Enzymatic interesterification of triolein and tristearin: chemical structure and differential scanning calorimetric analysis of the products

The structural composition and thermal properties of the products of enzymatic interesterification of triolein and tristearin were investigated. The biocatalyst for the reaction was an immobilized Candida antarctica lipase, SP435. Enzyme load of 10% (w/w reactants) produced 72% of desired total prod...

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Bibliographic Details
Published inJournal of the American Oil Chemists' Society Vol. 75; no. 6; pp. 711 - 716
Main Authors Seriburi, V, Akoh, C.C
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Springer-Verlag 01.06.1998
Springer
Springer Nature B.V
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Summary:The structural composition and thermal properties of the products of enzymatic interesterification of triolein and tristearin were investigated. The biocatalyst for the reaction was an immobilized Candida antarctica lipase, SP435. Enzyme load of 10% (w/w reactants) produced 72% of desired total products. Oleoyl‐distearoyl triglycerides (SSO, OSS) had higher melting points than dioleoyl‐stearoyl triglycerides (OOS, SOO) because the sample contained larger amounts of stearic acid than oleic acid residues. SOS and OSO were hardly produced (0.2 to 1.2%), which indicates that SP435 acted as a nonspecific lipase when catalyzing the interesterification of triolein and tristearin. The maximal yield of OSS and SSO (46.9%) was achieved with a 1.2 mole ratio of triolein to tristearin. As the proportion of tristearin was increased, the production of SOO and OOS decreased, the melting profile of the interesterified triglycerides shifted toward higher melting forms, and the solid fat content increased, indicating formation of hard fats.
Bibliography:Q04
Q02
1997072898
ISSN:0003-021X
1558-9331
DOI:10.1007/s11746-998-0210-9