Studies of lipase‐catalyzed esterification reactions of some acetylenic fatty acids

• Published in: Lipids
• Main Authors: Lie Ken Jie, Marcel S. F., Xun, Fu
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 1998
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1007/s11745-998-0181-2; https://onlinelibrary.wiley.com/doi/full/10.1007/s11745-998-0181-2

Abstract Esterification of five positional isomers of acetylenic fatty acids [ viz . 9:1(2a), 11:1(10a), 18:1(6a), 18:1(9a) and 22:1(13a)] of different chain lengths with n ‐butanol in n ‐hexane in the presence of eight different lipases [Lipozyme IM 20 ( Rhizomucor miehei ), Lipolase 100T ( R. miehei ), Novozyme 435 ( Candida antarctica ), PPL (porcine pancreatic lipase), CCL ( C. cylindracea ), PS‐D ( Pseudomonas cepacia ), Lipase A‐12 ( Aspergillus niger ) and Lipase AY‐30 ( C. rugosa )] was studied. 2‐Nonynoic acid was not esterified except when catalyzed by the lipase from C. antarctica (Novozyme 435) to give 42% butyl ester after 48 h. The lipases from A. niger (Lipase A‐12) and C. rugosa (Lipase AY‐30) showed poor biocatalytic behavior in the esterification of the acetylenic fatty acids studied. 10‐Undecynoic acid gave the highest conversion rate of esterification with each kind of lipase used. 6‐Octadecynoic acid showed a marked degree of resistance to esterification carried out in the presence of C. cylindracea (CCL), P. cepacia (PS‐D), or porcine pancreatic (PPL) lipase but not significantly in the presence of the lipases of R. miehei (Lipozyme IM 20), R. miehei (Lipolase 100T), or Novozyme 435. 9‐Octadecynoic acid and 13‐docosynoic acid were not discriminated and were readily esterified by the remaining six lipases, but when compared to oleic acid the acetylenic fatty acids were comparatively much slower in conversion to the esters.