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Production of specific‐structured lipids by enzymatic interesterification: Elucidation of acyl migration by response surface design
Author(s) -
Xu X.,
Skands A. R. H.,
Høy C. E.,
Mu H.,
Balchen S.,
AdlerNissen J.
Publication year - 1998
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/s11746-998-0132-6
Subject(s) - interesterified fat , lipase , chemistry , rhizomucor miehei , substrate (aquarium) , response surface methodology , catalysis , enzyme , chromatography , organic chemistry , triacylglycerol lipase , biology , ecology
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 byproducts. 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 ( R 2 ) of the model were 0.996 and 0.981 for Q 2 value. The results show that the fitted quadratic model satisfactorily expresses acyl migration for the enzymatic interesterification in the batch reactor used.