Interesterification of butterfat by commercial microbial lipases in a cosurfactant‐free microemulsion system

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Abstract
Lipase‐catalyzed interesterification of butterfat was carried out in a cosurfactant‐free microemulsion system containing mixtures of Span 60 and Tween 60 (ICI Specialty Chemicals Altemix Inc., Brantford, Ontario, Canada) as surfactants. Four commercial lipases were used—Lipozyme 10,000L (Novo Nordisk, Copenhagen, Denmark) and N, D and MPA (Amano Pharmaceutical Co. Ltd., Nagoya, Japan). Stereospecific analyses of fractionated selected high‐molecular weight triacylglycerols were performed by enzymatic deacylation with commercial pancreatic lipase, random generation ofrac‐1,2‐diacylglycerols by Grignard degradation, synthesis ofrac‐phosphatidylcholines and a stereospecific release ofsn‐1,2 diacylglycerols by phospholipase A2. The results showed that the hydrolytic affinity of commercial lipases demonstrated an acyl‐group specificity toward lower‐molecular weight fatty acids C4–C14∶0. Stereospecific analyses of fatty acids of interesterified selected triacylglycerols of butterfat catalyzed by lipase N demonstrated a 46% increase in the proportion of C18∶1cis Δ9 at thesn‐2 position, whereas those catalyzed by lipases MAP, D and Lipozyme 10,000L were enriched with C16∶0 at the same position by 21, 35 and 41%, respectively.