Interesterification of olive oil with a fully hydrogenated fat in a batch reactor using step changes in temperature
- Authors
- Kim, In-Hwan; Lee, Sun-Mi; Lee, Bo-Mi; Park, Hye-Kyung; Kim, Jee-Young; Kwon, Kwang-Il; Kim, Jong-Wook; Lee, Jee-Sun; Kim, Yang-Ha
- Issue Date
- 23-Jul-2008
- Publisher
- AMER CHEMICAL SOC
- Keywords
- fully hydrogenated canola oil; interesterfication; lipase; melting point; olive oil; residual activity; solid fat content
- Citation
- JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, v.56, no.14, pp.5942 - 5946
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
- Volume
- 56
- Number
- 14
- Start Page
- 5942
- End Page
- 5946
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/123013
- DOI
- 10.1021/jf8007585
- ISSN
- 0021-8561
- 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.
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Collections - College of Health Sciences > School of Biosystems and Biomedical Sciences > 1. Journal Articles
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