52838–52849 (2016).
Mohammadi, M., Ashjari, M., Garmroodi, M., Yousefi, M. & Karkhane, A. A. The use of isocyanide-based multicomponent reaction for covalent immobilization of Rhizomucor miehei lipase on multiwall carbon nanotubes and graphene nanosheets. RSC Adv. 6, 72275–72285 (2016).
Zhu, J. & Bienaymé, H. Multicomponent Reactions (John Wiley & Sons, 2006).
Ashjari, M., Garmroodi, M., Ahrari, F., Yousefi, M. & Mohammadi, M. Soluble enzyme cross-linking via multi-component reactions: a new generation of cross-linked enzymes. Chem. Commun. 56, 9683–9686 (2020).
Ahrari, F., Yousefi, M., Habibi, Z. & Mohammadi, M. Application of undecanedicarboxylic acid to prepare cross-linked enzymes (CLEs) of Rhizomucor miehei lipase (RML); selective enrichment of polyunsaturated fatty acids. Mol. Catal. 520, 112172 (2022).
Chen, N. et al. Cross-linked enzyme aggregates immobilization: preparation, characterization, and applications. Crit. Rev. Biotechnol. 1–15 (2022).
Jegan Roy, J. & Emilia Abraham, T. Strategies in making cross-linked enzyme crystals. Chem. Rev. 104, 3705–3722 (2004).
Noori, R., Perwez, M. & Sardar, M. Cross-linked enzyme aggregates: current developments and applications. Biocatalysis 83–112 (2019).
Jiaojiao, X., Yan, Y., Bin, Z. & Feng, L. Improved catalytic performance of carrier-free immobilized lipase by advanced cross-linked enzyme aggregates technology. Bioprocess Biosyst. Eng. 45, 147–158 (2022).
Mateo, C. et al. Immobilization of enzymes on heterofunctional epoxy supports. Nat. Protoc. 2, 1022–1033 (2007).
Moosavi, F., Ahrari, F., Ahmadian, G. & Mohammadi, M. Sortase-mediated immobilization of Candida antarctica lipase B (CalB) on graphene oxide; comparison with chemical approach. Biotechnol. Rep. 34, e00733 (2022).
Fernandez-Lorente, G. et al. Solid-phase chemical amination of a lipase from Bacillus thermocatenulatus to improve its stabilization via covalent immobilization on highly activated glyoxyl-agarose. Biomacromolecules 9, 2553–2561 (2008).
Zimmermann, J. L., Nicolaus, T., Neuert, G. & Blank, K. Thiol-based, site-specific and covalent immobilization of biomolecules for single-molecule experiments. Nat. Protoc. 5, 975–985 (2010).
Amini, Y. et al. A multi-component reaction for covalent immobilization of lipases on amine-functionalized magnetic nanoparticles: production of biodiesel from waste cooking oil. Bioresour. Bioprocess. 9, 1–15 (2022).
Gao, Z. et al. Co-immobilization of laccase and TEMPO onto amino-functionalized magnetic Fe3O4 nanoparticles and its application in acid fuchsin decolorization. Bioresour. Bioprocess. 5, 1–8 (2018).
Vashist, S. K., Lam, E., Hrapovic, S., Male, K. B. & Luong, J. H. Immobilization of antibodies and enzymes on 3-aminopropyltriethoxysilane-functionalized bioanalytical platforms for biosensors and diagnostics. Chem. Rev. 114, 11083–11130 (2014).
Moreira, Kd. S. et al. Taguchi design-assisted co-immobilization of lipase A and B from Candida antarctica onto chitosan: characterization, kinetic resolution application, and docking studies. Chem. Eng. Res. Des. 177, 223–244 (2022).
Kannan, K. & Jasra, R. V. Improved catalytic hydrolysis of carboxy methyl cellulose using cellulase immobilized on functionalized meso cellular foam. J. Porous Mater. 18, 409–416 (2011).
Habibi, Z., Mohammadi, M. & Yousefi, M. Enzymatic hydrolysis of racemic ibuprofen esters using Rhizomucor miehei lipase immobilized on different supports. Process Biochem. 48, 669–676 (2013).
Mohammadi, M., Habibi, Z., Gandomkar, S. & Yousefi, M. A novel approach for bioconjugation of Rhizomucor miehei lipase (RML) onto amine-functionalized supports; application for enantioselective resolution of rac-ibuprofen. Int. J. Biol. Macromol. 117, 523–531 (2018).
Barbosa, O. et al. Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties. Biomacromolecules 14, 2433–2462 (2013).
Shahedi, M., Yousefi, M., Habibi, Z., Mohammadi, M. & As’ habi, M. A. Co-immobilization of Rhizomucor miehei lipase and Candida antarctica lipase B and optimization of biocatalytic biodiesel production from palm oil using response surface methodology. Renew. Energy 141, 847–857 (2019).
Babaki, M., Yousefi, M., Habibi, Z., Brask, J. & Mohammadi, M. Preparation of highly reusable biocatalysts by immobilization of lipases on epoxy-functionalized silica for production of biodiesel from canola oil. Biochem. Eng. J. 101, 23–31 (2015).
Ramon-Marquez, T., Medina-Castillo, A. L., Fernandez-Sanchez, J. F. & Fernández-Gutiérrez, A. Evaluation of different functional groups for covalent immobilization of enzymes in the development of biosensors with oxygen optical transduction. Anal. Methods 7, 2943–2949 (2015).
Kutorglo, E. M. et al. Carboxyethyl-functionalized 3D porous polypyrrole synthesized using a porogen-free method for covalent immobilization of urease. Micropor. Mesopor. Mat. 311, 110690 (2021).
Je, H. H. et al. Cellulose nanofibers for magnetically-separable and highly loaded enzyme immobilization. Chem. Eng. J. 323, 425–433 (2017).
Orrego, A. H. et al. Stabilization of enzymes by multipoint covalent attachment on aldehyde-supports: 2-picoline borane as an alternative reducing agent. Catalysts 8, 333 (2018).
Bolivar, J. M. et al. Stabilization of a formate dehydrogenase by covalent immobilization on highly activated glyoxyl-agarose supports. Biomacromolecules 7, 669–673 (2006).
Ashjari, M. et al. Application of multi-component reaction for covalent immobilization of two lipases on aldehyde-functionalized magnetic nanoparticles; production of biodiesel from waste cooking oil. Process Biochem. 90, 156–167 (2020).
Barbosa, O. et al. Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization. RSC Adv. 4, 1583–1600 (2014).
Salami, F., Habibi, Z., Yousefi, M. & Mohammadi, M. Covalent immobilization of laccase by one pot three component reaction and its application in the decolorization of textile dyes. Int. J. Biol. Macromol. 120, 144–151 (2018).
Weltz, J. S., Kienle, D. F., Schwartz, D. K. & Kaar, J. L. Reduced enzyme dynamics upon multipoint covalent immobilization leads to stability-activity trade-off. J. Am. Chem. Soc. 142, 3463–3471 (2020).

Isocyanide-based multi-component reactions for carrier-free and carrier-bound covalent immobilization of enzymes

推荐阅读