Am. Fureby et al., PREPARATION OF DIGLYCERIDES BY LIPASE-CATALYZED ALCOHOLYSIS OF TRIGLYCERIDES, Enzyme and microbial technology, 20(3), 1997, pp. 198-206
Lipase from Penicillium roquefortii immobilized on porous polypropylen
e particles was used for enzymatic preparation of 1,2-diglycerides by
alcoholysis in organic media. A screening of commercially available li
pases showed that lipases fi om Penicillium species produced high amou
nts of 1,2-diglycerides from triglycerides. Reaction parameters such a
s solvent, alcohol, water activity, and fatty acid chain length were i
nvestigated. The positional selectivity of the lipase as well as the s
electivity for type of glyceride specie were studied using pure isomer
s of the the partial glycerides. The enzyme showed high selectivity fo
r triglycerides and 1-monoglycerides and very low activity towards dig
lycerides. The lipase had a clear preference for the 1- and 3-position
s. The highest lipase activity was observed at low water activity, but
the yield increased with increasing water activity. Above all, the re
gio-isomeric purity of the diglycerides increased with increasing wate
r activity. The yield of dilaurin was 75% and furthermore, 95% of the
total dilaurin was 1,2-dilaurin. Alcohol concentration and chain lengt
h of the alcohol had insignificant effect on yield and enzyme activity
, but product stability increased when alcohol was present in the reac
tion medium. The best solvents were ethers; higher enzyme activities w
ere obtained in aliphatic hydrocarbons but yields and regio-isomeric p
urities were low presumably due to acyl migration. (C) 1997 by Elsevie
r Science Inc.