Bioprocess engineering to produce 10-hydroxystearic acid from oleic acid by recombinant Escherichia coli expressing the oleate hydratase gene of Stenotrophomonas maltophilia

Jeon, Eun Yeong; Lee, Jung Hoo; Yang, Kyung Mi; Joo, Young-Chul; Oh, Deok‐Kun; Park, Jin Byung

doi:10.1016/j.procbio.2012.03.002

Cited by 52 publications

(39 citation statements)

References 29 publications

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“…Oleate hydratases (EC 4.2.1.53)c onvert oleic acid (OA) into (R)-10-hydroxystearic acid (10-HSA), [1][2][3][4] ap roduct of increasing commercial interestb ecause of its potentiala pplication as as urfactant, al ubricant, an additive in the food or cosmetics industries, and as as tarting material in polymerc hemistry (Scheme 1). [5,6] Currently,t he applicabilityo fh ydratases on an industrials cale is limited primarily by their narrow substrate scope andb yr estricted informationo np rotein structure and mechanism.…”

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confidence: 99%

Structure‐Based Mechanism of Oleate Hydratase from Elizabethkingia meningoseptica

et al. 2015

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Hydratases provide access to secondary and tertiary alcohols by regio- and/or stereospecifically adding water to carbon-carbon double bonds. Thereby, hydroxy groups are introduced without the need for costly cofactor recycling, and that makes this approach highly interesting on an industrial scale. Here we present the first crystal structure of a recombinant oleate hydratase originating from Elizabethkingia meningoseptica in the presence of flavin adenine dinucleotide (FAD). A structure-based mutagenesis study targeting active site residues identified E122 and Y241 as crucial for the activation of a water molecule and for protonation of the double bond, respectively. Moreover, we also observed that two-electron reduction of FAD results in a sevenfold increase in the substrate hydration rate. We propose the first reaction mechanism for this enzyme class that explains the requirement for the flavin cofactor and the involvement of conserved amino acid residues in this regio- and stereoselective hydration.

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confidence: 99%

Structure‐Based Mechanism of Oleate Hydratase from Elizabethkingia meningoseptica

et al. 2015

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“…[18] Oleic acid will be transported into the cytoplasm via FadL in the outer membrane and subjected to hydration by OhyA into 10-hydroxyoctadecanoic acid (5). The recombinant E. coli was engineered to express not only the SADH, H3_RA and FadL, but also a fatty acid double bond hydratase (i. e., OhyA) from S. maltophilia.…”

Section: Biosynthesis Of 10-aminooctadecanoic Acid From Oleic Acidmentioning

confidence: 99%

“…The recombinant E. coli was engineered to express not only the SADH, H3_RA and FadL, but also a fatty acid double bond hydratase (i. e., OhyA) from S. maltophilia. [18] Oleic acid will be transported into the cytoplasm via FadL in the outer membrane and subjected to hydration by OhyA into 10-hydroxyoctadecanoic acid (5).…”

Section: Biosynthesis Of 10-aminooctadecanoic Acid From Oleic Acidmentioning

confidence: 99%

Enzyme Cascade Reactions for the Biosynthesis of Long Chain Aliphatic Amines from Renewable Fatty Acids

et al. 2019

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Enzyme cascade reactions for the synthesis of long chain aliphatic amines such as (Z)-12aminooctadec-9-enoic acid, 10-or 12-aminooctadecanoic acid, and 10-amino-12-hydroxyoctadecanoic acid from renewable fatty acids were investigated. (Z)-12-aminooctadec-9-enoic acid was produced from ricinoleic acid ((Z)-12-hydroxyoctadec-9-enoic acid) via (Z)-12-ketooctadec-9-enoic acid with a conversion of 71% by a two-step in vivo biotransformation involving a long chain secondary alcohol dehydrogenase (SADH) from Micrococcus luteus and a variant of the amine transaminase (ATA) from Vibrio fluvialis. 10-Aminooctadecanoic acid was prepared from oleic acid ((Z)-octadec-9-enoic acid) via 10-hydroxyoctadecanoic acid and 10-ketooctadecanoic acid by an in vivo three-step biocatalysis reaction involving not only the SADH and ATA variants, but also a fatty acid double bond hydratase (OhyA) from Stenotrophomonas maltophilia. 10-Aminooctadecanoic acid was produced at a total rate of 4.4 U/g dry cells with a conversion of 87% by recombinant Escherichia coli expressing the SADH and ATA variants, and OhyA simultaneously. In addition, bulky aliphatic amines could also be produced by the isolated enzymes (i. e., the SADH, the ATA variants, and a nicotinamide adenine dinucleotide (NADH) oxidase from Lactobacillus brevis) with methylbenzylamine or benzylamine as amino donor. This study thus contributes to the biosynthesis of long chain aliphatic amines having two large substituents next to the amine functionality.

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“…al. describe an industrially relevant E. coli whole-cell biotransformation utilizing a ∆9 hydratase from Stenotrophomonas maltophilia with a final product concentration of approximately 46 g/L and a product yield of 91% and a productivity of 8.2g/L*h in a 1 L-bioreactor scale [137]. What is more, the importance of regiospecific biocatalytic hydration as key step for the production of high-value-added products like flavors, resins, waxes, nylons, plastics, lubricants, polymers etc.…”

Section: Fatty Acid Double Bond Hydratasesmentioning

confidence: 99%

Engineering and application of enzymes for lipid modification, an update

Zorn

Oroz‐Guinea

Brundiek³

et al. 2016

Progress in Lipid Research

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This review first provides a brief introduction into the most important tools and strategies for protein engineering (i.e. directed evolution and rational protein design combined with high-throughput screening methods) followed by examples from literature, in which enzymes have been optimized for biocatalytic applications. This covers engineered lipases with altered fatty acid chain length selectivity, fatty acid specificity and improved performance in esterification reactions. Furthermore, recent achievements reported for phospholipases, lipoxygenases, P450 monooxygenases, decarboxylating enzymes, fatty acid hydratases and the use of enzymes in cascade reactions are treated.

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Bioprocess engineering to produce 10-hydroxystearic acid from oleic acid by recombinant Escherichia coli expressing the oleate hydratase gene of Stenotrophomonas maltophilia

Cited by 52 publications

References 29 publications

Structure‐Based Mechanism of Oleate Hydratase from Elizabethkingia meningoseptica

Structure‐Based Mechanism of Oleate Hydratase from Elizabethkingia meningoseptica

Enzyme Cascade Reactions for the Biosynthesis of Long Chain Aliphatic Amines from Renewable Fatty Acids

Engineering and application of enzymes for lipid modification, an update

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