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Resolution of (±)-trans-2-phenylcyclohexan-1-ol by lipases from Candida rugosa: effect of catalyst source and reaction conditions

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Abstract

Candida rugosa lipase resolved trans-2-phenylcyclohexan-1-ol. A commercial and a laboratory preparation were compared and better results were obtained with the latter (E >200). Both enzyme preparations were strongly dependent on the substrate concentration for their enantioselectivity. This effect could be due to the presence of an esterase activity unspecific for trans-2-phenylcyclohexan-1-ol. © Rapid Science Ltd. 1998

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Authors and Affiliations

  1. Laboratory of Biotechnolody, URQUIMA, S.A. (URIACH GROUP), Arnau de Vilanova, 22–42, 08105 Sant Fost de Campsentelles, Barcelona, Spain

    José Luis del Río & Ignacio Faus

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  1. José Luis del Río
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  2. Ignacio Faus
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Luis del Río, J., Faus, I. Resolution of (±)-trans-2-phenylcyclohexan-1-ol by lipases from Candida rugosa: effect of catalyst source and reaction conditions. Biotechnology Letters 20, 1021–1025 (1998). https://doi.org/10.1023/A:1005413812214

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  • DOI: https://doi.org/10.1023/A:1005413812214

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