Applied Biochemistry and Biotechnology

, Volume 149, Issue 1, pp 79–88 | Cite as

Screening and Immobilization Burkholderia sp. GXU56 Lipase for Enantioselective Resolution of (R,S)-Methyl Mandelate

  • Han-Ning Wei
  • Bo WuEmail author


Microorganisms producing lipase were isolated from soil and sewage samples and screened for enantioselective resolution of (R,S)-methyl mandelate to (R)-mandelic acid. A strain designated as GXU56 was obtained and identified as Burkholderia sp. Preparing immobilized GXU56 lipase by simple adsorption on octyl sepharose CL-4B, the optimum temperature was shifted from 40 °C (free lipase) to 50 °C (immobilized lipase), and the optimum pH was shifted from 8.0 (free lipase) to 7.2 (immobilized lipase). The immobilized enzyme displayed excellent stability in the pH range of 5.0–8.0, at the temperatures below 50 °C and in organic solvents compared with free enzyme. Enantioselectivity ratio for (R)-mandelic acid (E) was dramatically improved from 29.2 to more than 300 by applying immobilized lipase in the resolution of (R,S)-methyl mandelate. After five cycles of use of immobilized lipase, conversion and enantiomeric excess of (R)-mandelic acid were 34.5% and 98.5%, respectively, with enantioselectivity ratio for (R)-mandelic acid (E) of 230. Thus, octyl-sepharose-immobilized GXU56 lipase can be used as a bio-resolution reagent for producing (R)-mandelic acid.


Burkholderia sp. GXU56 Immobilization Lipase (R)-Mandelic acid 


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Copyright information

© Humana Press Inc. 2008

Authors and Affiliations

  1. 1.College of Life Science and TechnologyGuangxi University, The Key Laboratory of Ministry of Education for Microbial and Plant Genetic Engineering, Guangxi Key Laboratory of Subtropical Bioresources Conservation and UtilizationNanningPeople’s Republic of China

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