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This Letter introduces a new, cheap and green protocol for the thio-Michael reaction. Here we applied three free enzymes such as lipase from pancreas porcine, chymosin and papain and an immobilized one: the Liposyme®. The reactions were executed at room temperature and resulted in the thio-Michael adduct in good or excellent yields. The protocol describes the use of EtOH as solvent and a less percentage of enzymes, which is in concordance with the green chemistry topics, so we can mention that chymosin and papain were used as biocatalyst in an organic reaction for the first time in this Letter.

A method is described for the synthesis of (±)-2,3-epoxy propyl esters from glycerol, involving reaction of epichlorohydrin with sodium or potassium salts of carboxylic acids in the presence of TBAB as catalyst, with moderate to excellent yields. Kinetic resolution of glycidyl butyrate by lipase of Thermomyces lanuginosa has been achieved with remarkable enantiomeric excess (ee >99%) using 1,4-dioxane as a co-solvent in pure buffer solution (30 and 50 °C, pH = 7.0).

A synthesis of a functionalized bicyclo[6.2.1]undecane, N -(7-hydroxymethyl-bicyclo[6.2.1]undeca-3,5,9-trien-2-yl)-4-methyl-benzenesulfonamide, is described. Starting with a [6+4] cycloaddition between cyclopentadiene and cycloheptatrienone, the final product was prepared in five steps with an overall 37% yield. The remarkable resistance to hydrolysis of an intermediate lactam was overcome by tosylating the amide and reducing with LiAlH 4 .

A bicyclo[6.2.1]undecane model compound of the core structure of the biologically active furanoheliangolide sesquiterpene was synthesized. This new and short route was developed by using a solvent-free Diels–Alder reaction between cyclopentadiene and 3-nitro-2-cyclohexenone, followed by simple transformations. Theoretical calculations were performed in order to understand reactivity aspects of the cycloaddition.