Selectivity of lipases for estolides synthesis

Anamaria Todea, A.E. Frissen, Linda G. Otten, I. Arends, F. Peter, C.G. Boeriu*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

13 Citations (Scopus)


Lipase-catalyzed synthesis of estolides starting from different saturated (C16 16OH, C18 12OH) and unsaturated (C18:1 9 cis 12-OH) hydroxy-fatty acids was investigated. For this reason, the catalytic efficiency of several native and immobilized lipases in different organic reaction media at temperatures up to 75 °C was studied. The formation of mono- and di-lactone as well as estolide’s chain elongation depends on the type and source of lipase. The lipase from Pseudomonas stutzeri immobilized by cross-linking as cross-linked enzymes aggregates (CLEAs) was the best biocatalyst in terms of chain elongation. Estolides with polymerization degree up to 10 were obtained at substrate conversions higher than 80 %.
Original languageEnglish
Pages (from-to)51-58
JournalPure and Applied Chemistry
Issue number1
Publication statusPublished - 2015


  • Estolide
  • Hydroxy fatty acid
  • Lipase
  • POC-2014
  • Selectivity


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