Recent Trends in Enzyme Immobilization—Concepts for Expanding the Biocatalysis Toolbox
Abstract
:1. Introduction
2. Discussion: Novel Support Technologies
2.1. Polysaccharides
2.2. DNA
2.3. Chitosan
2.4. Renewables
2.5. Metal–Organic Frameworks
2.6. Controlled Pore Glass
2.7. Magnetic Nanoparticles
3. Integrating Immobilization into Develo** Biocatalytic Technology
3.1. Flow Biocatalysis
3.2. 3D-Printed Biocatalytic Scaffolds
3.3. Multi-Enzymatic Cascade Reactions
3.4. Integrating Enzyme Immobilization and Protein Engineering
4. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Conflicts of Interest
References
- Mix, S.; Moody, T.S.; Taylor, S.J. Biocatalysis—How Secret Should It Be? Chemical Knowledge Hub. Available online: https://www.chemicalsknowledgehub.com/article/14595/ (accessed on 16 August 2020).
- Mullin, R.; Moody, T.S. Ticking a new box in enzyme chemistry. Chem. Eng. News 2019, 97, 34–35. [Google Scholar]
- Moody, T.; Mix, S. Managing and redesigning chemical processes with enzymes. Spec. Chem. Mag. 2019, 22–25. Available online: https://www.specchemonline.com/ (accessed on 16 August 2020).
- Wu, S.; Snajdrova, R.; Moore, J.C.; Baldenius, K.; Bornscheuer, U.T. Biocatalysis: Enzymatic Synthesis for Industrial Applications. Angew. Chem. Int. Ed. 2021, 60, 88–119. [Google Scholar] [CrossRef] [PubMed]
- Federsel, H.-J.; Pesti, J.; Thompson, M.P. Immobilized Enzymes: Application in Organic Synthesis. In Catalyst Immobilization. Methods and Applications; Benaglia, M., Puglisi, A., Eds.; Wiley-VCH: Weinheim, Germany, 2020; Chapter 13; pp. 437–463. [Google Scholar] [CrossRef]
- Salvi, H.M.; Yadav, G.D. Process intensification using immobilized enzymes for the development of white biotechnology. Catal. Sci. Technol. 2021, 11, 1994–2020. [Google Scholar] [CrossRef]
- Bilal, M.; Iqbal, H.M. Naturally-derived biopolymers: Potential platforms for enzyme immobilization. Int. J. Biol. Macromol. 2019, 130, 462–482. [Google Scholar] [CrossRef] [PubMed]
- Reis, C.; Sousa, E.; Serpa, J.; Oliveira, R.; Santos, J. Design of immobilized enzyme biocatalysts: Drawbacks and opportunities. Química Nova 2019, 42, 768–783. [Google Scholar] [CrossRef]
- Rodriguez-Abetxuko, A.; Sánchez-Dealcázar, D.; Muñumer, P.; Beloqui, A. Tunable Polymeric Scaffolds for Enzyme Immobilization. Front. Bioeng. Biotechnol. 2020, 8, 830. [Google Scholar] [CrossRef]
- Kong, H.J. Designing alginate hydrogels to maintain viability of immobilized cells. Biomaterials 2003, 24, 4023–4029. [Google Scholar] [CrossRef]
- Singh, R.; Kennedy, J. Immobilization of yeast inulinase on chitosan beads for the hydrolysis of inulin in a batch system. Int. J. Biol. Macromol. 2017, 95, 87–93. [Google Scholar] [CrossRef] [PubMed]
- Lv, M.; Ma, X.; Anderson, D.P.; Chang, P.R. Immobilization of urease onto cellulose spheres for the selective removal of urea. Cellulose 2017, 25, 233–243. [Google Scholar] [CrossRef]
- Nawaz, M.A.; Karim, A.; Bibi, Z.; Rehman, H.U.; Aman, A.; Hussain, D.; Ullah, M.; Qader, S.A.U. Maltase entrapment approach as an efficient alternative to increase the stability and recycling efficiency of free enzyme within agarose matrix. J. Taiwan Inst. Chem. Eng. 2016, 64, 31–38. [Google Scholar] [CrossRef]
