Abstract
Production of specific-structured lipids (SSL) by lipase-catalyzed
interesterification has been attracting more and more attention
recently. However, it was found that acyl migration occurs during
the reaction and causes the production of by-products. In this
paper, the elucidation of acyl migration by response surface
design was carried out in the Lipozyme IM (Rhizomucor
miehei)-catalyzed interesterification between rapeseed oil and
capric acid in solvent-free media. A five-factor response surface
design was used to evaluate the influence of five major factors
and their relationships. The five factors, water content, reaction
temperature, enzyme load, reaction time and substrate ratio, were
varied at three levels together with two star points. All
parameters besides substrate ratio had strong positive influences
on acyl migration, and reaction temperature was most significant.
The contour plots clearly show the interactions between the
parameters. The migration rates of different fatty acids were also
compared from three different sets of experiments during the
lipase-catalyzed reaction. The best-fitting quadratic response
surface model was determined by regression and backward
elimination. The coefficients of determination (R2) of the model
were 0.996 and 0.981 for Q2 value. The results show that the
fitted quadratic model satisfactorily expresses acyl migration for
the enzymatic interesterification in the batch reactor used.
Original language | English |
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Journal | Journal of the american oil chemists society |
Volume | 75 |
Issue number | 9 |
Pages (from-to) | 1179-1186 |
ISSN | 0003-021X |
DOIs | |
Publication status | Published - 1998 |