Triglyceride interesterification by lipases. 3. Alcoholysis of pure triglycerides
Kanasawud, Pawinee ; Phutrakul, Suree ; Bloomer, Scott ; Adlercreutz, Patrick LU
and Mattiasson, Bo
LU
(1992)
In Enzyme and Microbial Technology
14(12).
p.959-965
- Abstract
Lipase-catalyzed alcoholysis of triolein dissolved in ethanol or isopropanol for the formation of ethyl and isopropyl esters was investigated. Of 16 lipases screened, Amano lipase from P. fluorescens was selected for investigation of the effects of basic reaction conditions on alcoholysis yields. Ethanolysis yields were only slightly affected by water additions to immobilized lipase preparations. Isopropyl ester yields decreased with water addition. Good operational stability was observed over 17 days. Changes in initial triolein concentration in the range 5-50 mM had very little effect on ester yields. The ionic strength of the phosphate buffer used in lipase immobilization affected ethanolysis and isopropanolysis yields in opposite... (More)
Lipase-catalyzed alcoholysis of triolein dissolved in ethanol or isopropanol for the formation of ethyl and isopropyl esters was investigated. Of 16 lipases screened, Amano lipase from P. fluorescens was selected for investigation of the effects of basic reaction conditions on alcoholysis yields. Ethanolysis yields were only slightly affected by water additions to immobilized lipase preparations. Isopropyl ester yields decreased with water addition. Good operational stability was observed over 17 days. Changes in initial triolein concentration in the range 5-50 mM had very little effect on ester yields. The ionic strength of the phosphate buffer used in lipase immobilization affected ethanolysis and isopropanolysis yields in opposite ways. The highest ethanolysis yields were obtained with lipases immobilized from 250 mM buffer, while isopropyl ester yields were highest with lipases immobilized from water. In addition, the quantities and isomers of monoglyceride intermediates in ethanolysis were affected by the immobilization buffer strength. Larger quantities of 2-monoglycerides were formed in ethanolysis reactions with lipase preparations immobilized from water.
(Less)
- author
- Kanasawud, Pawinee
; Phutrakul, Suree
; Bloomer, Scott
; Adlercreutz, Patrick
LU
and Mattiasson, Bo
LU
- organization
- publishing date
- 1992-01-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- alcoholysis, immobilized enzymes, interesterification, lipase, monoglycerides, operational stability
- in
- Enzyme and Microbial Technology
- volume
- 14
- issue
- 12
- pages
- 7 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:0027006836
- ISSN
- 0141-0229
- DOI
- 10.1016/0141-0229(92)90078-3
- language
- English
- LU publication?
- yes
- id
- 94c526b5-ee45-4181-8522-cdda430f30b5
- date added to LUP
- 2019-06-22 09:26:25
- date last changed
- 2025-04-04 14:31:22
@article{94c526b5-ee45-4181-8522-cdda430f30b5,
abstract = {{<p>Lipase-catalyzed alcoholysis of triolein dissolved in ethanol or isopropanol for the formation of ethyl and isopropyl esters was investigated. Of 16 lipases screened, Amano lipase from P. fluorescens was selected for investigation of the effects of basic reaction conditions on alcoholysis yields. Ethanolysis yields were only slightly affected by water additions to immobilized lipase preparations. Isopropyl ester yields decreased with water addition. Good operational stability was observed over 17 days. Changes in initial triolein concentration in the range 5-50 mM had very little effect on ester yields. The ionic strength of the phosphate buffer used in lipase immobilization affected ethanolysis and isopropanolysis yields in opposite ways. The highest ethanolysis yields were obtained with lipases immobilized from 250 mM buffer, while isopropyl ester yields were highest with lipases immobilized from water. In addition, the quantities and isomers of monoglyceride intermediates in ethanolysis were affected by the immobilization buffer strength. Larger quantities of 2-monoglycerides were formed in ethanolysis reactions with lipase preparations immobilized from water.</p>}},
author = {{Kanasawud, Pawinee and Phutrakul, Suree and Bloomer, Scott and Adlercreutz, Patrick and Mattiasson, Bo}},
issn = {{0141-0229}},
keywords = {{alcoholysis; immobilized enzymes; interesterification; lipase; monoglycerides; operational stability}},
language = {{eng}},
month = {{01}},
number = {{12}},
pages = {{959--965}},
publisher = {{Elsevier}},
series = {{Enzyme and Microbial Technology}},
title = {{Triglyceride interesterification by lipases. 3. Alcoholysis of pure triglycerides}},
url = {{http://dx.doi.org/10.1016/0141-0229(92)90078-3}},
doi = {{10.1016/0141-0229(92)90078-3}},
volume = {{14}},
year = {{1992}},
}