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Updated: May 31, 2026

An Assay for Measuring the Activity of Escherichia coli Inducible Lysine Decarboxyase
Published on: December 19, 2010
Linoleate isomerase activity occurs in lactic acid bacteria strains and is affected by pH and temperature
L Gorissen1, S Weckx, B Vlaeminck
1Laboratory for Animal Nutrition and Animal Product Quality, Department of Animal Production, Ghent University, Melle, Belgium.
Aims:
To investigate the ability of lactic acid bacteria (LAB) to convert linoleic acid (LA) and α-linolenic acid (α-LNA) to conjugated linoleic acid (CLA) and conjugated linolenic acid (CLNA), respectively. To assess pH and temperature influences on CLA and CLNA production by Lactobacillus sakei LMG 13558.
Methods And Results:
A screening of 48 LAB yielded one Lactobacillus curvatus, five Lactobacillus plantarum and four Lact. sakei strains displaying linoleate isomerase (LAI) activity. CLNA conversion percentages varied largely (1-60%). CLA conversion, occurring in three strains, was lower (2-5%). The LAI gene sequences of the ten LAI-positive strains shared 75-99% identity with the LAI gene sequence of a Lact. plantarum AS1.555. At pH 6.2, CLA and CLNA production by Lact. sakei LMG 13558 was higher at 30°C than at 20 and 25°C. At pH 5.5 (30°C) or 37°C (pH 6.2), LA was not converted and α-LNA only slightly converted.
Conclusions:
LAB show strain-dependent LAI activity. Production of CLA and CLNA is affected by pH and temperature, as shown for Lact. sakei LMG 13558.
Significance And Impact Of The Study:
Several LAB produce CLA and/or CLNA, as shown for Lact. sakei and Lact. curvatus for the first time. These findings offer potential for the manufacturing of fermented functional foods.
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