Partially purified Carica papaya lipase: A versatile biocatalyst for the hydrolytic resolution of (R,S)-2-arylpropionic thioesters in water-saturated organic solvents

I. Son Ng, Shau Wei Tsai*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

26 Scopus citations

Abstract

With the hydrolytic resolution of (R,S)-naproxen 2,2,2-trifluoroethyl thioesters in water-saturated isooctane as a model system, improvements of the specific lipase activity and thermal stability were found when a crude Carica papaya lipase (CPL) was partially purified and employed as the biocatalyst. The partially purified Carica papaya lipase (PCPL) was furthermore explored as an effective enantioselective biocatalyst for the hydrolytic resolution of (R,S)-profen thioesters in water-saturated organic solvents. The kinetic analysis in water-saturated isooctane indicated that both acyl donor and acyl acceptor have profound influences on the lipase activity, E-value, and enantioselectivity. Inversion of the enantioselectivity from (S)- to (R)-thioester was found for (R,S)-fenoprofen and (R,S)-ketoprofen thioesters that contained a bulky substituent at the meta-position of 2-phenyl moiety of the acyl part. Kinetic constants for the acylation step were furthermore estimated for elucidating the kinetic data and postulating an active site model. The thermodynamic analysis indicated that the enantiomer discrimination was driven by the difference of activation enthalpy (ΔΔH) and that of activation entropy (ΔΔS), yet the latter was dominated for most of the reacting systems. The postulated active site model was supported from the variation of ΔΔH and ΔΔS with the acyl moiety, in which a good linear enthalpy-entropy compensation relationship was also illustrated. A comparison of the performances between Candida rugosa lipase (CRL) and PCPL indicated that PCPL was superior to CRL in terms of the better thermal stability, similar or better lipase activity for the fast-reacting substrate, time-course-stability, and lower enzyme cost.

Original languageEnglish
Pages (from-to)106-113
Number of pages8
JournalBiotechnology and Bioengineering
Volume91
Issue number1
DOIs
StatePublished - 05 07 2005
Externally publishedYes

Keywords

  • (R,S)-profen thioesters
  • Hydrolytic resolution
  • Partially purified Carica papaya lipase

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