Interesterification of Olive Oil with a Fully Hydrogenated Fat in a Batch Reactor Using Step Changes in Temperature

Abstract

Interesterification of a 60:40 (wt/wt) mixture of olive oil and fully hydrogenated canola oil was carried out in a batch reactor using a commercial immobilized lipase from Thermomyces lanuginose as a biocatalyst. The effects of a stepwise change of temperature on the degree of conversion, the solid fat content (SFC) of the products, and the residual activity of the enzyme were investigated. As a reference condition, an interesterification trial was conducted at a constant temperature of 70 degrees C for 48 h. For trials in which a temperature of 70 degrees C was used for the first 4 h of reaction and a temperature of 60 degrees C was employed for the following 44 h, there were no significant differences (p < 0.05) in the overall degree of conversion relative to the reference condition. Oils interesterified for only 1 or 2 h at 70 degrees C had melting points higher than 60 degrees C, whereas an oil produced by interesterification at 70 degrees C for only 4 h had a melting point of 58 degrees C. There was little difference (p < 0.05) between the SFC profiles of the interesterification products prepared by two different temperature protocols (70 degrees C for 24 h; 70 degrees C for 4 h followed by 60 degrees C for 20 h). Use of the protocol involving a step decrease in temperature significantly decreased catalyst deactivation effects, thereby increasing the residual activity of the immobilized lipase.

Lipase‐Catalyzed Interesterification in Packed Bed Reactor Using 2 Different Temperatures

“…For trials using a stepwise temperature protocol, there were no significant differences in the conversion degrees relative to those for the constant temperature (70 °C). These results were consistent with previous results obtained in a batch reaction system (Kim and others 2008). …”

“…The time course of the reaction was studied for each temperature protocol. Depletion of the primary TAG species present in the physical blends, specifically tristearin, was as a direct indicator of the extent of interesterification (Lopóz‐Hernandez and others 2007; Kim and others 2008). …”

Lipase-catalyzed acidolysis of sunflower oil: Kinetic behavior

“…It means that the added water of 50% (a w = 0.52) was high enough to maintain the liquid phase hydrated in a similar level over time even though solids adsorbed water. So, it is to remark that added water was not only in the surroundings of the enzyme, as could be the case when water was not added or when immobilized enzyme is conditioned in an atmosphere of known activity water (as other authors had analyzed (Rønne et al, 2005;Kim et al, 2008)), but also throughout the liquid phase. Glycerol was not observed during chromatographic essays, not even when water was added to the reaction media and reaction time was long enough to allow the enzyme to complete hydrolysis reaction in all three positions if it was possible.…”

Optimization of Reaction Conditions in the Enzymatic Interesterification of Soybean Oil and Fully Hydrogenated Soybean Oil to Produce Plastic Fats

“…For the enzyme concentration range selection the values considered were the most frequently used in the literature, as well as the two enzymes used [4,13]. For the factor time, 1 h was chosen as a time to evaluate the initial stage of the reaction, while 24 h was considered as a moment in which the reaction would reach the stationary state [14]. Regarding the substrates ratio, two extreme ratios were considered for screening a wide range of this variable.…”