High performing immobilized Baeyer-Villiger monooxygenase and glucose dehydrogenase for the synthesis of ε-caprolactone derivative

Delgove, Marie A. F.; Valencia, Daniela; Solé, Jordi; Bernaerts, Katrien V.; Wildeman, Stefaan M. A. De; Guillén, Marina; Álvaro, Gregorio

doi:10.1016/j.apcata.2018.12.036

Cited by 23 publications

(41 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A reusability of ten times with 2 % of loss of biocatalytic activity per reuse was assumed. This is a realistic estimation of the performance of this particular enzyme, based on direct experimental studies on its stability and reusability if immobilized . To model the reuse of the enzyme, the enzyme preparation procedure and the product isolation step must be adapted appropriately because the standard procedure includes the deactivation of all remaining enzyme by addition of methanol.…”

Section: Resultsmentioning

confidence: 99%

“…[42] Ar eusability of ten times with 2% of loss of biocatalytic activity per reuse was assumed.T his is ar ealistic estimation of the performance of this particulare nzyme, based on direct experimental studies on its stabilitya nd reusability if immobilized. [43] To model the reuse of the enzyme, the enzyme preparation procedure and the product isolation step must be adapted appropriately because the standard procedure includes the deactivation of all remaining enzyme by addition of methanol. The enzyme can potentially be recycled if used in the form of whole-cells,w hicha re separated from the reaction mixture by ultrafiltration, after which the product can be directly extracted from the reaction mixture.T he electricity consumption for ultrafiltration was calculated based on data from the literature.…”

Section: Effect Of Enzyme Recyclingmentioning

confidence: 99%

See 1 more Smart Citation

A Prospective Life Cycle Assessment (LCA) of Monomer Synthesis: Comparison of Biocatalytic and Oxidative Chemistry

et al. 2019

Self Cite

View full text Add to dashboard Cite

Biotechnological processes are typically perceived to be greener than chemical processes. A life cycle assessment (LCA) was performed to compare the chemical and biochemical synthesis of lactones obtained by Baeyer–Villiger oxidation. The LCA is prospective (based on experiments at a small scale with primary data) because the process is at an early stage. The results show that the synthesis route has no significant effect on the climate change impact [(1.65±0.59) kgCO2 gproduct−1 vs. (1.64±0.67) kgCO2 gproduct−1]. Key process performance metrics affecting the environmental impact were evaluated by performing a sensitivity analysis. Recycling of solvents and enzyme were shown to provide an advantage to the enzymatic synthesis. Additionally, the climate change impact was decreased by 71 % if renewable electricity was used. The study shows that comparative LCAs can be used to usefully support decisions at an early stage of process development.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Effect Of Enzyme Recyclingmentioning

confidence: 99%

A Prospective Life Cycle Assessment (LCA) of Monomer Synthesis: Comparison of Biocatalytic and Oxidative Chemistry

et al. 2019

Self Cite

View full text Add to dashboard Cite

show abstract

“…However, in order to ideally study an immobilized biocatalyst in an industrial target reaction, the support should contain the highest number of units of activity possible. [21] To do so, the two best performing carriers, according to the IY and RA obtained during characterization, were chosen: Epoxy-agarose M1 and Epoxy-agarose M2 (pH 9).…”

Section: Immobilization Of Adhaa On Epoxy-agarose M1 and M2 Applying mentioning

confidence: 99%

“…[21][22][23] Numerous are the examples in literature about immobilized alcohol dehydrogenases, [24][25][26][27] however, this is the first time that immobilization has been studied on Artemisia annua's ADH. Furthermore, immobilization of ADHaa on different supports was investigated in order to re-use the enzyme in various cycles of reaction.…”

Section: Introductionmentioning

confidence: 99%

“…In this sense, immobilization often results in an increased stability of the catalyst and allows an ease separation of the enzymes from the reactor content. [21][22][23] Numerous are the examples in literature about immobilized alcohol dehydrogenases, [24][25][26][27] however, this is the first time that immobilization has been studied on Artemisia annua's ADH.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Ketoisophorone Synthesis with an Immobilized Alcohol Dehydrogenase

Solé

Brummund²,

Caminal

et al. 2019

ChemCatChem

Self Cite

View full text Add to dashboard Cite

The monoterpenoid α-isophorone is sourced from the available and renewable plant dry matter, as well as a waste recovery operation from acetone. This compound, can be hydroxylated to 4-hydroxy-isophorone which is the main precursor for the synthesis of ketoisophorone. On its turn, ketoisophorone is a key intermediate for the production of carotenoids and Vitamin E. Here, the enzymatic oxidation of 4-hydroxy-isophorone to ketoisophorone is demonstrated employing an alcohol dehydrogenase (ADHaa) from Artemisia annua and a NADPH oxidase (NOX), as a cofactor regeneration enzyme. After 24 h of reaction and an initial substrate concentration of 50 mM, 95.7 % yield and a space time yield of 6.52 g L À 1 day À 1 could be obtained. Furthermore, the immobilization of the alcohol dehydrogenase was studied on 17 different supports. An epoxy-functionalized agarose resulted in the highest metrics, 100 � 0% immobilization yield and 58.2 � 3.5 % retained activity. Finally, the immobilized ADHaa was successfully implemented in 4 reaction cycles (96 h operation) presenting a biocatalyst yield of 23.4 g product g À 1 of enzyme. It represents a 2.5-fold increase compared with the reaction with soluble enzymes.

show abstract

Crosslinked Aggregates of Fusion Enzymes in Microaqueous Organic Media

2023

View full text Add to dashboard Cite

Baeyer-Villiger monooxygenases (BVMOs) are attractive for selectively oxidizing various ketones using oxygen into valuable esters and lactones. However, the application of BVMOs is restrained by cofactor dependency and enzyme instability combined with water-related downsides such as low substrate loading, low oxygen capacity, and water-induced side reactions. Herein, we described a redox-neutral linear cascade with in-situ cofactor regeneration catalyzed by fused alcohol dehydrogenase and cyclohexanone monooxygenase in aqueous and microaqueous organic media. The cascade conditions have been optimized regarding substrate concentrations as well as the amounts of enzymes and cofactors with the Design of Experiments (DoE). The carrier-free immobilization technique, crosslinked enzyme aggregates (CLEAs), was applied to fusion enzymes. The resultant fusion CLEAs were proven to function in microaqueous organic systems, in which the enzyme ratios, water contents (0.5-5 vol. %), and stability have been systematically studied. The fusion CLEAs showed promising operational (up to 5 cycles) and storage stability.

show abstract

High performing immobilized Baeyer-Villiger monooxygenase and glucose dehydrogenase for the synthesis of ε-caprolactone derivative

Cited by 23 publications

References 35 publications

A Prospective Life Cycle Assessment (LCA) of Monomer Synthesis: Comparison of Biocatalytic and Oxidative Chemistry

A Prospective Life Cycle Assessment (LCA) of Monomer Synthesis: Comparison of Biocatalytic and Oxidative Chemistry

Ketoisophorone Synthesis with an Immobilized Alcohol Dehydrogenase

Crosslinked Aggregates of Fusion Enzymes in Microaqueous Organic Media

Contact Info

Product

Resources

About