A.Bhaskar Rao

Stereoselective synthesis of (R)-(−)-denopamine, (R)-(−)-tembamide and (R)-(−)-aegeline via asymmetric reduction of azidoketones by Daucus carota in aqueous medium

A simple and efficient stereoselective synthesis of (R)-denopamine and other naturally occurring hydroxy amides from optically active (R)-2-azido-1-arylethanols, is described for the first time via reduction of the corresponding α-azidoarylketones with enzymes from Daucus Carota root, under mild and environmentally friendly conditions. The products are formed with high degrees of enantioselectivity.

A facile synthesis of (R)-(−)-2-azido-1-arylethanols from 2-azido-1-arylketones using baker's yeast

Abstract A novel and efficient stereoselective reduction of 2-azido-1-aryl ketones using bakers yeast is described.

Lipase catalysed kinetic resolution of racemic (±)2,2-dimethyl-3-(2-methyl-1-propenyl)-cyclopropane carboxyl esters+

Optically active (1R)(−) and (1S)(+)-trans-Chrysanthemic acid and its esters were prepared from corresponding racemic methyl ester by lipase mediated enantioselective hydrolysis, is described.

Enzyme catalysed kinetic resolution of racemic 2,2-dimethyl-3-(2,2-disubstituted vinyl) cyclopropane car☐ylic acids anchored on polymer supports

Kinetic resolution oftrans-substituted cyclopropane car☐ylic acids anchored on a solid support by lipase is described.

Optimization of fermentation conditions for production of glycopeptide antibiotic vancomycin by Amycolatopsis orientalis.

Glycopeptides produced by Streptomyces species are the drugs used against β-lactam drug-resistant staphylococcal infections, and vancomycin is important among them. Increased prevalence of resistant strains increased the usage of vancomycin worldwide and also promoted attempts for indigenous production. The optimum process conditions pH, temperature, inoculum size, agitation, and aeration for vancomycin production by Amycolatopsis orientalis were evaluated, statistically analyzed, and the response surface curves were constructed. The optimum process conditions were a pH of 7.6, a temperature of 29°C, an inoculum size of 4.5%, an agitation of 255 rpm, and an aeration of less than 1:10 medium-to-air ratio.

Enzymatic asymmetric hydroxylation of unnatural substrates with soybean lipoxygenase

Abstract Surrogate substrates mimicking the natural substrate (linoleic acid) bearing a spacing prosthetic group with a non-ionic hydroxyl terminus undergo asymmetric hydroxylation with soybean lipoxygenase. The prosthetic modifier supplies the missing structural features needed for enzymatic recognition and controls the regiochemical outcome of the reaction by its high hydrophobic content. The effect of pH on the regiochemistry clearly shows that all the substrates can arrange themselves at the active site of soybean lipoxygenase in only one orientation leading to formation of hydroperoxides by oxygenation at the ω-6 carbon.

Design and synthesis of useful intermediates for novel lipoxygenase substrates through enzymatic resolution

Abstract Unnatural lipoxygenase substrates carrying spacing modifiers with a non-ionic hydroxy terminus and with methylene (flanked by the cis,cis diene moiety) pro-( S )-hydrogen can be synthesized from the intermediates 1a – 1c . These intermediates are conveniently synthesized via enzymatic resolution with lipase in organic solvents.

Enzymatic resolution of (±)-cis-3-(2,2-dichloro-3,3,3-trifluoropropyl)-2,2-dimethylcyclopropane carboxylate

A novel biocatalytic kinetic resolution of a chemically labile racemic cis-3-(2,2-dichloro-3,3,3-trifluoropropyl)-2,2-dimethyl cyclopropane carboxylate ester is studied.

l-Selective dipeptide synthesis using novel thermophilic enzyme from Clostridium sp.

Abstract— A novel, inexpensive, thermophilic protease-type enzyme isolated from Clostridium thermohydrosulfuricum was used fordipeptide synthesis. The enzyme showed broad substrate selectivity and enantioselectivity towards L -amino acids in peptide bondformation.