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Interesterification of Olive Oil with a Fully Hydrogenated Fat in a Batch Reactor Using Step Changes in Temperature
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...
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Published in: | Journal of agricultural and food chemistry 2008-07, Vol.56 (14), p.5942-5946 |
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Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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 °C for 48 h. For trials in which a temperature of 70 °C was used for the first 4 h of reaction and a temperature of 60 °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 °C had melting points higher than 60 °C, whereas an oil produced by interesterification at 70 °C for only 4 h had a melting point of 58 °C. There was little difference (p < 0.05) between the SFC profiles of the interesterification products prepared by two different temperature protocols (70 °C for 24 h; 70 °C for 4 h followed by 60 °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. |
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ISSN: | 0021-8561 1520-5118 |
DOI: | 10.1021/jf8007585 |