Lipase-catalyzed solvent-free transesterification of wood sterols.
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.
Martínez
Irene
I
School of Biochemical Engineering, Catholic University of Valparaíso, Av. Brazil 2147, PO Box 4059, Valparaíso, Chile.
Markovits
Alejandro
A
Chamy
Rolando
R
Markovits
Andrés
A
D004951:Esterification; D004952:Esters; D005227:Fatty Acids / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry* / Q000145:classification*; D010865:Pilot Projects; D010938:Plant Oils / Q000737:chemistry*; D044223:Pseudomonas stutzeri / Q000201:enzymology*; D012997:Solvents / Q000737:chemistry; D013045:Species Specificity; D013261:Sterols / Q000737:chemistry*; D000074242:Sunflower Oil; D014934:Wood
D004952:Esters; D005227:Fatty Acids; D010938:Plant Oils; D012997:Solvents; D013261:Sterols; D000074242:Sunflower Oil; D008049:Lipase