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Please use this identifier to cite or link to this item: http://hdl.handle.net/10204/762

Title: Optimisation of the biocatalytic resolution of styrene oxide by whole cells of Rhodotorula glutinis
Authors: Yeates, CA
Smit, MS
Botes, AL
Breytenbach, JC
Krieg, HM
Keywords: Styrene oxide
Yeast epoxide hydrolase
Whole cells
Vicinal diols
Rhodotorula glutinis
Issue Date: Jan-2007
Publisher: Elsevier Science Inc
Citation: Yeates CA et al. 2007. Optimisation of the biocatalytic resolution of styrene oxide by whole cells of Rhodotorula glutinis. Enzyme and Microbial Technology, Vol 40(2), pp 221-227
Abstract: Various studies have described the optimisation of the hydrolysis of epoxides through epoxide hydrolase, however, far fewer have investigated the specific application of whole cells containing the enzyme. For this reason the enantioselective biocatalytic hydrolysis of styrene oxide by Rhodotorula glutinis UOFS Y-0653 through the use of whole cells was explored. It was found that a pH of 7.2, temperature of 45 °C and an initial substrate concentration of 50 mM led to maximum enzymatic activity. The whole cells were resistant to a changing environment. High temperatures were found to increase enzymatic activity but decrease enantioselectivity. At low temperatures (15 °C) enantioselectivity was significantly increased leading to an increase in both enantiopure substrate yield and the enantiomeric excess of both the substrate and product. No substrate inhibition was observed at initial substrate concentrations as high as 100 mM. The low deactivation energy (85.2 kJ/mol) obtained for this hydrolysis reaction suggests thermal instability of the enzyme. No significant effect on the reaction was observed when using unbuffered water instead of phosphate buffer as reaction medium.
Description: http://0-www.sciencedirect.com.innopac.up.ac.za/science/journal/01410229
URI: http://hdl.handle.net/10204/762
ISSN: 0141-0229
Appears in Collections:Microbial expression systems
Enzyme technologies
General science, engineering & technology

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