Detailed Information

Cited 0 time in webofscience Cited 0 time in scopus
Metadata Downloads

Interesterification of olive oil with a fully hydrogenated fat in a batch reactor using step changes in temperature

Authors
Kim, In-HwanLee, Sun-MiLee, Bo-MiPark, Hye-KyungKim, Jee-YoungKwon, Kwang-IlKim, Jong-WookLee, Jee-SunKim, 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.
Files in This Item
There are no files associated with this item.
Appears in
Collections
College of Health Sciences > School of Biosystems and Biomedical Sciences > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Related Researcher

Researcher Kim, In Hwan photo

Kim, In Hwan
College of Health Sciences (School of Biosystems and Biomedical Sciences)
Read more

Altmetrics

Total Views & Downloads

BROWSE