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Acidolysis and glyceride synthesis reactions using fatty acids with two Pseudomonas lipases having different substrate specificities

Paper ID Volume ID Publish Year Pages File Format Full-Text
22105 43254 2006 5 PDF Available
Title
Acidolysis and glyceride synthesis reactions using fatty acids with two Pseudomonas lipases having different substrate specificities
Abstract

Enzymatic acidolysis and glyceride synthesis using polyunsaturated fatty acids (PUFAs) with lipases from Pseudomonas fluorescens HU380 (HU-lipase), P. fluorescens AK102 (AK-lipase), and Candida rugosa (CR-lipase) were studied. The acidolysis of triolein with eicosapentaenoic acid (EPA) or docosahexaenoic acid (DHA) in n-hexane was evaluated with lipases immobilized on Celite 545. HU-lipase showed the highest incorporation rate at a low temperature (10°C) with either EPA or DHA as the acyl donor, and the rate decreased with increasing reaction temperature. At 45°C, the rates for EPA and DHA were 7.1 and 0.5 relative to those at 10°C, respectively. The EPA incorporation rate was even higher at a low temperature (10°C), and the DHA incorporation rate increased with decreasing temperature. Although AK-lipase showed the reverse tendency for incorporation rate, the DHA incorporation rate increased with increasing reaction temperature with both PUFAs. HU-lipase reacted well with PUFAs such as DHA, EPA, arachidonic acid (AA), mead acid (MA), and dihomo-γ-linolenic acid (DGLA) on acidolysis and glyceride synthesis. The reactivities of AK-lipase toward these PUFAs except for DGLA, i.e., MA, AA, EPA, and DHA, were low for both reactions. The unique substrate specificities of the lipases from the Pseudomonas strains will enable us to use these lipases for the modification of fats and oils containing PUFAs such as fish oil.

Keywords
acidolysis; glyceride synthesis; Pseudomonas fluorescens; unsaturated fatty acid
First Page Preview
Acidolysis and glyceride synthesis reactions using fatty acids with two Pseudomonas lipases having different substrate specificities
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 102, Issue 3, September 2006, Pages 179–183
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering