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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.

On the importance of the support material for bioorganic synthesis : Influence of water partition between solvent, enzyme and solid support in water‐poor reaction media

α‐Chymotrypsin was adsorbed on solid support materials and the catalytic activity of the preparations in organic solvents was studied. The activity was highly dependent on the nature of the support material and on the amount of water present in the reaction mixture. There appears to be competition for the water in the system between the enzyme, the support material and the solvent. The support mat

The influence of water on protease‐catalyzed peptide synthesis in acetonitrile/water mixtures

Protease‐catalyzed peptide synthesis in acetonitrile water mixtures, containing 0–90% water, was investigated. α‐Chymotrypsin, as well as thermolysin, were deposited on solid supports, prior to exposure to the reaction media. Peptide syntheses were performed using both a kinetically controlled process (chymotrypsin) and an equilibrium‐controlled synthesis (thermolysin). The activity of chymotrypsi

Activity and operational stability of immobilized mandelonitrile lyase in methanol/water mixtures

The enzyme mandelonitrile lyase was covalently immobilized on solid support materials using different methods. Immobilization on porous silica using coupling with glutaraldehyde afforded preparations with high enzyme loading (up to 9% (w/w)). The immobilized enzyme was used in a packed bed reactor for the continuous production of d-mandelonitrile from benzaldehyde and cyanide. The influence of the