Pushing the limits: Cyclodextrin-based intensification of bioreductions

Rapp, Christian; Nidetzky, Bernd; Kratzer, Regina

doi:10.1016/j.jbiotec.2020.11.017

Cited by 7 publications

(18 citation statements)

References 39 publications

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“…The catalytic e ciency increased 215-fold for racemic 2-phenylpropanal and 270-fold for the (S)-aldehyde compared to the wild-type. Likewise, the catalytic e ciency for reduction of o-chloroacetophenone was improved 13-times by the D51A mutation (14) whereas a 50-fold decrease was observed for the conversion of xylose (19). Our results stressed the notion made by Kavanagh et al (18) that Asp-51 in CtXR contributes the most to the relative polarity of the binding site and hence speci city for sugar substrates.…”

Section: Literature Surveysupporting

confidence: 80%

“…Cyclodextrin addition. The addition of 75 mM 2-hydroxypropyl-β-cyclodextrin has previously shown to boost bioreductions based on the used catalyst (14). Here, the addition of 38, 75 or 115 mM 2-hydroxypropyl-β-cyclodextrin had no signi cant effect on bioreductions of 1 and 2 M 2-phenylpropanal (Table 3).…”

Section: Optimization Of 2-phenylpropanal Bioreductionmentioning

confidence: 73%

“…Its biocatalytic applicability was, however, limited by moderate catalytic activity and low stability of the wild-type enzyme. Several substrate-binding site mutants with improved speci city for aromatic ketones were used in the synthesis of (R)-ethyl mandelates and (S)phenylethanols (13,14).…”

Section: Resultsmentioning

confidence: 99%

“…The replacement of Trp-24 by smaller phenylalanine and tyrosine increased activities on bulky ketone-substrates (13,19). Asp-51 contributes the most to the relative polarity of the binding site; substitution by alanine led to improved selectivity for the aromatic ketone o-chloroacetophenone (14).…”

Section: Ct Xr Mutantsmentioning

confidence: 99%

“…An E. coli Rosetta2 strain co-expressing CtXR D51A and CbFDH (GenBank ID AJ011046) was used. Whole-cell biocatalyst production was previously described by Rapp et al (14). The biomass was frozen at -20°C, lyophilized (Christ α 1-4 lyophilizer from Braun Biotech International) and stored at -20°C.…”

Section: Whole-cell Biocatalystmentioning

confidence: 99%

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Enzymatic Dynamic Reductive Kinetic Resolution Towards 115 g/L (S)-2-Phenylpropanol

Rapp

Pival-Marko

Tassano

et al. 2021

Preprint

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BackgroundPublished biocatalytic routes towards chiral 2-phenylpropanol by oxidoreductases showed product concentrations of maximally 80 mM. Enzyme deactivation turned out as one major limitation and was attributed to adduct formation of the aldehyde substrate with the catalytic reductase.ResultsA Candida tenuis xylose reductase single-point mutant (CtXR D51A) with very high catalytic efficiency (43·103 s-1M-1) for (S)-2-phenylpropanal was identified. The enzyme showed high enantioselectivity for the (S)-enantiomer but was deactivated by 0.5 mM substrate within 2 h. A whole-cell biocatalyst based on the engineered reductase and a yeast formate dehydrogenase for NADH-recycling provided substantial stabilization of the reductase. The relatively slow in situ racemization of 2-phenylpropanal and the still limited biocatalyst stability required a subtle adjustment of the substrate-to-catalyst ratio. A value of 3.4 gsubstrate/gcell-dry-weight turned out as compromise between product enantiopurity and conversion. A catalyst loading of 40 gcell-dry-weight was used to convert 1 M racemic 2-phenylpropanal to (S)-phenylpropanol in 93.1 % e.e. ConclusionMainly hydrolases have been exploited for the production of profenols at industrial scale so far. The herein established bioreduction presents an alternative route towards profenols that is competitive to hydrolase-catalyzed kinetic resolutions.

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Section: Literature Surveysupporting

confidence: 80%

Section: Optimization Of 2-phenylpropanal Bioreductionmentioning

confidence: 73%

Section: Resultsmentioning

confidence: 99%

Section: Ct Xr Mutantsmentioning

confidence: 99%

Section: Whole-cell Biocatalystmentioning

confidence: 99%

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Enzymatic Dynamic Reductive Kinetic Resolution Towards 115 g/L (S)-2-Phenylpropanol

Rapp

Pival-Marko

Tassano

et al. 2021

Preprint

Self Cite

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Selective Immobilization of His‐Tagged Phosphomannose Isomerase on Ni Chelated Nanoparticles with Good Reusability and Activity

et al. 2022

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Self‐stable precipitation polymerization was used to prepare an enzyme‐immobilized microsphere composite. Phosphomannose isomerase (PMI) with His‐tag was successfully immobilized on Ni2+ charged pyridine‐derived particles. The maximum amount of PMI immobilized on such particles was ∼184 mg/g. Compared with free enzyme, the activity of the immobilized enzymes was significantly improved. In addition, the immobilized enzymes showed a much better thermostability than free enzymes. At the same time, the immobilized enzymes can be reused for multiple reaction cycles. We observed that the enzyme activity did not decrease significantly after six cycles. We conclude that the pyridine‐derived particles can be used to selectively immobilize His‐tagged enzymes, which can couple the enzyme purification and catalysis steps and improve the efficiency of enzyme‐catalyzed industrial processes.

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Efficient Synthesis of Chiral Aryl Alcohol with a Novel Kosakonia radicincitans Isolate in Tween 20/L-carnitine: Lysine-Containing Synergistic Reaction System

Kong

Gui

Liu

et al. 2023

Appl Biochem Biotechnol

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Pushing the limits: Cyclodextrin-based intensification of bioreductions

Cited by 7 publications

References 39 publications

Enzymatic Dynamic Reductive Kinetic Resolution Towards 115 g/L (S)-2-Phenylpropanol

Enzymatic Dynamic Reductive Kinetic Resolution Towards 115 g/L (S)-2-Phenylpropanol

Selective Immobilization of His‐Tagged Phosphomannose Isomerase on Ni Chelated Nanoparticles with Good Reusability and Activity

Efficient Synthesis of Chiral Aryl Alcohol with a Novel Kosakonia radicincitans Isolate in Tween 20/L-carnitine: Lysine-Containing Synergistic Reaction System

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