Cc. Akoh et Ln. Yee, ENZYMATIC-SYNTHESIS OF POSITION-SPECIFIC LOW-CALORIE STRUCTURED LIPIDS, Journal of the American Oil Chemists' Society, 74(11), 1997, pp. 1409-1413
An immobilized sn-1,3-specific lipase from Rhizomucor miehei (IM 60) w
as used to catalyze the interesterification of tristearin (C-18:0) and
tricaprin (C-10:0) to produce low-calorie structured lipids (SL). Acc
eptable product yields were obtained from a 1:1 mole ratio of both tri
acylglycerols with 10% (w/w of reactants) of IM 60 in 3 mL hexane. The
SL molecular species, based on total carbon number, were 44.2% C-41 a
nd 40.5% C-49, with 3.8 and 11.5% unreacted tristearin C-57 and tricap
rin C-27, respectively, remaining in the product mixture. The best yie
ld of C-41 species (44.3%) was obtained with zero added water. Tricapr
ylin (C-8:0) was also successfully interesterified with tristearin in
good yields at 1:1 mole ratio. Products were analyzed by reverse-phase
high-performance liquid chromatography with an evaporative light-scat
tering detector. Reaction parameters, such as substrate mole ratio, en
zyme load, time course, added water, reaction media, and enzyme reuse,
were also investigated. Hydrolysis by pancreatic lipase revealed the
specific fatty acids present at the sn-1,3 positions of SL.