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Interesterification of butterfat by commercial microbial lipases in a cosurfactant‐free microemulsion system
Author(s) -
Safari M.,
Kermasha S.
Publication year - 1994
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02542263
Subject(s) - interesterified fat , butterfat , lipase , chemistry , stereospecificity , hydrolysis , organic chemistry , rhizomucor miehei , chromatography , triacylglycerol lipase , enzyme , milk fat , catalysis , linseed oil
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 of rac ‐1,2‐diacylglycerols by Grignard degradation, synthesis of rac ‐phosphatidylcholines and a stereospecific release of sn ‐1,2 diacylglycerols by phospholipase A 2 . 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∶1 cis Δ 9 at the sn ‐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.