Characterization of fatty amides produced by lipase-catalyzed amidation of multi-hydroxylated fatty acids.
Novel multi-hydroxylated primary fatty amides produced by direct amidation of 7,10-dihydroxy-8(E)-octadecenoic acid and 7,10,12-trihydroxy-8(E)-octadecenoic acid were characterized by GC-MS and NMR. The amidation reactions were catalyzed by immobilized Pseudozyma (Candida) antarctica lipase B (Novozym 435) in organic solvent with ammonium carbamate. The mass spectra of the underivatized products exhibited characteristic primary amide peaks at m/z 59 and m/z 72 that differed in peak intensities. Other peaks present were consistent with cleavage next to the hydroxyl groups. The mass spectra of the silylated amidation products showed the correct molecular weight and the typical fragmentation pattern of silylated hydroxy compounds. The mass spectra, together with proton and 13C NMR data, suggest that the products of lipase-catalyzed direct amidation of 7,10-dihydroxy-8(E)-octadecenoic acid and 7,10,12-trihydroxy-8(E)-octadecenoic acid are, 7,10-dihydroxy-8(E)-octadecenamide and 7,10,12-trihydroxy-8(E)-octadecenamide acid, respectively. Amidation of multi-hydroxylated fatty acids had increased the melting point, but reduced the surface active property of the resulting primary amides.
Levinson
William E
WE
Microbial Genomics and Bioprocessing Research Unit, National Center for Agricultural Utilization Research, Agricultural Research Service, United States Department of Agriculture, 1815 N. University Street, Peoria, IL 61604, USA.
Kuo
Tsung Min
TM
Knothe
Gerhard
G
D000577:Amides / Q000378:metabolism*; D002384:Catalysis; D005227:Fatty Acids / Q000378:metabolism*; D006900:Hydroxylation; D008049:Lipase / Q000378:metabolism*; D021241:Spectrometry, Mass, Electrospray Ionization
D000577:Amides; D005227:Fatty Acids; D008049:Lipase