Enzyme-catalyzed regioselective transesterification of peracylated sophorolipids

Jason A. Carr, Kirpal S. Bisht

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


Regioselective transesterifications and hydrolysis of peracylated sophorolipid (SL) derivatives catalyzed by lipases was investigated. This study is the first evaluation of the lipase-catalyzed reactions on the non-lactonic SL derivatives. Four lipases, namely from porcine pancreas (PPL, Type II), Candida rugosa (AYS, TypeVII), Pseudomonas cepacia (PS-30), and Candida antarctica (Novozym 435, carrier fixed lipase fraction B) were used in anhydrous THF or in phosphate buffer (pH=7.4, 0.2 M). It was confirmed from the detailed spectral analysis of the products that transesterification failed to furnish any free hydroxyls on the sophorose ring. Instead, transesterification took place on the methyl ester located at the carboxylic end of the 17-hydroxyoctadecenoic acid chain attached to the C-1′ position of the sophorose ring. It is proposed that in absence of the lactonic structural motif, the binding of the peracylated non-lactonic SLs in the lipase binding pocket takes place such that the carboxyl group of the octadecenoic acid, not the sophorose sugar, is preferentially accessible to the active site.

Original languageEnglish (US)
Pages (from-to)7713-7724
Number of pages12
Issue number39
StatePublished - Sep 22 2003
Externally publishedYes


  • Lipase
  • Regioselective
  • Sophorolipids
  • Transesterification

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry


Dive into the research topics of 'Enzyme-catalyzed regioselective transesterification of peracylated sophorolipids'. Together they form a unique fingerprint.

Cite this