Optimisation of the biocatalytic resolution of styrene oxide by whole cells of Rhodotorula glutinis

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 gl...

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Vydáno v:	Enzyme and microbial technology Ročník 40; číslo 2; s. 221 - 227
Hlavní autoři:	Yeates, C.A., Smit, M.S., Botes, A.L., Breytenbach, J.C., Krieg, H.M.
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Amsterdam Elsevier Inc 01.01.2007 Elsevier Science
Témata:	Biological and medical sciences Biotechnology Enantioselectivity Fundamental and applied biological sciences. Psychology Optimisation Rhodotorula glutinis Styrene oxide Whole cells Yeast epoxide hydrolase Enantioselectivity Whole cells Optimisation Yeast epoxide hydrolase Styrene oxide Biocatalysis Yeast Enzyme Rhodotorula glutinis Epoxide hydrolase Optimization Fungi Styrene Ether hydrolases Hydrolases Fungi Imperfecti Thallophyta
ISSN:	0141-0229, 1879-0909
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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.
AbstractList	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 50mM 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 100mM. The low deactivation energy (85.2kJ/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. 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.
Author	Smit, M.S. Breytenbach, J.C. Botes, A.L. Yeates, C.A. Krieg, H.M.
Author_xml	– sequence: 1 givenname: C.A. surname: Yeates fullname: Yeates, C.A. organization: Department of Pharmaceutical Chemistry, North-West University, Private Bag X6001, Potchefstroom 2520, South Africa – sequence: 2 givenname: M.S. surname: Smit fullname: Smit, M.S. organization: Microbial, Biochemical and Food Biotechnology, University of the Free State, P.O. Box 339, Bloemfontein 9300, South Africa – sequence: 3 givenname: A.L. surname: Botes fullname: Botes, A.L. organization: Bio/Chemtek, CSIR, P.O. Box 395, Pretoria 0001, South Africa – sequence: 4 givenname: J.C. surname: Breytenbach fullname: Breytenbach, J.C. organization: Department of Pharmaceutical Chemistry, North-West University, Private Bag X6001, Potchefstroom 2520, South Africa – sequence: 5 givenname: H.M. surname: Krieg fullname: Krieg, H.M. email: chehmk@puk.ac.za organization: School of Chemistry and Biochemistry, North-West University, Private Bag X6001, Potchefstroom 2520, South Africa
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Cites_doi	10.1271/bbb1961.54.1819 10.1016/S1367-5931(00)00179-4 10.1016/S0957-4166(97)00639-3 10.1016/S0957-4166(99)00355-9 10.1016/S1381-1177(98)00123-4 10.1016/S0040-4020(98)00422-0 10.1023/A:1005500407152 10.1016/j.tet.2003.10.119 10.1016/S0957-4166(98)00180-3 10.1021/jo9714371 10.1002/(SICI)1097-0290(19960105)49:1<70::AID-BIT9>3.0.CO;2-Q 10.1016/S0168-1656(02)00359-0 10.1016/S1381-1177(97)00005-2 10.1023/A:1023427305388 10.1016/S1381-1169(01)00394-6 10.1016/S1381-1177(00)00230-7
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Keywords	Enantioselectivity Whole cells Optimisation Yeast epoxide hydrolase Styrene oxide Biocatalysis Yeast Enzyme Rhodotorula glutinis Epoxide hydrolase Optimization Fungi Styrene Ether hydrolases Hydrolases Fungi Imperfecti Thallophyta
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SubjectTerms	Biological and medical sciences Biotechnology Enantioselectivity Fundamental and applied biological sciences. Psychology Optimisation Rhodotorula glutinis Styrene oxide Whole cells Yeast epoxide hydrolase
Title	Optimisation of the biocatalytic resolution of styrene oxide by whole cells of Rhodotorula glutinis
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