Multi-level engineering of Baeyer-Villiger monooxygenase-based Escherichia coli biocatalysts for the production of C9 chemicals from oleic acid

Seo, Eun Ji; Kang, Changhui; Woo, Ji Min; Jang, Se Bok; Yeon, Young Joo; Jung, Gyoo Yeol; Park, Jin Byung

doi:10.1016/j.ymben.2019.03.012

Cited by 32 publications

(32 citation statements)

References 44 publications

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“…The biotransformations were conducted based on our previous reports [9,10,36,37,38]. Briefly, the recombinant cells were harvested at the stationary growth phase usually 12 h after cell cultivation by centrifugation at 4 °C.…”

Section: Methodsmentioning

confidence: 99%

“…Oils and fatty acids can be used as starting materials for the production of a variety of monomers for the polymers such as polyesters and polyamides [7,8,9,10,11,12]. For example, microbial production of ω-hydroxycarboxylic acids, α,ω-dicarboxylic acids, and ω-aminocarboxylic acids from fatty acids and fatty acid methyl esters have been reported [12,13,14,15].…”

Section: Introductionmentioning

confidence: 99%

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Multi-Step Enzymatic Synthesis of 1,9-Nonanedioic Acid from a Renewable Fatty Acid and Its Application for the Enzymatic Production of Biopolyesters

et al. 2019

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1,9-Nonanedioic acid is one of the valuable building blocks for producing polyesters and polyamides. Thereby, whole-cell biosynthesis of 1,9-nonanedioic acid from oleic acid has been investigated. A recombinant Corynebacterium glutamicum, expressing the alcohol/aldehyde dehydrogenases (ChnDE) of Acinetobacter sp. NCIMB 9871, was constructed and used for the production of 1,9-nonanedioic acid from 9-hydroxynonanoic acid, which had been produced from oleic acid. When 9-hydroxynonanoic acid was added to a concentration of 20 mM in the reaction medium, 1,9-nonanedioic acid was produced to 16 mM within 8 h by the recombinant C. glutamicum. The dicarboxylic acid was isolated via crystallization and then used for the production of biopolyester by a lipase. For instance, the polyesterification of 1,9-nonanedioic acid and 1,8-octanediol in diphenyl ether by the immobilized lipase B from Candida antarctica led to formation of the polymer product with the number-average molecular weight (Mn) of approximately 21,000. Thereby, this study will contribute to biological synthesis of long chain dicarboxylic acids and their application for the enzymatic production of long chain biopolyesters.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Multi-Step Enzymatic Synthesis of 1,9-Nonanedioic Acid from a Renewable Fatty Acid and Its Application for the Enzymatic Production of Biopolyesters

et al. 2019

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“…Co-expression of the Ohy, ADH and BVMO in E.coli resulted in an effective whole cell biocatalyst containing the whole cascade (Seo et al 2019a). By optimising the protein expression and by using an engineered BVMO, a yield of nnonanoic acid and 9-hydroxynonnoic acid of 6 mmol/g dry cells was obtained.…”

Section: Multi-step Reactions To Broaden the Product Scopementioning

confidence: 99%

Novel oleate hydratases and potential biotechnological applications

Hagedoorn

Hollmann

Hanefeld

2021

Appl Microbiol Biotechnol

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Oleate hydratase catalyses the addition of water to the CC double bond of oleic acid to produce (R)-10-hydroxystearic acid. The enzyme requires an FAD cofactor that functions to optimise the active site structure. A wide range of unsaturated fatty acids can be hydrated at the C10 and in some cases the C13 position. The substrate scope can be expanded using ‘decoy’ small carboxylic acids to convert small chain alkenes to secondary alcohols, albeit at low conversion rates. Systematic protein engineering and directed evolution to widen the substrate scope and increase the conversion rate is possible, supported by new high throughput screening assays that have been developed. Multi-enzyme cascades allow the formation of a wide range of products including keto-fatty acids, secondary alcohols, secondary amines and α,ω-dicarboxylic acids. Key points • Phylogenetically distinct oleate hydratases may exhibit mechanistic differences. • Protein engineering to improve productivity and substrate scope is possible. • Multi-enzymatic cascades greatly widen the product portfolio.

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“…Recently, an elegant route was developed by the Park group, comprising multistep enzymatic or chemoenzymatic cascade reactions, to convert ricinoleic acid, linoleic acid, and oleic acid into ω-hydroxy fatty acids. [14][15][16][17][18][19][20][21][22] PpBVMO from Pseudomonas putida KT2440 [23] and PfBVMO from Pseudomonas fluorescens DSM 50106, [24] first reported by the Bornscheuer group, were usually employed in this route. PpBVMO favored oxygen atom insertion at the higher substitution site of the asymmetric linear fatty ketone to generate a "normal" ester and the corresponding ωhydroxy fatty acid through hydrolysis.…”

mentioning

confidence: 99%

“…The specific activity of this enzyme toward 2-tridecanone (18, C 13 ) was 0.714 U mg À 1 , which was the highest among the linear ketones tested. Notably, the enzyme showed generally poor activity toward the alicyclic ketones tested, such as cyclopentanone (22), cyclohexanone (23), and cycloheptanone (24), except for cyclobutanone (21), which are usually well accepted by BVMOs, including CPMOs and CHMOs. [13,33] Based on the substrate scope determination, GsBVMO was confirmed to be more suitable for the catalysis of long-chain aliphatic keto acids and medium-chain aliphatic ketones, rather than alicyclic ketones.…”

mentioning

confidence: 99%

Discovery and Engineering of a Novel Baeyer‐Villiger Monooxygenase with High Normal Regioselectivity

et al. 2020

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Baeyer‐Villiger monooxygenases (BVMOs) are remarkable biocatalysts for the Baeyer‐Villiger oxidation of ketones to generate esters or lactones. The regioselectivity of BVMOs is essential for determining the ratio of the two regioisomeric products (“normal” and “abnormal”) when catalyzing asymmetric ketone substrates. Starting from a known normal‐preferring BVMO sequence from Pseudomonas putida KT2440 (PpBVMO), a novel BVMO from Gordonia sihwensis (GsBVMO) with higher normal regioselectivity (up to 97/3) was identified. Furthermore, protein engineering increased the specificity constant (kcat/KM) 8.9‐fold to 484 s−1 mM−1 for 10‐ketostearic acid derived from oleic acid. Consequently, by using the variant GsBVMOC308L as an efficient biocatalyst, 10‐ketostearic acid was efficiently transformed into 9‐(nonanoyloxy)nonanoic acid, with a space‐time yield of 60.5 g L−1 d−1. This study showed that the mutant with higher regioselectivity and catalytic efficiency could be applied to prepare medium‐chain ω‐hydroxy fatty acids through biotransformation of long‐chain aliphatic keto acids derived from renewable plant oils.

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Multi-level engineering of Baeyer-Villiger monooxygenase-based Escherichia coli biocatalysts for the production of C9 chemicals from oleic acid

Cited by 32 publications

References 44 publications

Multi-Step Enzymatic Synthesis of 1,9-Nonanedioic Acid from a Renewable Fatty Acid and Its Application for the Enzymatic Production of Biopolyesters

Multi-Step Enzymatic Synthesis of 1,9-Nonanedioic Acid from a Renewable Fatty Acid and Its Application for the Enzymatic Production of Biopolyesters

Novel oleate hydratases and potential biotechnological applications

Discovery and Engineering of a Novel Baeyer‐Villiger Monooxygenase with High Normal Regioselectivity

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