Characterization of the linoleic acid Δ9 hydratase catalyzing the first step of polyunsaturated fatty acid saturation metabolism in Lactobacillus plantarum AKU 1009a

Takeuchi, Mitsuaki; Kishino, Shigenobu; Hirata, Akiko; Park, Si‐Bum; Kitamura, Nahoko; Ogawa, Jun

doi:10.1016/j.jbiosc.2014.10.022

Cited by 55 publications

(66 citation statements)

References 32 publications

(25 reference statements)

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“…It was distinct from that of the 13-hydroxy-cis -9-octadecenoic acid produced by L. acidophilus IFO 13951, which had the ( S )-confi guration ( 14 ). The 10-hydroxy-cis -12-octadecenoic acid produced by FA-HY2 has the ( S )-confi guration (data not shown), which is the same as that of the 10-hydroxy-cis -12-octadecenoic acid produced by CLA-HY ( 12 ).…”

Section: Discussionmentioning

confidence: 79%

“…The MCRA protein family is highly conserved among different bacterial species, including gram-positive and gram-negative bacteria, and some of them have FA hydratase activity ( 12,13,(16)(17)(18)(19)28 ).…”

Section: Discussionmentioning

confidence: 99%

“…However, the hydratase responsible for the conversion of LA to 13-hydroxycis -9-octadecenoic acid has not yet been identifi ed, and the physiological activities of 13-hydroxy-cis -9-octadecenoic acid are unclear. As for the known bacterial hydratases, the length of the carbon chain in the substrate FA is limited to C16 and C18 ( 1,12,13,(16)(17)(18)(19).…”

Section: Lipid Analysesmentioning

confidence: 99%

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A novel unsaturated fatty acid hydratase toward C16 to C22 fatty acids from Lactobacillus acidophilus

Hirata

Kishino

Park

et al. 2015

Journal of Lipid Research

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This article is available online at http://www.jlr.org revealed that the metabolites of LA, 10-hydroxy-cis -12-octadecenoic acid and 13-hydroxy-cis -9-octadecenoic acid, were detected at higher levels in the intestines of specifi c pathogen-free (SPF) mice than in those of germ-free mice, indicating that gastrointestinal microbes play a role in modifying the FA profi le of their host mice.The physiological functions of 10-hydroxy FAs and their derivatives begin to become clear. 10-Hydroxy-cis -12-octadecenoic acid ameliorates intestinal epithelial barrier impairment via the G protein-coupled receptor 40 (GPR40)-MAPK/ERK kinase (MEK)-ERK pathway and may be useful in the treatment of tight junction-related disorders such as infl ammatory bowel disease ( 3 ). 10-Oxo-cis -12-octadecenoic acid potently activates PPAR ␥ , a master regulator of adipocyte differentiation, and may be involved in the regulation of host energy metabolism ( 5 ).The production of 10-hydroxy-cis -12-octadecenoic acid from LA has been reported in many bacteria, including Lactobacillus acidophilus ( 7 ), L. plantarum ( 8, 9 ), Streptococcus bovis ( 10 ), and Stenotrophomonas nitritireducens ( 11 ). In our previous study, we reported that the enzyme linoleic acid hydratase (CLA-HY) from L. plantarum AKU 1009a catalyzes the hydration of the cis -9 double bond in C16 and C18 FAs, forming the corresponding 10-hydroxy FAs ( 12 ). Volkov et al. ( 13 ) reported that SPH, a hydratase from Streptococcus pyogenes M49, is a myosin-cross-reactive antigen (MCRA) family protein that catalyzes the hydration of the cis-9 and cis -12 double bonds in C16 and C18 FAs, forming the corresponding 10-hydroxy and 10,13-dihydroxy FAs.The production of 13-hydroxy-cis -9-octadecenoic acid from LA has also been reported in some anaerobic bacteria. Hudson et al. ( 10 ) reported that a ruminant bacterium, S. bovis JB1, converts LA into 13-hydroxy-cis -9-octadecenoic acid, and Kishimoto et al. ( 14 ) reported that L. acidophilus Abstract Hydroxy FAs, one of the gut microbial metabolites of PUFAs, have attracted much attention because of their various bioactivities. The purpose of this study was to identify lactic acid bacteria with the ability to convert linoleic acid (LA) to hydroxy FAs. A screening process revealed that a gut bacterium, Lactobacillus acidophilus NTV001, converts LA mainly into 13-hydroxy-cis -9-octadecenoic acid and resulted in the identifi cation of the hydratase responsible, fatty acid hydratase 1 (FA-HY1) . Recombinant FA-HY1 was purifi ed, and its enzymatic characteristics were investigated. FA-HY1 could convert not only C18 PUFAs but also C20 and C22 PUFAs. C18 PUFAs with a cis carbon-carbon double bond at the ⌬ 12 position were converted into the corresponding 13-hydroxy FAs. Arachidonic acid and DHA were converted into the corresponding 15-hydroxy FA and 14-hydroxy FA, respectively. To the best of our knowledge, this is the fi rst report of a bacterial FA hydratase that can convert C20 and C22 PUFAs into the corresponding hydroxy FAs. These novel ...