- Singh, V.; Singh, D. Glucose Oxidase Immobilization on Guar Gum–Gelatin Dual-Templated Silica Hybrid Xerogel. Ind. Eng. Chem. Res. 2014, 53, 3854–3860. [Google Scholar] [CrossRef]
- Prakash, O.; Jaiswal, N. Immobilization of a Thermostable α-Amylase on Agarose and Agar Matrices and its Application in Starch Stain Removal. World Appl. Sci. J. 2011, 13, 572–577. [Google Scholar]
- Kara, F.; Demirel, G.; Tümtürk, H. Immobilization of urease by using chitosan–alginate and poly(acrylamide-co-acrylic acid)/κ-carrageenan supports. Bioprocess Biosyst. Eng. 2006, 29, 207–211. [Google Scholar] [CrossRef] [PubMed]
- Bilal, M.; Asgher, M.; Iqbal, H.M.N.; Hu, H.; Zhang, X. Gelatin-Immobilized Manganese Peroxidase with Novel Catalytic Characteristics and Its Industrial Exploitation for Fruit Juice Clarification Purposes. Catal. Lett. 2016, 146, 2221–2228. [Google Scholar] [CrossRef]
- Rocha-Martin, J.; Acosta, A.; Berenguer, J.; Guisan, J.M.; Lopez-Gallego, F. Selective oxidation of glycerol to 1,3-dihydroxyacetone by covalently immobilized glycerol dehydrogenases with higher stability and lower product inhibition. Bioresour. Technol. 2014, 170, 445–453. [Google Scholar] [CrossRef] [PubMed]
- Yovcheva, T.; Vasileva, T.; Viraneva, A.; Cholev, D.; Bodurov, I.; Marudova, M.; Bivolarski, V.; Iliev, I. Effect of immobilization conditions on the properties of β-galactosidase immobilized in xanthan/chitosan multilayers. J. Phys. Conf. Ser. 2017, 794, 12032. [Google Scholar] [CrossRef]
- Costas, L.; Bosio, V.E.; Pandey, A.; Castro, G.R. Effects of Organic Solvents on Immobilized Lipase in Pectin Microspheres. Appl. Biochem. Biotechnol. 2008, 151, 578–586. [Google Scholar] [CrossRef]
- Gür, S.D.; Idil, N.; Aksöz, N. Optimization of Enzyme Co-Immobilization with Sodium Alginate and Glutaraldehyde-Activated Chitosan Beads. Appl. Biochem. Biotechnol. 2017, 184, 538–552. [Google Scholar] [CrossRef]
- Klein, W.P.; Thomsen, R.P.; Turner, K.B.; Walper, S.A.; Vranish, J.; Kjems, J.; Ancona, M.G.; Medintz, I.L. Enhanced Catalysis from Multienzyme Cascades Assembled on a DNA Origami Triangle. ACS Nano 2019, 13, 13677–13689. [Google Scholar] [CrossRef] [PubMed]
- Verma, M.L.; Kumar, S.; Das, A.; Randhawa, J.S.; Chamundeeswari, M. Chitin and chitosan-based support materials for enzyme immobilization and biotechnological applications. Environ. Chem. Lett. 2020, 18, 315–323. [Google Scholar] [CrossRef]
- Verma, M.L.; Kumar, S.; Das, A.; Randhawa, J.S.; Chamundeeswari, M. Enzyme Immobilization on Chitin and Chitosan-Based Supports for Biotechnological Applications. In Sustainable Agriculture Reviews 35, 1st ed.; Crini, G., Lichtfouse, E., Eds.; Springer: Cham, Switzerland, 2019; pp. 147–173. [Google Scholar] [CrossRef]
- Bösiger, P.; Tegl, G.; Richard, I.M.; Le Gat, L.; Huber, L.; Stagl, V.; Mensah, A.; Guebitz, G.M.; Rossi, R.M.; Fortunato, G. Enzyme functionalized electrospun chitosan mats for antimicrobial treatment. Carbohydr. Polym. 2018, 181, 551–559. [Google Scholar] [CrossRef] [PubMed]
- Girelli, A.M.; Astolfi, M.L.; Scuto, F.R. Agro-industrial wastes as potential carriers for enzyme immobilization: A review. Chemosphere 2020, 244, 125368. [Google Scholar] [CrossRef] [PubMed]
