Production of ω-hydroxyundec-9-enoic acid and n-heptanoic acid from ricinoleic acid by recombinant Escherichia coli-based biocatalyst

Jang, Hyun-Young; Jeon, Eun-Yeong; Baek, A-Hyung; Lee, Sun-Mee; Park, Jin Byung

doi:10.1016/j.procbio.2014.01.025

Cited by 48 publications

(43 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several examples were published by the group of Park (Song et al 2013). They focused on the use of renewable starting materials like fat or fatty acids (14) (γ-linolenic acid , ricinoleic acid (Jang et al 2014), linoleic acid ) and applied artificial enzymatic cascades in vivo for the production of flavors, antifungal agents, plastics, waxes, nylons, and secondary metabolites. In general, they combined a hydratase for the introduction of an alcohol group with an alcohol dehydrogenase (ADH) to produce the corresponding ketone (16).…”

Section: Bvmos Applied In Cascade Type Reactionsmentioning

confidence: 99%

Baeyer-Villiger oxidations: biotechnological approach

Bučko

Gemeiner

Schenkmayerová

et al. 2016

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Baeyer-Villiger monooxygenases (BVMOs) are a very well-known and intensively studied class of flavin-dependent enzymes. Their substrate promiscuity, high chemo-, regio-, and enantioselectivity are prerequisites for the use in synthetic chemistry and should pave the way for successful industrial processes. Nonetheless, only a very limited number of industrial relevant transformations are known, mainly due to the lack of BVMOs stability and cofactor dependency. In this review, we focus on novel BVMO-mediated transformations, BVMOs in cascade type reactions, potential industrial applications, and how limitations have been tackled by the community. Special attention will be put on whole-cell immobilization strategies. We emphasize to bridge recent developments in fundamental research to industrial applications.

show abstract

Section: Bvmos Applied In Cascade Type Reactionsmentioning

confidence: 99%

Baeyer-Villiger oxidations: biotechnological approach

Bučko

Gemeiner

Schenkmayerová

et al. 2016

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…Although each MCS was preceded by its own T7 promoter and followed by a single terminator, the number of moles of the two expressed enzymes was not similar in the Duo strains, the ratio barely reaching 0.3 (in moles of monomer). This unbalanced enzyme production in favor of ADH has been previously observed in other ADH−BVMO cascades (Jang, Jeon, Baek, Lee, & Park, 2014;Müller et al, 2014) and may be due to the different size of the two enzymes, making the longer one more difficult to synthesize (Fernandes et al, 2017).…”

Section: The Effect Of Plasmid Combination On Enzyme Productionmentioning

confidence: 55%

Tuning of the enzyme ratio in a neutral redox convergent cascade: A key approach for an efficient one‐pot/two‐step biocatalytic whole‐cell system

Ménil

Petit

Courvoisier-Dezord

et al. 2019

Biotech & Bioengineering

View full text Add to dashboard Cite

The efficiency of a versatile in vivo cascade involving a promiscuous alcohol dehydrogenase, obtained from a biodiversity search, and a Baeyer–Villiger monooxygenase was enhanced by the independent control of the production level of each enzyme to produce ε‐caprolactone and 3,4‐dihydrocoumarin. This goal was achieved by adjusting the copy number per cell of Escherichia coli plasmids. We started from the observation that this number generally correlates with the amount of produced enzyme and demonstrated that an in vivo multi‐enzymatic system can be improved by the judicious choice of plasmid, the lower activity of the enzyme that drives the limiting step being counter‐balanced by a higher concentration. Using a preconception‐free approach to the choice of the plasmid type, we observed positive and negative synergetic effects, sometimes unexpected and depending on the enzyme and plasmid combinations. Experimental optimization of the culture conditions allowed us to obtain the complete conversion of cyclohexanol (16 mM) and 1‐indanol (7.5 mM) at a 0.5‐L scale. The yield for the conversion of cyclohexanol was 80% (0.7 g ε‐caprolactone, for the productivity of 244 mg·L −1·h −1) and that for 1‐indanol 60% (0.3 g 3,4‐dihydrocoumarin, for the productivity of 140 mg·L −1·h −1).

show abstract

“…Therefore, pACYC was considered as an appropriate vector to express the linoleate 13-hydratase by proper expression control. This vector has been used in the expression of many hydroxylases and oxygenases expression (Dong et al, 2013;Jang et al, 2014;Liu et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

“…Recombinant cells harboring pAhyd plasmid were cultivated in SOC medium at 37 • C, and IPTG was added at 2 h, corresponding to 0.6-0.8 of the optical density at 600 nm of the bacterial culture because IPTG addition at this optical density had been previously used for the effective expression of the pACYC plasmid (Dong et al, 2013;Jang et al, 2014;Liu et al, 2014). To determine the optimal IPTG concentration, IPTG concentrations ranging from 0.1 mM to 2 mM IPTG were added at 2 h, and the culture was incubated at 16 • C for a further 18 h (Fig.…”

Section: Optimization Of Induction Conditions For Maximizing the Exprmentioning

confidence: 99%

Production of 13S-hydroxy-9(Z)-octadecenoic acid from linoleic acid by whole recombinant cells expressing linoleate 13-hydratase from Lactobacillus acidophilus

Park

Lee

Kim

et al. 2015

Journal of Biotechnology

Self Cite

View full text Add to dashboard Cite

Production of ω-hydroxyundec-9-enoic acid and n-heptanoic acid from ricinoleic acid by recombinant Escherichia coli-based biocatalyst

Cited by 48 publications

References 22 publications

Baeyer-Villiger oxidations: biotechnological approach

Baeyer-Villiger oxidations: biotechnological approach

Tuning of the enzyme ratio in a neutral redox convergent cascade: A key approach for an efficient one‐pot/two‐step biocatalytic whole‐cell system

Production of 13S-hydroxy-9(Z)-octadecenoic acid from linoleic acid by whole recombinant cells expressing linoleate 13-hydratase from Lactobacillus acidophilus

Contact Info

Product

Resources

About