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Section: Discussionmentioning

confidence: 79%

Section: Discussionmentioning

confidence: 99%

Section: Lipid Analysesmentioning

confidence: 99%

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A novel unsaturated fatty acid hydratase toward C16 to C22 fatty acids from Lactobacillus acidophilus

Hirata

Kishino

Park

et al. 2015

Journal of Lipid Research

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“…We investigated the improved hydration activity of holo-OhyA1 with FAD and NADH together. The hydration activity of linoleate hydratase from Lactobacillus plantarum also increased significantly upon addition of FAD supplemented with NADH (20). Some oxidative enzymes, such as 2-haloacrylate hydratase (21) and 2-hydroxybiphenyl 3-monooxygenase (22), showed similar results for FAD supplemented with NADH.…”

Section: Discussionmentioning

confidence: 90%

Comparison of Biochemical Properties of the Original and Newly Identified Oleate Hydratases from Stenotrophomonas maltophilia

Kang

Seo

Shin

et al. 2017

Appl Environ Microbiol

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Oleate hydratases (OhyAs) catalyze the conversion of unsaturated fatty acids to 10-hydroxy fatty acids, which are used as precursors of important industrial compounds, including lactones and -hydroxycarboxylic and ␣, -dicarboxylic acids. The genes encoding OhyA and a putative fatty acid hydratase in Stenotrophomonas maltophilia were identified by genomic analysis. The putative fatty acid hydratase was purified and identified as an oleate hydratase (OhyA2) based on its substrate specificity. The activity of OhyA2 as a holoenzyme was not affected by adding cofactors, whereas the activity of the original oleate hydratase (OhyA1) showed an increase. Thus, all characterized OhyAs were categorized as either OhyA1 or OhyA2 based on the activities of holoenzymes upon adding cofactors, which were determined by the type of the fourth conserved amino acid of flavin adenine dinucleotide (FAD)-binding motif. The hydration activities of S. maltophilia OhyA2 toward unsaturated fatty acids, including oleic acid, palmitoleic acid, linoleic acid, ␣-linolenic acid, and ␥-linolenic acid, were greater than those of OhyA1. Moreover, the specific activity of S. maltophilia OhyA2 toward unsaturated fatty acids, with the exception of ␥-linolenic acid, was the highest among all reported OhyAs. IMPORTANCE All characterized OhyAs were categorized as OhyA1s or OhyA2s based on the different properties of the reported and newly identified holo-OhyAs in S. maltophilia upon the addition of cofactors. OhyA2s showed higher activities toward polyunsaturated fatty acids (PUFAs), including linoleic acid, ␣-linolenic acid, and ␥-linolenic acid, than those of OhyA1s. This suggests that OhyA2s can be used more effectively to convert plant oils to 10-hydroxy fatty acids because plant oils contain not only oleic acid but also PUFAs. The hydration activity of the newly identified OhyA2 from S. maltophilia toward oleic acid was the highest among the activity levels reported so far. Therefore, this enzyme is an efficient biocatalyst for the conversion of plant oils to 10-hydroxy fatty acids, which can be further converted to important industrial materials. KEYWORDS Stenotrophomonas maltophilia, enzyme characterization, oleate hydrataseO leate hydratase (OhyA) converts unsaturated fatty acids to 10-hydroxy fatty acids, which are then converted to ␥-lactones by the yeasts Candida boidinii and Waltomyces lipofer (1, 2). ␥-Lactones are flavor compounds used in food and cosmetics (3). Multistep enzymatic reactions involving OhyA, alcohol dehydrogenase, Baeyer-Villiger monooxygenases, and esterase convert unsaturated fatty acids to -hydroxycarboxylic and ␣, -dicarboxylic acids (4), which are used in the preparation of resins, nylons, plastics, and lubricants (5). An effective OhyA is necessary for the efficient production of ␥-lactones, -hydroxycarboxylic acids, and ␣, -dicarboxylic acids.

