Enzymatic processes in alternative reaction media: a mini review

Ghaffari‐Moghaddam, Mansour; Eslahi, Hassan; Aydin, Yasar Andelib; Saloglu, Didem

doi:10.14440/jbm.2015.60

Cited by 38 publications

(19 citation statements)

References 91 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Enzymatic reactions intrinsically offer several advantages, making them ideal alternatives to classical synthesis strategies: Enzymes typically exhibit high substrate specificities, both regio‐ and stereoselectivities, circumventing the problem of expensive and time‐consuming isolation of by‐products and intermediates . Enzymatic reactions typically take place under environmentally benign reaction conditions; toxic auxiliaries can (mostly) be prevented . Furthermore, enzymes are intrinsically biodegradable, thus increasing the eco‐efficiency of enzymatic reactions…”

Section: Introductionmentioning

confidence: 99%

Stimulus‐Responsive Regulation of Enzyme Activity for One‐Step and Multi‐Step Syntheses

2019

View full text Add to dashboard Cite

Multi‐step biocatalytic reactions have gained increasing importance in recent years because the combination of different enzymes enables the synthesis of a broad variety of industrially relevant products. However, the more enzymes combined, the more crucial it is to avoid cross‐reactivity in these cascade reactions and thus achieve high product yields and high purities. The selective control of enzyme activity, i.e., remote on‐/off‐switching of enzymes, might be a suitable tool to avoid the formation of unwanted by‐products in multi‐enzyme reactions. This review compiles a range of methods that are known to modulate enzyme activity in a stimulus‐responsive manner. It focuses predominantly on in vitro systems and is subdivided into reversible and irreversible enzyme activity control. Furthermore, a discussion section provides indications as to which factors should be considered when designing and choosing activity control systems for biocatalysis. Finally, an outlook is given regarding the future prospects of the field.

show abstract

Section: Introductionmentioning

confidence: 99%

Stimulus‐Responsive Regulation of Enzyme Activity for One‐Step and Multi‐Step Syntheses

2019

View full text Add to dashboard Cite

show abstract

“…The product amine was therefore extracted into the aqueous phase to investigate the potential of downstream processing and in situ product recovery approaches. Furthermore, as often seen in lipase‐catalyzed processes, and more recently in the cutinase‐catalyzed synthesis of aliphatic polyesters and in the cellulase‐catalyzed hydrolysis of cellulose into glucose, enzymatic reactions can be run in the presence of only the reactants and biocatalyst, without bulk solvents or other aqueous components, thus resulting in solvent‐free systems (SFSs). This approach minimizes the required volume of the reactor, simplifies the downstream processing and reduces the associated costs.…”

Section: Introductionmentioning

confidence: 99%

Jeffamine® ED‐600: a polyether amine donor for enzymatic transamination in organic solvent/solvent‐free medium with membrane‐assisted product extraction

Matassa

Romani

Ormerod

et al. 2019

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND: Amine transaminases have been extensively used for synthesizing various pharmaceutically relevant compounds, mainly in aqueous media. However, their applications are often limited by poor substrate solubility, low productivity and difficult product separation. This paper reports the use of Jeffamine ® ED-600, a novel polyether amine donor, for the transaminase-catalyzed synthesis of 4-phenyl-2-butylamine in non-aqueous media.RESULTS: Enzymatic transamination was performed in the presence of a non-polar organic solvent (n-heptane), in which the selected amine donor is not soluble, thus a two-liquid-phase system was achieved. Coupling the reaction system with membrane-assisted extraction resulted in simultaneous recovery of product, without any consistent contamination of the unreacted substrates. Moreover, a product yield of 60% was reached, compared with 15% without product extraction. The reaction was also successfully conducted without addition of any organic solvent, thus providing the first example of a solvent-free transamination system. In the presence of only enzyme and substrates, up to 6-fold higher product concentrations were achieved compared with the reaction performed in organic solvent. CONCLUSION: The use of the Jeffamine ® ED-600 in non-aqueous media resulted beneficial for 4-phenyl-2-butylamine synthesis. Enzymatic transamination in organic solvent with membrane-assisted product extraction enabled shifting of the equilibrium and selective product extraction. Solvent-free transamination minimized the required volume of the reactor and minimized the environmental impact. Extension to other substrate/enzyme solvent-free systems could open new possibilities and perspectives in transaminase-catalyzed chiral amine synthesis. Two-liquid-phase transaminationTransamination was performed in 10 mL glass vials (diameter 2.5 cm), in which a biphasic system was built (Fig. 1, left side). According to our previous studies, 16 0.05 g of TA-v2 enzyme was wetted with 100 μL of 0.5 mmol L −1 PLP/water mixture. The amine donor (AD) Jeffamine ED-600 was then added to the vials (either J Chem Technol Biotechnol 2020; 95: 604-613

show abstract

“…In recent decades, enzymes have been regarded as green catalysts because they are recyclable non-toxic materials and the enzymatic reactions are usually performed under mild conditions [ 1 , 2 ]. Lipases are the most used enzymes because of their high stability, activity, wide range of substrates, and low cost [ 3 , 4 , 5 , 6 ].…”

Section: Introductionmentioning

confidence: 99%

Ionic Liquids: Efficient Media for the Lipase-Catalyzed Michael Addition

et al. 2018

View full text Add to dashboard Cite

Recently, ionic liquids (ILs) have been regarded as ideal media for non-aqueous bio-catalysis. In this work, the synthesis of warfarin by the lipase-catalyzed Michael addition in IL media and the parameters that affected the warfarin yield were investigated. Experimental results demonstrated that the chemical structures of the ILs were a major factor for influencing the warfarin yield. The ILs containing the NTf2– anion were suitable reaction media due to the high chemical stability of this anion. The incorporation of the hydroxyl group on the IL cation significantly improved the lipase activity due to the H2O-mimicking property of this group. The lipase activity decreased by increasing the alkyl chain length on the IL cation due to the non-polar domain formation of the IL cation at the active site entrance of lipase. The ILs and lipase could be reused no less than five times without reduction in the warfarin yield.

show abstract

Enzymatic processes in alternative reaction media: a mini review

Cited by 38 publications

References 91 publications

Stimulus‐Responsive Regulation of Enzyme Activity for One‐Step and Multi‐Step Syntheses

Stimulus‐Responsive Regulation of Enzyme Activity for One‐Step and Multi‐Step Syntheses

Jeffamine® ED‐600: a polyether amine donor for enzymatic transamination in organic solvent/solvent‐free medium with membrane‐assisted product extraction

Ionic Liquids: Efficient Media for the Lipase-Catalyzed Michael Addition

Contact Info

Product

Resources

About