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Substrate specificity of α-chymotrypsin-catalyzed esterification in organic media

11 amino acid derivatives were tested as α-chymotrypsin substrates in the esterification reaction with methanol in organic media. The reactions were carried out in water-saturated ethyl acetate and in acetonitrile containing 4% water. α-Chymotrypsin adsorbed on Celite was used as a catalyst. From initial reaction rate measurements, the Michaelis-Menten parameters Vmax and KM were determine. All th

Asymmetric reduction of ketones with enzymes from acetic acid bacteria

Six strains of acetic acid bacteria were evaluated with respect to their capability to catalyze the stereoselective reduction of ketones. The cells were permeabilized before the bioconversions. The best strains were Gluconobacter oxydans DSM 50049 and Acetobacter aceti DSM 2002. Using either of these two strains it was possible to reduce all 12 ketones to (S)-alcohols with an enantiomeric excess o

On the importance of the support material for enzymatic synthesis in organic media : Support effects at controlled water activity

Enzymes were deposited on different porous support materials and these preparations were used to catalyze reactions in organic media. Reactions were carried out at specific water activities, achieved by equilibrating both the enzyme preparation and the substrate solution at the desired water activity before mixing them and thereby starting the reactions. The reaction rates obtained at the same wat

Enzyme catalysis in uni- and bi-continuous microemulsions : Dependence of kinetics on substrate partitioning

The kinetics of enzymatic conversion in a microemulsion have been investigated. Racemic 3-methylcyclohexanone was oxidized by horse-liver alcohol dehydrogenase (HLADH, E.C. 1.1.1.1.) using a coupled substrate-coenzyme regenerating cycle in a sodium bis-(2-ethylhexyl) sulphosuccinate (AOT)-isooctane-buffer microemulsion. Initial enzyme activity was measured as a function of the oil volume fraction

Three systems used for biocatalysis in organic solvents a comparative study

The activity and operational stability of horse liver alcohol dehydrogenase (HLADH) and αchymotrypsin were investigated in three systems commonly used for biocatalysis in organic solvents: 1. enzyme adsorbed on a solid support (celite) and added to the organic solvent (isooctane) 2. enzyme powder directly added to the organic solvent (isooctane). 3. enzyme dissolved in a microemulsion (AOT/isoocta

Green banana protection of gastric mucosa against experimentally induced injuries in rats

The protective capacities of fresh green (unripe) sweet bananas and of phosphatidylcholine and pectin (banana ingredients) against acute (ethanol- or indomethacin-induced) and chronic (indomethacin-induced) gastric mucosal lesions were evaluated in rats. Banana pulp was mixed with saline and given by gavage, as a pretreatment in a single dose. The identical protocol was used for pectin and phospha

Formation of C—C bonds by mandelonitrile lyase in organic solvents

Mandelonitrile lyase (EC 4.1.2.10) catalyzes the formation of D‐mandelonitrile from HCN and benzaldehyde. Mandelonitrile lyase was immobilized by adsorption to support materials, for example, Celite. The enzyme preparations were used in diisopropyl ether for production of D‐mandelonitrile. In order to obtain optically pure D‐mandelonitrile it was necessary to use reaction conditions which favor th

Enzymatic peptide synthesis in organic media : a comparative study of water-miscible and water-immiscible solvent systems

Peptide synthesis was carried out in a variety of organic solvents with low contents of water. The enzyme was deposited on the support material, celite, from an aqueous buffer solution. After evaporation of the water the biocatalyst was suspended in the reaction mixtures. The chymotrypsin-catalyzed reaction between Z-Phe-OMe and Leu-NH2 was used as a model reaction. Under the conditions used ([Z-P

Triglyceride interesterification by lipases. 1. Cocoa butter equivalents from a fraction of palm oil

Twelve commercially available triacylglycerol lipase preparations were screened for their suitability as catalysts in the interesterification of palm oil mid fraction and ethyl stearate to form a cocoa butter equivalent. Five fungal lipase preparations were found to be suitable. The hydrolytic activity of the commercial lipase preparations was tested with sunflower seed oil and was independent of

Enzymatic catalysis in microemulsions : Enzyme reuse and product recovery

A technique for enzyme reuse and product recovery from enzymatic catalysis in microemulsions is demonstrated. The enzymatic reaction is performed in a homogeneous isotropic microemulsion; AOT (sodium bis‐(2‐ethyl‐ hexyl)sulfosuccinate)/isooctane/buffer or C12E5(penta ethylene glycol dodecyl ether)/heptane/buffer. By small temperature changes the systems are shifted to two phase regions, where an o

Influence of the reaction medium on the product distribution of peroxidase-catalysed oxidation of p-cresol

p-Cresol was oxidized by hydrogen peroxide in a reaction catalysed by horseradish peroxidase and the low molecular weight products were investigated. In aqueous media Pummerer's ketone (I) was the dominating product but in organic media the product distribution was quite different; 2,2'-dihydroxy-5,5'-dimethyldiphenyl (II) was the main low molecular weight product. Similar product distributions we

A potentiometric enzyme electrode for monitoring in organic solvents

A potentiometric enzyme electrode is described for monitoring reactions in organic solvents. By use of an enzyme deposited on magnetic particles which are attracted to the tip of the electrode by means of a magnetic field, it is possible to produce an electrode in which the enzyme can easily be exchanged. As an example, studies of the chymotrypsin-catalyzed ester synthesis in diisopropyl ether and

Oxidation of trans- and cis-1,2-cyclohexanediol by Gluconobacter oxydans - Preparation of (R)- and (S)-2-hydroxycyclohexanone

The enzymatic oxidation of 1,2-cyclohexanediol and related substrates by Gluconobacter oxydans (ATCC 621) was investigated. At low pH, membrane-bound enzymes were active and at high pH, NAD-dependent, soluble enzymes showed activity. Whole bacterial cells were used to catalyze some bioconversions. Racemic trans-1,2-cyclohexanediol was oxidized at pH 3.5 to give (R)-2-hydroxycyclohexanone (96% e.e.