Production of bioactive conjugated linoleic acid by the multifunctional enolase from Lactobacillus plantarum
Por:
Ortega-Anaya, Joana, Hernandez-Santoyo, Alejandra
Publicada:
1 oct 2016
Resumen:
Lactobacillus plantarum alpha-enolase, a
multifunctional-anchorless-surface protein belonging to the conserved
family of enolases with a central role in glycolytic metabolism, was
characterized to have a side role in the intricate metabolism of
biohydrogenation of linoleic acid, catalyzing the formation of bioactive
9-cis-11-trans-CLA through dehydration and isomerization of
10-hydroxy-12-cis-octadecenoic acid. The identity of the enolase was
confirmed through mass spectrometric analysis that showed the
characteristic 442 amino acid sequence with a molecular mass of 48.03
kDa. The enolase was not capable of using linoleic acid directly as a
substrate but instead uses its hydroxyl derivative
10-hydroxi-12-cis-octadecenoic acid to finally form bioactive conjugated
linoleic acid. Biochemical optimization studies were carried out to
elucidate the conditions for maximum production of 9-cis-11-trans-CLA
and maximum stability of alpha-enolase when catalyzing this reaction.
Furthermore, through structural analysis of the protein, we propose the
binding sites of substrate and product molecules that were characterized
as two hydrophobic superficial pockets located at opposite ends of the
enolase connected through a channel where the catalysis of dehydration
and isomerization might occur. These results prove that multifunctional
alpha-enolase also plays a role in cell detoxification from
polyunsaturated fatty acids such as linoleic acid, along with the
linoleate isomerase complex. (C) 2016 Elsevier B.V. All rights reserved.
Filiaciones:
Ortega-Anaya, Joana:
Univ Nacl Autonoma Mexico, Inst Quim, Dept Quim Biomacromol, Circuito Exterior, Ciudad Univ, Coyoacan 04510, Mexico
Hernandez-Santoyo, Alejandra:
Univ Nacl Autonoma Mexico, Inst Quim, Dept Quim Biomacromol, Circuito Exterior, Ciudad Univ, Coyoacan 04510, Mexico
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