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  4. Engineering of a borneol dehydrogenase from P. putida for the enzymatic resolution of camphor
 
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2021
Journal Article
Title

Engineering of a borneol dehydrogenase from P. putida for the enzymatic resolution of camphor

Abstract
Several thousand different terpenoid structures are known so far, and many of them are interesting for applications as pharmaceuticals, flavors, fragrances, biofuels, insecticides, or fine chemical intermediates. One prominent example is camphor, which has been utilized since ancient times in medical applications. Especially (−)-camphor is gaining more and more interest for pharmaceutical applications. Hence, a commercial reliable source is needed. The natural sources for (−)-camphor are limited, and the oxidation of precious (−)-borneol would be too costly. Hence, synthesis of (−)-camphor from renewable alpha-pinene would be an inexpensive alternative. As the currently used route for the conversion of alpha-pinene to camphor produces a mixture of both enantiomers, preferably catalytic methods for the separation of this racemate are demanded to yield enantiopure camphor. Enzymatic kinetic resolution is a sustainable way to solve this challenge but requires suitable enzymes. In this study, the first borneol dehydrogenase from Pseudomonas sp. ATCC 17453, capable of catalyzing the stereoselective reduction of camphor, was examined. By using a targeted enzyme engineering approach, enantioselective enzyme variants were created with E-values > 100. The best variant was used for the enzymatic kinetic resolution of camphor racemate, yielding 79% of (−)-camphor with an ee of > 99%.
Author(s)
Hofer, Michael  
Diener, Julia  
Begander, Benjamin
Kourist, Robert
Sieber, Volker  
Journal
Applied microbiology and biotechnology  
Open Access
DOI
10.1007/s00253-021-11239-5
Language
English
Fraunhofer-Institut für Grenzflächen- und Bioverfahrenstechnik IGB  
Keyword(s)
  • Borneol dehydrogenase

  • Enzymatic resolution

  • Camphor

  • Racemate

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