Asymmetric Biocatalytic Cannizzaro‐Type Reaction

Wuensch, Christiane; Lechner, Horst; Glueck, Silvia M.; Zangger, Klaus; Hall, Mélanie; Faber, Kurt

doi:10.1002/cctc.201300028

Cited by 26 publications

(10 citation statements)

References 46 publications

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“…reported Novozyme 435 catalyzed Canizzaro reaction of substituted benzaldehydes ( Scheme ) . The reaction occurred in an aqueous medium at 30 o C and had no requirement for an external redox reagent like the single‐enzyme Canizzaro reaction with an aldehyde dehydrogenase In a self‐Canizzaro reaction, it is anticipated that an equal amount of alcohol and acid would be formed as a result of the disproportionation of the aldehyde. However, the team reported a rapid conversion of p ‐nitrobenzaldehyde to the alcohol precisely in 6 h using lipase.…”

Section: Introductionmentioning

confidence: 99%

Promiscuity of Lipase‐Catalyzed Reactions for Organic Synthesis: A Recent Update

et al. 2018

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Lipase-catalyzed organic reactions have widely been practiced in the past three decades. In addition to its wide acceptance in conventional reactions such as hydrolysis, transesterification, and enantiopure synthesis (kinetic resolution and dynamic kinetic resolution) several reports on the catalytic promiscuity of lipases have also been published. The concept of promiscuity, where lipase catalyzes reactions beyond its natural function, has been perceived as a useful phenomenon which can enhance the utility of lipase as a biocatalyst. Many useful organic reactions such as Aldol condensation, Hantzsch reaction, Canizzaro reaction, Mannich reaction, Baylis-Hillman reaction, Knoevenagel condensation, Michael addition, Ugi reaction, and oxidation catalyzed by lipases have surfaced in the literature. The current review is a critical compilation of such research findings to put forth the synthetic applications of lipase, beyond the orthodox biocatalytic toolbox.

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Section: Introductionmentioning

confidence: 99%

Promiscuity of Lipase‐Catalyzed Reactions for Organic Synthesis: A Recent Update

et al. 2018

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“…Oxidation of the aldehyde occur via a gem ‐diol formed in aqueous environments. Wuensch and co‐workers have however demonstrated that when using catalytic amounts of cofactors, different ADHs can give significantly different ratios of alcohol and acids during time‐course reactions . As our reactions contained excess amounts of Sm NOX to ensure cofactor regeneration was not limiting the reactions, only NAD(P) + is available thus permitting only the gem ‐diol (aldehyde) oxidation reaction.…”

Section: Resultsmentioning

confidence: 99%

An Alcohol Dehydrogenase from the Short‐Chain Dehydrogenase/Reductase Family of Enzymes for the Lactonization of Hexane‐1,6‐diol

et al. 2018

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Biocatalytic production of lactones, and in particular ϵ‐caprolactone (CL), have gained increasing interest as a greener route to polymer building blocks, especially through the use of Baeyer–Villiger monooxygenases (BVMOs). Despite several advances in the field, BVMOs, however, still suffer several practical limitations. Alcohol dehydrogenase (ADH)‐mediated lactonization of diols in turn has received far less attention and very few enzymes have been identified for the conversion of diols to lactones, with horse‐liver ADH (HLADH) remaining the catalyst of choice. Screening of a diverse panel of ADHs, AaSDR‐1, a member of the short‐chain dehydrogenase/reductase family, was found to produce ϵ‐caprolactone from hexane‐1,6‐diol. Moreover, cofactor regeneration by an NADH oxidase eliminated the requirement of co‐substrates, yielding water as the sole by‐product. Despite lower turnover frequencies as compared to HLADH, higher selectivity was found for the production of CL, with HLADH forming significant amounts of 6‐hydroxyhexanoic acid and adipic acid through aldehyde dehydrogenation/oxidation of the gem‐diol intermediates. Also, CL yield were shown to be dependent on buffer choice, as structural elucidation of a Tris adduct confirmed the buffer amine to react with aliphatic aldehydes forming a Schiff‐base intermediate which through further ADH oxidation, forms a tricyclic acetal product.

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“…The thermostable ADH‐ht from Bacillus stearothermophilus , an ADH with known oxidation activity towards primary alcohols, exclusively accepted the carboxybenzyl (Cbz)‐protected amino alcohol ( 4 a ) and gave 27 % of the desired aldehyde within 2 h reaction time. Furthermore, ADH‐a from R. ruber , which was predominantly reported for the oxidation of secondary alcohols with few exceptions, such as 2‐phenylethanol ( 1 a ), showed no activity towards our model substrates . More promising results were obtained by applying AlkJ, an ADH from Pseudomonas putida , which was known for the oxidation of aliphatic alcohols.…”

Section: Resultsmentioning

confidence: 99%

Cell Factory Design and Optimization for the Stereoselective Synthesis of Polyhydroxylated Compounds

et al. 2017

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A synthetic cascade for the transformation of primary alcohols into polyhydroxylated compounds in Escherichia coli, through the in situ preparation of cytotoxic aldehyde intermediates and subsequent aldolase-mediated C-C bond formation, has been investigated. An enzymatic toolbox consisting of alcohol dehydrogenase AlkJ from Pseudomonas putida and the dihydroxyacetone-/hydroxyacetone-accepting aldolase variant Fsa1-A129S was applied. Pathway optimization was performed at the genetic and process levels. Three different arrangements of the alkJ and fsa1-A129S genes in operon, monocistronic, and pseudo-operon configuration were tested. The last of these proved to be most beneficial with regard to bacterial growth and protein expression levels. The optimized whole-cell catalyst, combined with a refined solid-phase extraction downstream purification protocol, provides diastereomerically pure carbohydrate derivatives that can be isolated in up to 91 % yield over two reaction steps.

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Asymmetric Biocatalytic Cannizzaro‐Type Reaction

Cited by 26 publications

References 46 publications

Promiscuity of Lipase‐Catalyzed Reactions for Organic Synthesis: A Recent Update

Promiscuity of Lipase‐Catalyzed Reactions for Organic Synthesis: A Recent Update

An Alcohol Dehydrogenase from the Short‐Chain Dehydrogenase/Reductase Family of Enzymes for the Lactonization of Hexane‐1,6‐diol

Cell Factory Design and Optimization for the Stereoselective Synthesis of Polyhydroxylated Compounds

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