Linoleic Acid Isomerase inLactobacillus plantarumAKU1009a Proved to Be a Multi-Component Enzyme System Requiring Oxidoreduction Cofactors
Author(s) -
Shigenobu Kishino,
Jun Ogawa,
Kenzo Yokozeki,
Sakayu Shimizu
Publication year - 2011
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.100699
Subject(s) - chemistry , cofactor , linoleic acid , isomerase , conjugated linoleic acid , enzyme , isomerization , divalent , biochemistry , catalysis , organic chemistry , fatty acid
Linoleic acid isomerase in Lactobacillus plantarum was found to be a novel multi-component enzyme system widespread in membrane and soluble fractions. The isomerization reaction involved a hydration step, 10-hydroxy-12-octadecenoic acid production from linoleic acid, as part of the reaction, and the hydration reaction was catalyzed by the membrane fraction. Both membrane and soluble fractions were required for the whole isomerization reaction, i.e., conjugated linoleic acid (CLA) production from linoleic acid, and for CLA production from 10-hydroxy-12-octadecenoic acid, a reaction intermediate. The multi-component enzyme system was inhibited by o-phenanthroline, and divalent metal ions such as Ni(2+) and Co(2+) restored activity. Metal oxides such as VO(4)(3+), MoO(4)(2+), and MnO(4)(2+) enhanced activity. The multi-component enzyme systems required oxidoreduction cofactors such as NADH together with FAD or NADPH for total activity.
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