- Brígida, A.I.S.; Pinheiro, Á.D.T.; Ferreira, A.L.O.; Gonçalves, L.R.B. Immobilization of Candida antarctica Lipase B by Adsorption to Green Coconut Fiber. Appl. Biochem. Biotechnol. 2008, 146, 173–187. [Google Scholar] [CrossRef] [PubMed]
- Cristóvão, R.O.; Silvério, S.C.; Tavares, A.P.M.; Brígida, A.I.S.; Loureiro, J.M.; Boaventura, R.A.R.; Macedo, E.A.; Coelho, M.A.Z. Green coconut fiber: A novel carrier for the immobilization of commercial laccase by covalent attachment for textile dyes decolourization. World J. Microbiol. Biotechnol. 2012, 28, 2827–2838. [Google Scholar] [CrossRef] [PubMed]
- Borgio, J.F. Immobilization of Microbial (Wild and Mutant Strains) Amylase on Coconut Fiber and Alginate Matrix for Enhanced Activity. Am. J. Biochem. Mol. Biol. 2011, 1, 255–264. [Google Scholar] [CrossRef]
- Bonet-Ragel, K.; López-Pou, L.; Tutusaus, G.; Benaiges, M.D.; Valero, F. Rice husk ash as a potential carrier for the immobilization of lipases applied in the enzymatic production of biodiesel. Biocatal. Biotransform. 2018, 36, 151–158. [Google Scholar] [CrossRef]
- Kessi, E.; Arias, J.L. Using Natural Waste Material as a Matrix for the Immobilization of Enzymes: Chicken Eggshell Membrane Powder for β-Galactosidase Immobilization. Appl. Biochem. Biotechnol. 2018, 187, 101–115. [Google Scholar] [CrossRef]
- Bassan, J.C.; Bezerra, T.M.D.S.; Peixoto, G.; Da Cruz, C.Z.P.; Galán, J.P.M.; Vaz, A.B.D.S.; Garrido, S.S.; Filice, M.; Monti, R. Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein. Materials 2016, 9, 357. [Google Scholar] [CrossRef] [Green Version]
- Pandey, D.; Daverey, A.; Arunachalam, K. Biochar: Production, properties and emerging role as a support for enzyme immobilization. J. Clean. Prod. 2020, 255, 120267. [Google Scholar] [CrossRef]
- Ye, N.; Kou, X.; Shen, J.; Huang, S.; Chen, G.; Ouyang, G. Metal-Organic Frameworks: A New Platform for Enzyme Immobilization. ChemBioChem 2020, 21, 2585–2590. [Google Scholar] [CrossRef]
- Hu, C.; Bai, Y.; Hou, M.; Wang, Y.; Wang, L.; Cao, X.; Chan, C.-W.; Sun, H.; Li, W.; Ge, J.; et al. Defect-induced activity enhancement of enzyme-encapsulated metal-organic frameworks revealed in microfluidic gradient mixing synthesis. Sci. Adv. 2020, 6, eaax5785. [Google Scholar] [CrossRef] [Green Version]
- Cassimjee, K.E.; Kadow, M.; Wikmark, Y.; Humble, M.S.; Rothstein, M.L.; Rothstein, D.M.; Bäckvall, J.-E. A general protein purification and immobilization method on controlled porosity glass: Biocatalytic applications. Chem. Commun. 2014, 50, 9134–9137. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Engelmark Cassimjee, K.; Federsel, H.-J. EziG: A Universal Platform for Enzyme Immobilization. In Biocatalysis: An Industrial Perspective; de Gonzalo, G., de Maria, P.D., Eds.; RSC Catalysis Series No. 29; The Royal Society of Chemistry: London, UK, 2018; Chapter 13; pp. 345–362. [Google Scholar] [CrossRef]
- Cassimjee, K.E.; Hendil-Forssell, P.; Volkov, A.; Krog, A.; Malmo, J.; Aune, T.E.V.; Knecht, W.; Miskelly, I.R.; Moody, T.S.; Humble, M.S. Streamlined Preparation of Immobilized Candida antarctica Lipase B. ACS Omega 2017, 2, 8674–8677. [Google Scholar] [CrossRef] [PubMed]
