Integrating enzyme immobilization and protein engineering: An alternative path for the development of novel and improved industrial biocatalysts

Bernal, Claudia; Rodríguez, Karen Villalba; Martínez, Ronny

doi:10.1016/j.biotechadv.2018.06.002

Cited by 277 publications

(136 citation statements)

References 155 publications

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“…Enzyme immobilization in packed‐bed reactors is often required, to enable a piston flow pattern while conferring stability to the biocatalyst. Immobilization strategies can be based on covalent bonding, adsorption, entrapment, or cross‐linking, leading to derivatives that are more resistant to deactivation mechanisms, such as aggregation, denaturation, conformational changes, or even dissociation into subunits (e. g. when multimeric enzymes are used). In the case of multimeric enzymes, some experimental conditions can weaken the subunit‐subunit interactions.…”

Section: Motivation Synergies Among Biocatalysis Environmentally‐frmentioning

confidence: 99%

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Guajardo

Marı́a²

2019

ChemCatChem

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Enzyme catalysis (biocatalysis) is a mature strategy to perform organic synthesis with high selectivity and under mild reaction conditions. However, despite their origin and biodegradability, the simple use of enzymes is not sufficient to validate a process as green or sustainable. To reinforce the value that biocatalysis may offer, enzymatic processes can be established in environmentally‐friendly media, such as water, neoteric solvents (e. g. deep‐eutectic‐solvents, DES), biogenic solvents (e. g. 2‐MeTHF or terpenes), or even solvent‐free systems (if substrates allow that). Furthermore, these options can be conducted in continuous biocatalytic processes, which are more efficient and sustainable. Hence, a triple synergy is generated, and very promising environmentally‐friendly options can be envisaged. This conceptual paper discusses these alternatives, providing relevant, recently reported, successful examples.

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Section: Motivation Synergies Among Biocatalysis Environmentally‐frmentioning

confidence: 99%

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Guajardo

Marı́a²

2019

ChemCatChem

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“…However, the use of free enzymes for industrial applications is often hampered by their limited operational stability as well as by difficulties with their recovery and recycling. Immobilization of soluble enzymes on solid supports is an effective strategy to overcome these limitations as it provides a number of benefits including enhanced enzyme stability, easy separation and recovery, and continuous use . Considerable efforts have been invested in the development of scaffolds with controllable pore structures and surface properties in order to produce immobilized enzymes with enhanced stability while maintaining activity and selectivity …”

Section: Introductionmentioning

confidence: 99%

Hierarchical Micro‐ and Mesoporous Zn‐Based Metal–Organic Frameworks Templated by Hydrogels: Their Use for Enzyme Immobilization and Catalysis of Knoevenagel Reaction

Cheng

Švec

et al. 2019

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Encapsulation of enzymes in metal–organic frameworks (MOFs) is often obstructed by the small size of the orifices typical of most reported MOFs, which prevent the passage of larger‐size enzymes. Here, the preparation of hierarchical micro‐ and mesoporous Zn‐based MOFs via the templated emulsification method using hydrogels as a template is presented. Zinc‐based hydrogels featuring a 3D interconnecting network are first produced via the formation of hydrogen bonds between melamine and salicylic acid in which zinc ions are well distributed. Further coordination with organic linkers followed by the removal of the hydrogel template produces hierarchical Zn‐based MOFs containing both micropores and mesopores. These new MOFs are used for the encapsulation of glucose oxidase and horseradish peroxidase to prove the concept. The immobilized enzymes exhibit a remarkably enhanced increased operational stability and enzymatic activity with a kcat/km value of 85.68 mm s–1. This value is 7.7‐fold higher compared to that found for the free enzymes in solution, and 2.7‐fold higher than enzymes adsorbed on conventional microporous MOFs. The much higher catalytic activity of the mesoporous conjugate for Knoevenagel reactions is demonstrated, since the large pores enable easier access to the active sites, and compared with that observed for catalysis using microporous MOFs.

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“…For example, cross‐linked enzyme aggregates (CLEAs) are prepared by simply precipitating the enzyme from an aqueous solution, including crude cell lysate, by standard procedures followed by cross‐linking with a bifunctional reagent such as glutaraldehyde. Another trend is to improve enzyme immobilization through protein engineering …”

Section: Expanding the Scope And Potential Of Biocatalysismentioning

confidence: 99%

“…Another trend is to improve enzyme immobilization throughp rotein engineering. [70] Multiple enzymes can be combined to form biocatalystsc apable of multistep "cascade" reactions. For example, ac ombi-CLEA of aK RED and GDHwas used repeatedly in the reduction of the keto ester in the synthesis of the key atorvastatin intermediate (see earlier).…”

Section: Betterformulation and Recycling Of Enzymes Through Immobilizmentioning

confidence: 99%

Broadening the Scope of Biocatalysis in Sustainable Organic Synthesis

2019

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This Review is aimed at synthetic organic chemists who may be familiar with organometallic catalysis but have no experience with biocatalysis, and seeks to provide an answer to the perennial question: if it is so attractive, why wasn't it extensively used in the past? The development of biocatalysis in industrial organic synthesis is traced from the middle of the last century. Advances in molecular biology in the last two decades, in particular genome sequencing, gene synthesis and directed evolution of proteins, have enabled remarkable improvements in scope and substantially reduced biocatalyst development times and cost contributions. Additionally, improvements in biocatalyst recovery and reuse have been facilitated by developments in enzyme immobilization technologies. Biocatalysis has become eminently competitive with chemocatalysis and the biocatalytic production of important pharmaceutical intermediates, such as enantiopure alcohols and amines, has become mainstream organic synthesis. The synthetic space of biocatalysis has significantly expanded and is currently being extended even further to include new‐to‐nature biocatalytic reactions.

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Integrating enzyme immobilization and protein engineering: An alternative path for the development of novel and improved industrial biocatalysts

Cited by 277 publications

References 155 publications

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Hierarchical Micro‐ and Mesoporous Zn‐Based Metal–Organic Frameworks Templated by Hydrogels: Their Use for Enzyme Immobilization and Catalysis of Knoevenagel Reaction

Broadening the Scope of Biocatalysis in Sustainable Organic Synthesis

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