Enzymatic catalysis in supercritical carbon dioxide: Comparison of different lipases and a novel esterase

Michor, Harald; Marr, Rolf; Gamse, Thomas; Schilling, Tobias; Klingsbichel, E.; Schwab, Helmut

doi:10.1007/bf00137815

Cited by 39 publications

(15 citation statements)

References 13 publications

(7 reference statements)

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“…The synthesis of (−)-citronellyl oleate from racemic citronellol was achieved using a Candida cylindracea lipase in supercritical carbon dioxide, but only in a narrow window of pressure and temperature (Ikushima et al, 1996). Some contradictory results suggest, however, that a generalisation of these findings should be treated with caution (Michor et al, 1996).…”

Section: Flavour Precursor Enzymes Referencesmentioning

confidence: 96%

Biotechnological Flavour Generation

Berger

Krings

Zorn

2010

Food Flavour Technology

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Section: Flavour Precursor Enzymes Referencesmentioning

confidence: 96%

Biotechnological Flavour Generation

Berger

Krings

Zorn

2010

Food Flavour Technology

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“…The use of scCO 2 as a process medium introduces the unique transport properties and the adjustable solvent power of an SCF [67].…”

Section: Enzymatically Catalyzed Esterification Of Monoterpenoids Witmentioning

confidence: 99%

“…Transesterification of racemic menthol 65 to optically active menthol acetate 66 by lipases (Lipase AY30, Lipase PS, Lipozym IM60, Novozym 435) and esterase (Esterase EP10) in scCO 2 was studied [67]. Isopropenyl acetate, n-butyl acetate, and triacetin were used as acetate sources (Scheme 18).…”

Section: Enzymatically Catalyzed Esterification Of Monoterpenoids Witmentioning

confidence: 99%

Environmentally Benign Transformations of Monoterpenes and Monoterpenoids in Supercritical Fluids

Волчо

Anikeev

2014

Supercritical Fluid Technology for Energy and Environmental Applications

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“…Enzyme-membrane reactors coupled with a membrane-based extractive product separation are especially used in the reduction of nonpolar ketones (Liese et al, 1998). However, the enzyme catalysis in pure alkanes (Laane et al, 1987;Klibanov, 1986), microemulsion-based gels (Backlund et al, 1995;Jenta et al, 1997), or supercritical fluids (Celia et al, 1999;Johnston et al, 1996;Michor et al, 1996) also seem to be promising alternatives to the catalysis in pure water. Another possibility for performing the reduction of hydrophobic substrates, is a reaction in a polar-water-miscible organic solvent, where enzymes and substrates are soluble.…”

Section: Introduction Generalmentioning

confidence: 99%

Stability and activity of alcohol dehydrogenases in W/O‐microemulsions: Enantioselective reduction including cofactor regeneration

Orlich

Berger

Lade

et al. 2000

Biotech & Bioengineering

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Microemulsions provide an interesting alternative to classical methods for the conversion of less water‐soluble substrates by alcohol dehydrogenase, but until now stability and activity were too low for economically useful processes. The activity and stability of the enzymes are dependent on the microemulsion composition, mostly the water and the surfactant concentration. Therefore, it is necessary to know the exact phase behavior of a given microemulsion reaction system and the corresponding enzyme behavior therein. Because of their economic and ecologic suitability polyethoxylated fatty alcohols were investigated concerning their phase behavior and their compatibility with enzymes in ternary mixtures. The phase behavior of Marlipal O13‐60 (C13EO6 in industrial quality)/cyclohexane/water and its effect on the activity and stability of alcohol dehydrogenase from Yeast (YADH) and horse liver (HLADH) and the carbonyl reductase from Candida Parapsilosis (CPCR) is presented in this study. Beside the macroscopic phase behavior of the reaction system, the viscosity of the system indicates structural changes of aggregates in the microemulsion. The changes of the enzyme activities with the composition are discussed on the basis of transitions from reverse micelles to swollen reverse micelles and finally, the transition to the phase separation. The formate dehydrogenase from Candida boidinii was used for the NADH‐regeneration during reduction reactions. While the formate dehydrogenase did not show any kinetic effect on the microemulsion composition, the other enzymes show significant changes of activity and stability varying the water or surfactant concentration of the microemulsion. Under certain conditions, stability could be maintained with HLADH for several weeks. Successful experiments with semi‐batch processes including cofactor regeneration and product separation were performed. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 70: 638–646, 2000.

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Enzymatic catalysis in supercritical carbon dioxide: Comparison of different lipases and a novel esterase

Cited by 39 publications

References 13 publications

Biotechnological Flavour Generation

Biotechnological Flavour Generation

Environmentally Benign Transformations of Monoterpenes and Monoterpenoids in Supercritical Fluids

Stability and activity of alcohol dehydrogenases in W/O‐microemulsions: Enantioselective reduction including cofactor regeneration

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