- Bilal, M.; Zhao, Y.; Rasheed, T.; Iqbal, H.M. Magnetic nanoparticles as versatile carriers for enzymes immobilization: A review. Int. J. Biol. Macromol. 2018, 120, 2530–2544. [Google Scholar] [CrossRef]
- Cui, J.; Cui, L.; Jia, S.; Su, Z.; Zhang, S. Hybrid Cross-Linked Lipase Aggregates with Magnetic Nanoparticles: A Robust and Recyclable Biocatalysis for the Epoxidation of Oleic Acid. J. Agric. Food Chem. 2016, 64, 7179–7187. [Google Scholar] [CrossRef]
- Gao, J.; Yu, H.; Zhou, L.; He, Y.; Ma, L.; Jiang, Y. Formation of cross-linked nitrile hydratase aggregates in the pores of tannic-acid-templated magnetic mesoporous silica: Characterization and catalytic application. Biochem. Eng. J. 2017, 117, 92–101. [Google Scholar] [CrossRef]
- Tural, B.; Tarhan, T.; Tural, S. Covalent immobilization of benzoylformate decarboxylase from Pseudomonas putida on magnetic epoxy support and its carboligation reactivity. J. Mol. Catal. B Enzym. 2014, 102, 188–194. [Google Scholar] [CrossRef]
- Zlateski, V.; Fuhrer, R.; Koehler, F.M.; Wharry, S.; Zeltner, M.; Stark, W.J.; Moody, T.S.; Grass, R.N. Efficient Magnetic Recycling of Covalently Attached Enzymes on Carbon-Coated Metallic Nanomagnets. Bioconj. Chem. 2014, 25, 677–684. [Google Scholar] [CrossRef]
- Romero-Fernández, M.; Paradisi, F. Protein immobilization technology for flow biocatalysis. Curr. Opin. Chem. Biol. 2020, 55, 1–8. [Google Scholar] [CrossRef] [PubMed]
- Britton, J.; Majumdar, S.; Weiss, G.A. Continuous flow biocatalysis. Chem. Soc. Rev. 2018, 47, 5891–5918. [Google Scholar] [CrossRef]
- Thompson, M.P.; Peñafiel, I.; Cosgrove, S.C.; Turner, N.J. Biocatalysis Using Immobilized Enzymes in Continuous Flow for the Synthesis of Fine Chemicals. Org. Process Res. Dev. 2019, 23, 9–18. [Google Scholar] [CrossRef]
- Bolivar, J.M.; Mannsberger, A.; Thomsen, M.S.; Tekautz, G.; Nidetzky, B. Process intensification for O2-dependent enzymatic transformations in continuous single-phase pressurized flow. Biotechnol. Bioeng. 2019, 116, 503–514. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Bolivar, J.M.; Luley-Goedl, C.; Leitner, E.; Sawangwan, T.; Nidetzky, B. Production of glucosyl glycerol by immobilized sucrose phosphorylase: Options for enzyme fixation on a solid support and application in microscale flow format. J. Biotechnol. 2017, 257, 131–138. [Google Scholar] [CrossRef]
- Valikhani, D.; Bolivar, J.M.; Pfeiffer, M.; Nidetzky, B. Multivalency Effects on the Immobilization of Sucrose Phosphorylase in Flow Microchannels and Their Use in the Development of a High-Performance Biocatalytic Microreactor. ChemCatChem 2017, 9, 161–166. [Google Scholar] [CrossRef]
- Ye, J.; Chu, T.; Chu, J.; Gao, B.; He, B. A Versatile Approach for Enzyme Immobilization Using Chemically Modified 3D-Printed Scaffolds. ACS Sustain. Chem. Eng. 2019, 7, 18048–18054. [Google Scholar] [CrossRef]
- Mayer, S.F.; Kroutil, W.; Faber, K. Enzyme-Initiated Domino (Cascade) Reactions. Chem. Soc. Rev. 2001, 30, 332–339. [Google Scholar] [CrossRef]
- Schoffelen, S.; Van Hest, J.C.M. Multi-enzyme systems: Bringing enzymes together in vitro. Soft Matter 2011, 8, 1736–1746. [Google Scholar] [CrossRef]
- Ricca, E.; Brucher, B.; Schrittwieser, J.H. Multi-Enzymatic Cascade Reactions: Overview and Perspectives. Adv. Synth. Catal. 2011, 353, 2239–2262. [Google Scholar] [CrossRef]
