Biocatalysis - key to sustainable industrial chemistry

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Current Opinion in Biotechnology (Impact Factor: 8.04). 10/2010; 21(6):713-24. DOI: 10.1016/j.copbio.2010.09.016
Source: PubMed

ABSTRACT The ongoing trends to process improvements, cost reductions and increasing quality, safety, health and environment requirements of industrial chemical transformations have strengthened the translation of global biocatalysis research work into industrial applications. One focus has been on biocatalytic single-step reactions with one or two substrates, the identification of bottlenecks and molecular as well as engineering approaches to overcome these bottlenecks. Robust industrial procedures have been established along classes of biocatalytic single-step reactions. Multi-step reactions and multi-component reactions (MCRs) enable a bottom-up approach with biocatalytic reactions working together in one compartment and recations hindering each other within different compartments or steps. The understanding of the catalytic functions of known and new enzymes is key for the development of new sustainable chemical transformations.

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    ABSTRACT: The screening of four invasive plant species for use as biocatalysts in the stereoselective reduction of ketones is reported. Our studies revealed that fruits of Ligustrum lucidum can be used for the bioreduction of acetophenone to (S)-1-phenylethanol (94% conversion, > 99 enantiomeric excess [ee]%). Using this methodology, 13 substituted (S)-phenylethanols were synthesized with good ee values (> 99.9 to 78%) using a technique which is more environmentally friendly than classical reduction of prochiral ketones. The results reveal the fruits of L. lucidum to be promising biocatalysts for the production of key intermediates.
    Biocatalysis and Biotransformation 12/2014; 32(5-6). DOI:10.3109/10242422.2014.976634 · 1.09 Impact Factor
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    ABSTRACT: Diverse applications of the versatile bacterial cytochrome P450 enzymes (P450s) are hampered by their requirement for the auxiliary proteins, ferredoxin reductases and ferredoxins, that transfer electrons to P450s. Notably, this limits the use of P450s as immobilized enzymes for industrial purposes. Herein, we demonstrate the immobilization of a bacterial P450 and its redox protein partners by supramolecular complex formation using a self-assembled heterotrimeric protein. Employment of homodimeric phosphite dehydrogenase (PTDH) for cross-linking "proliferating cell nuclear antigen-utilized protein complex of P450 and its two electron transfer-related proteins" (PUPPET) yielded a gelling PUPPET-PTDH system capable of regenerating NADH for electron supply owing to its phosphite oxidation activity. The protein gel catalyzed monooxygenation in the presence of phosphite and NAD(+). The gel was completely water-insoluble and could be reused. This concept of oligomeric protein-insolubilized enzymes can be widely applied to various multienzymatic reactions such as cascade reactions and coupling reactions.
    Scientific Reports 03/2015; 5:8648. DOI:10.1038/srep08648 · 5.08 Impact Factor
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    ABSTRACT: Biocatalytic asymmetric reduction of ethyl-4,4,4-trifluoroacetoacetate under water-deficient reaction conditions using a ‘smart cosubstrate’ 1,4-butanediol was demonstrated up to 2 liter-scale. Substrate concentrations of 100 g/L were applied by using half-molar equivalent of 1,4-butanediol in methyl-tert-butylether (MTBE). Using this approach, full conversion of ethyl-4,4,4-trifluoroacetoacetate to the corresponding (S)-alcohol with an excellent enantiomeric excess (ee) of ≥99% was accomplished in 5 days. 150 g of isolated enantiopure product with high purity (94%) was obtained.
    Organic Process Research & Development 02/2015; 19(2). DOI:10.1021/op500374x · 2.55 Impact Factor


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Dec 31, 2014