Interspecies differences in the enantioselectivity of epoxide hydrolases in Cryptococcus laurentii (Kufferath) C.E. Skinner and Cryptococcus podzolicus (Bab'jeva & Reshetova) Golubev.

Isolates representing Cryptococcus laurentii and Cryptococcus podzolicus, originating from soil of a heathland indigenous to South Africa, were screened for the presence of enantioselective epoxide hydrolases for 2,2-disubstituted epoxides. Epoxide hydrolase activity for the 2,2-disubstituted epoxide (+/-)-2-methyl-2-pentyl oxirane was found to be abundantly present in all isolates. The stereochemistry of the products formed by the epoxide hydrolase enzymes from isolates belonging to the two species (11 isolates representing C.

Hydrolytic kinetic resolution of the enantiomers of the structural isomers trans -1-phenylpropene oxide and (2,3-epoxypropyl)benzene by yeast epoxide hydrolase.

Kinetic resolution of the enantiomers of trans -1-phenylpropene oxide and (2,3-epoxypropyl)benzene was achieved by yeasts from the genus Rhodotorula. The resolution of trans -1-phenylpropene oxide by Rhodotorula glutinis UOFS Y-0123 yielded (1R,2R)-epoxide (ee >98%, yield 30%) and (1R,2S)-diol (ee 95%, yield 40%). The highest enantio- and regioselectivity toward (2,3-epoxypropyl)benzene resided in Rhodotorula sp.

Correlation between the physicochemical properties of organic solvents and their biocompatibility toward epoxide hydrolase activity in whole-cells of a yeast, Rhodotorula sp.

Epoxides are often highly hydrophobic substrates and the presence of an organic co-solvent within an aqueous bioreactor is in such cases indicated. The effect of 40 water-miscible and -immiscible organic solvents on epoxide hydrolase activity in whole-cells of the yeast Rhodotorula sp. UOFS Y-0448 was investigated.