Carica papaya lipase-catalyzed transesterification resolution of secondary alcohols in organic solvents

Hung Ming Chen, Pei Yun Wang, Shau Wei Tsai*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

16 Scopus citations

Abstract

Aside from the capability in lipids bioconversion and kinetic resolution of chiral acids, Carica papaya lipase (CPL) as a naturally immobilized enzyme is explored as a potential biocatalyst for the transesterification resolution of chiral secondary alcohols with vinyl esters as the acyl donor in anhydrous solvents. A substrate-type model was proposed for interpreting the enzyme stereochemical preference, showing low enantioselectivity for all tested secondary alcohols except for (R,S)-methyl 3-phenyllactate (2). The kinetic analysis further revealed that the high enantioselectivity was mainly due to the prompt proton transfer from fast-reacting (S)-2 to the imidazole moiety of catalytic histidine in the deacylation step, as well as the low enzyme specific activity for (R)-1 or (S)-1 was owing to the difficult substrate affinity to the active site. Effects of changing the solvent, vinyl ester, and enzyme pretreatments on the lipase performance were also reported. Crown

Original languageEnglish
Pages (from-to)549-554
Number of pages6
JournalJournal of the Taiwan Institute of Chemical Engineers
Volume40
Issue number5
DOIs
StatePublished - 09 2009

Keywords

  • C. papaya lipase
  • Secondary alcohols
  • Transesterification resolution

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