Lipase-Catalyzed Solvent-Free Transesterification of Wood Sterols

Irene Martínez, Alejandro Markovits, Rolando Chamy, Andrés Markovits

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


Eighteen commercial lipase preparations, either immobilized or crude enzyme powders, were screened for the transesterification of wood sterols. The reactions were carried out in a solvent-free system, at the optimum temperature of the enzyme preparations as reported by the manufacturer and at the pressure of 2 mbar, with 5 or 10% in weight of the enzyme relative to the wood sterol content of the reacting mixture. Methyl esters of sunflower fatty acids were used as transesterifying agent. Of all the enzymes assayed, only Lipase TL from Pseudomonas stutzeri PL-836 (Meito Sangyo) exhibited any significant transesterifying capacity, 85 and 95% of conversion after 2 and 8 h of reaction, respectively, when 10% in weight of enzyme was used.

Original languageEnglish
Pages (from-to)55-62
Number of pages8
JournalApplied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Issue number1
StatePublished - Jan 2004


  • Enzymatic transesterification
  • Lipase
  • Solvent-free system
  • Sterols
  • Steryl esters


Dive into the research topics of 'Lipase-Catalyzed Solvent-Free Transesterification of Wood Sterols'. Together they form a unique fingerprint.

Cite this