Biocatalysis—Key to sustainable industrial chemistry

Sigma-Aldrich, Industriestrasse 25, CH-9470 Buchs, Switzerland.
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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    • "Tomando en cuenta lo anterior, actualmente muchas aplicaciones industriales se ven apoyadas en gran medida por el uso de la tecnología enzimática, lo cual ha provocado que las ventas de enzimas a nivel mundial crezcan anualmente en aproximadamente un 7.5 % (Beilen y Li, 2002; Rasmussen y Morrissey, 2007; Ferraro y col. 2010; Wohlgemuth, 2010). Las enzimas del grupo de las hidrolasas, particularmente las proteasas, representan al menos el 60% de las ventas globales de enzimas en el mundo. "
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    • "These alcohols are required as key intermediates in the production of pharmaceuticals and other important chemicals (Yadav 2002 and 2008; Ishihara et al. 2003; Caron et al. 2005). Despite these reductive processes being of great importance to the chemical industry, comparatively few reduction methodologies have been developed, which take into account the concept of green chemistry (environmentally friendly reaction systems) in order to avoid the formation of toxic waste that may pollute the environment (Wohlgemuth 2010). Compared with conventional chemical processing, biocatalytic asymmetric reductions can offer more selective reactions, environmentally benign processes, and energy-effi cient operations. "
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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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    • "Enzyme biocatalysis is positioned as a green and sustainable technology (Wohlgemuth, 2010) but achievement of satisfactory bioconversion efficiencies and effective use of the enzymes may require special measures such as re-cycling or immobilization for successful industrial application (Garcia-Galan et al., 2011). "
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    ABSTRACT: A simple enzyme immobilization method accomplished by promoting membrane fouling formation is proposed. The immobilization method is based on adsorption and entrapment of the enzymes in/on the membrane. To evaluate the concept, two membrane orientations, skin layer facing feed (normal mode) and support layer facing feed (reverse mode), were used to immobilize alcohol dehydrogenase (ADH, EC and glutamate dehydrogenase (GDH, EC, respectively. The nature of the fouling in each mode was determined by filtration fouling models. The permeate flux was larger in the normal mode, but the reverse mode allowed for higher enzyme loading and stability, and irreversible fouling (i.e. pore blocking) developed more readily in the support structure than in the skin layer. Compared with an enzymatic membrane reactor (EMR) with free enzymes, the novel EMR with enzymes immobilized in membrane support improved the enzyme reusability (especially for ADH), and reduced the product inhibition (especially for GDH).
    Bioresource Technology 08/2013; 147C:260-268. DOI:10.1016/j.biortech.2013.08.019 · 5.04 Impact Factor
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