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Biocatalysis screening

Kruse T, Ho K, Yoo HD, Johnson T, Hippely M, Park JH, Flavell R, Bobzin S (2008) In planta biocatalysis screen of P450s identifies 8-methoxyp-soralen as a substrate for the CYP82C subfamily, yielding original chemical structures. Chem Biol 15 149-156... [Pg.441]

In order to broaden the field of biocatalysis in ionic liquids, other enzyme classes have also been screened. Of special interest are oxidoreductases for the enan-tioselective reduction of prochiral ketones [40]. Formate dehydrogenase from Candida boidinii was found to be stable and active in mixtures of [MMIM][MeS04] with buffer (Entry 12) [41]. So far, however, we have not been able to find an alcohol dehydrogenase that is active in the presence of ionic liquids in order to make use of another advantage of ionic liquids that they increase the solubility of hydrophobic compounds in aqueous systems. On addition of 40 % v/v of [MMIM][MeS04] to water, for example, the solubility of acetophenone is increased from 20 mmol to 200 mmol L ... [Pg.342]

Directed Enzyme Evolution Screening and Selection Methods, Humana Press, Totowa. Vol. 230. (b) Brakmann, S. and Johnsson, K. (eds)(2002) Directed Molecular Evolution of Proteins (or How to Improve Enzymes for Biocatalysis), Wdey-VCH Verlag GmbH, Weinheim. (c) Brakmann, S. and Schwienhorst, A. (eds)... [Pg.57]

Microbial reduction has been recognized for decades as a laboratory method of preparing alcohols from ketones with exquisite enantioselectivity. The baker s yeast system represents one of the better known examples of biocatalysis, taught on many undergraduate chemistry courses. Numerous other microorganisms also produce the ADH enzymes (KREDs) responsible for asymmetric ketone reduction, and so suitable biocatalysts have traditionally been identified by extensive microbial screening. Homann et have... [Pg.48]

The examples of bioorganic chemistry in the previous paragraph are all concerned with the known biocatalytic assays, in which the effects of miniaturization on the efficiency of the analytical method were investigated. Recently, a new development has started in which the biocatalytic process itself has become the center of attention. Biocatalysis in microreactors, as described in here, deal with the investigation of the use of enzymes for the production of molecules. Two different approaches can be identified. In one line of investigation, the miniaturized reaction environment is used to screen the efficiency of an enzyme. In this case, only small amounts of... [Pg.193]

Microreactor technology offers the possibility to combine synthesis and analysis on one microfluidic chip. A combination of enantioselective biocatalysis and on-chip analysis has recently been reported by Beider et al. [424]. The combination of very fast separations (<1 s) of enantiomers using microchip electrophoresis with enantioselective catalysis allows high-throughput screening of enantioselective catalysts. Various epoxide-hydrolase mutants were screened for the hydrolysis of a specific epoxide to the diol product with direct on-chip analysis of the enantiomeric excess (Scheme 4.112). [Pg.203]

PHENOMICS platform) and screen for potential uses in biotechnology. Table 31.11 lists different classes of extremophiles from which useful enzymes have been derived. Further information on extremophiles and their potential utility for biocatalysis can be found in the reviews by Van den Burg (2003) and Gomes and Steiner (2004).31 32... [Pg.1415]

Rubin-Pitel SB, Zhao H. Recent advances in biocatalysis by directed enzyme evolution. Comb. Chem. High Throughput Screen 2006 9 247-257. [Pg.344]


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See also in sourсe #XX -- [ Pg.276 , Pg.277 ]

See also in sourсe #XX -- [ Pg.1019 ]




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Biocatalysis

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