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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Published in | Journal of the American Oil Chemists' Society Vol. 75; no. 6; pp. 711 - 716 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Berlin/Heidelberg
Springer-Verlag
01.06.1998
Springer Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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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. |
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Bibliography: | Q04 Q02 1997072898 |
ISSN: | 0003-021X 1558-9331 |
DOI: | 10.1007/s11746-998-0210-9 |