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“…7) The saturation metabolism consists of four enzymes: CLA-HY (unsaturated fatty acid hydratase), CLA-DH (hydroxy fatty acid dehydrogenase), CLA-DC (isomerase), and CLA-ER (enone reductase). [8][9][10][11] This strain produces cis-9,trans-11-conjugated linoleic acid (CLA) and trans-9,trans-11-CLA as byproducts during the saturation of linoleic acid (LA) to oleic acid (OA). [12][13][14] The application of these enzymes enables us to produce intermediate fatty acids such as 10-hydroxy-cis-12-octadecenoic acid (HYA), 10-hydroxyoctadecanoic acid (HYB), 10-oxo-cis-12-octadecenoic acid (KetoA), and 10-oxooctadecanoic acid (KetoB) from LA.…”

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confidence: 99%

Production of dicarboxylic acids from novel unsaturated fatty acids by laccase-catalyzed oxidative cleavage

Takeuchi

Kishino

Park

et al. 2016

Bioscience, Biotechnology, and Biochemistry

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The establishment of renewable biofuel and chemical production is desirable because of global warming and the exhaustion of petroleum reserves. Sebacic acid (decanedioic acid), the material of 6,10-nylon, is produced from ricinoleic acid, a carbon-neutral material, but the process is not eco-friendly because of its energy requirements. Laccase-catalyzing oxidative cleavage of fatty acid was applied to the production of dicarboxylic acids using hydroxy and oxo fatty acids involved in the saturation metabolism of unsaturated fatty acids in Lactobacillus plantarum as substrates. Hydroxy or oxo fatty acids with a functional group near the carbon-carbon double bond were cleaved at the carbon-carbon double bond, hydroxy group, or carbonyl group by laccase and transformed into dicarboxylic acids. After 8 h, 0.58 mM of sebacic acid was produced from 1.6 mM of 10-oxo-cis-12,cis-15-octadecadienoic acid (αKetoA) with a conversion rate of 35% (mol/mol). This laccase-catalyzed enzymatic process is a promising method to produce dicarboxylic acids from biomass-derived fatty acids.

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Characterization of the linoleic acid Δ9 hydratase catalyzing the first step of polyunsaturated fatty acid saturation metabolism in Lactobacillus plantarum AKU 1009a

Cited by 55 publications

References 32 publications

A novel unsaturated fatty acid hydratase toward C16 to C22 fatty acids from Lactobacillus acidophilus

A novel unsaturated fatty acid hydratase toward C16 to C22 fatty acids from Lactobacillus acidophilus

Comparison of Biochemical Properties of the Original and Newly Identified Oleate Hydratases from Stenotrophomonas maltophilia

Production of dicarboxylic acids from novel unsaturated fatty acids by laccase-catalyzed oxidative cleavage

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