- Monti, D.; Ferrandi, E.E.; Zanellato, I.; Hua, L.; Polentini, F.; Carrea, G.; Riva, S. One-Pot Multienzymatic Synthesis of 12-Ketoursodeoxycholic Acid: Subtle Cofactor Specificities Rule the Reaction Equilibria of Five Biocatalysts Working in a Row. Adv. Synth. Catal. 2009, 351, 1303–1311. [Google Scholar] [CrossRef]
- Lopez-Gallego, F.; Schmidt-Dannert, C. Multi-enzymatic synthesis. Curr. Opin. Chem. Biol. 2010, 14, 174–183. [Google Scholar] [CrossRef] [PubMed]
- Zhang, Y.; Hess, H. Toward Rational Design of High-efficiency Enzyme Cascades. ACS Catal. 2017, 7, 6018–6027. [Google Scholar] [CrossRef] [Green Version]
- Bruggink, A.; Schoevaart, R.; Kieboom, T. Concepts of Nature in Organic Synthesis: Cascade Catalysis and Multistep Conversions in Concert. Org. Process Res. Dev. 2003, 7, 622–640. [Google Scholar] [CrossRef]
- Ji, Q.; Wang, B.; Tan, J.; Zhu, L.; Li, L. Immobilized multienzymatic systems for catalysis of cascade reactions. Process Biochem. 2016, 51, 1193–1203. [Google Scholar] [CrossRef]
- Mateo, C.; Chmura, A.; Rustler, S.; Van Rantwijk, F.; Stolz, A.; Sheldon, R.A. Synthesis of enantiomerically pure (S)-mandelic acid using an oxynitrilase–nitrilase bienzymatic cascade: A nitrilase surprisingly shows nitrile hydratase activity. Tetrahedron Asymmetry 2006, 17, 320–323. [Google Scholar] [CrossRef]
- Zhang, Y.; Wang, Q.; Hess, H. Increasing Enzyme Cascade Throughput by pH-Engineering the Microenvironment of Individual Enzymes. ACS Catal. 2017, 7, 2047–2051. [Google Scholar] [CrossRef]
- Findrik, Z.; Vasić-Rački, Đ. Biotransformation of d-methionine into l-methionine in the cascade of four enzymes. Biotechnol. Bioeng. 2007, 98, 956–967. [Google Scholar] [CrossRef] [PubMed]
- Hwang, E.T.; Lee, S. Multienzymatic Cascade Reactions via Enzyme Complex by Immobilization. ACS Catal. 2019, 9, 4402–4425. [Google Scholar] [CrossRef]
- Velasco-Lozano, S.; Benítez-Mateos, A.I.; López-Gallego, F. Co-immobilized Phosphorylated Cofactors and Enzymes as Self-Sufficient Heterogeneous Biocatalysts for Chemical Processes. Angew. Chem. Int. Ed. 2017, 56, 771–775. [Google Scholar] [CrossRef] [PubMed]
- Wu, M.; He, Q.; Shao, Q.; Zuo, Y.; Wang, F.; Ni, H. Preparation and Characterization of Monodispersed Microfloccules of TiO2 Nanoparticles with Immobilized Multienzymes. ACS Appl. Mater. Interfaces 2011, 3, 3300–3307. [Google Scholar] [CrossRef]
- Cao, L.; Van Rantwijk, F.; Sheldon, R.A. Cross-Linked Enzyme Aggregates: A Simple and Effective Method for the Immobilization of Penicillin Acylase. Org. Lett. 2000, 2, 1361–1364. [Google Scholar] [CrossRef]
- Sheldon, R.A. Cross-linked enzyme aggregates (CLEA®s): Stable and recyclable biocatalysts. Biochem. Soc. Trans. 2007, 35, 1583–1587. [Google Scholar] [CrossRef] [Green Version]
- Sheldon, R.A. Cross-Linked Enzyme Aggregates as Industrial Biocatalysts. Org. Process Res. Dev. 2011, 15, 213–223. [Google Scholar] [CrossRef]
- Sheldon, R.A. Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs). Appl. Microbiol. Biotechnol. 2011, 92, 467–477. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Yamaguchi, H.; Kiyota, Y.; Miyazaki, M. Techniques for Preparation of Cross-Linked Enzyme Aggregates and Their Applications in Bioconversions. Catalysts 2018, 8, 174. [Google Scholar] [CrossRef] [Green Version]
- Mateo, C.; Van Langen, L.M.; Van Rantwijk, F.; Sheldon, R.A. A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates. Biotechnol. Bioeng. 2004, 86, 273–276. [Google Scholar] [CrossRef] [PubMed]
- Vaidya, B.K.; Kuwar, S.S.; Golegaonkar, S.B.; Nene, S.N. Preparation of cross-linked enzyme aggregates of l-aminoacylase via co-aggregation with polyethyleneimine. J. Mol. Catal. B Enzym. 2012, 74, 184–191. [Google Scholar] [CrossRef]
- Perez, D.I.; Van Rantwijk, F.; Sheldon, R.A. Cross-Linked Enzyme Aggregates of Chloroperoxidase: Synthesis, Optimization and Characterization. Adv. Synth. Catal. 2009, 351, 2133–2139. [Google Scholar] [CrossRef]
- Sheldon, R.A. Industrial Applications of Asymmetric Synthesis using Cross-Linked Enzyme Aggregates. In Comprehensive Chirality, 1st ed.; Carreira, E.M., Yamamoto, H., Eds.; Elsevier: Amsterdam, The Netherlands, 2012; Volume 9, pp. 353–366. [Google Scholar]
- Mahmod, S.S.; Yusof, F.; Jami, M.S.; Khanahmadi, S. Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease. Bioresour. Bioprocess. 2016, 3, 3. [Google Scholar] [CrossRef] [Green Version]
- Sheldon, R.A. CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy. Catalysts 2019, 9, 261. [Google Scholar] [CrossRef] [Green Version]
- Ahumada, K.; Martínez-Gil, A.; Moreno-Simunovic, Y.; Illanes, A.; Wilson, L. Aroma Release in Wine Using Co-Immobilized Enzyme Aggregates. Molecules 2016, 21, 1485. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Bernal, C.; Rodríguez, K.; Martínez, R. Integrating enzyme immobilization and protein engineering: An alternative path for the development of novel and improved industrial biocatalysts. Biotechnol. Adv. 2018, 36, 1470–1480. [Google Scholar] [CrossRef] [PubMed]
- Singh, R.K.; Tiwari, M.K.; Singh, R.; Lee, J.-K. From Protein Engineering to Immobilization: Promising Strategies for the Upgrade of Industrial Enzymes. Int. J. Mol. Sci. 2013, 14, 1232–1277. [Google Scholar] [CrossRef] [PubMed]
- Redeker, E.S.; Ta, D.T.; Cortens, D.; Billen, B.; Guedens, W.; Adriaensens, P. Protein Engineering For Directed Immobilization. Bioconj. Chem. 2013, 24, 1761–1777. [Google Scholar] [CrossRef]
- Bilal, M.; Iqbal, H.M.; Guo, S.; Hu, H.; Wang, W.; Zhang, X. State-of-the-art protein engineering approaches using biological macromolecules: A review from immobilization to implementation view point. Int. J. Biol. Macromol. 2018, 108, 893–901. [Google Scholar] [CrossRef]
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Federsel, H.-J.; Moody, T.S.; Taylor, S.J.C. Recent Trends in Enzyme Immobilization—Concepts for Expanding the Biocatalysis Toolbox. Molecules 2021, 26, 2822. https://doi.org/10.3390/molecules26092822
Federsel H-J, Moody TS, Taylor SJC. Recent Trends in Enzyme Immobilization—Concepts for Expanding the Biocatalysis Toolbox. Molecules. 2021; 26(9):2822. https://doi.org/10.3390/molecules26092822
Chicago/Turabian StyleFedersel, Hans-Jürgen, Thomas S. Moody, and Steve J.C. Taylor. 2021. "Recent Trends in Enzyme Immobilization—Concepts for Expanding the Biocatalysis Toolbox" Molecules 26, no. 9: 2822. https://doi.org/10.3390/molecules26092822