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

Kwon

Choi

et al. 2022

J. Agric. Food Chem.

A huge amount of phospholipids or lecithin is produced as a byproduct in the vegetable oil industry. However, most are just used as a feed additive. This study has focused on enzymatic valorization of lecithin. This was exploited by enzymatic transformation of soy lecithin into lysolecithin liposomes, including functional free fatty acids, hydroxy fatty acids, hydrocarbons, or secondary fatty alcohols. One of the representative examples was the preparation of lysolecithin liposomes containing secondary fatty alcohols [e.g., 9-Hydroxyheptadec-11-ene (9) and 9-heptadecanol (10)] by using a phospholipase A2 from Streptomyces violaceoruber, a fatty acid double-bond hydratase from Stenotrophomonas maltophilia, and a photoactivated decarboxylase from Chlorella variabilis NC64A. The engineered liposomes turned out to range ca. 144 nm in diameter by dynamic light scattering analysis. Thereby, this study will contribute to application of functional fatty acids and their derivatives as well as valorization of lecithin for the food and cosmetic industries.

“…coli BL21 star (DE3) pET28a- Sm-OhyA2 to a cell density of 7.2 g dry cells/L into the reaction medium. The agitation and reaction temperature were 400 rpm and 35 °C. , …”

Section: Methodsmentioning

confidence: 99%

Valorization of Soy Lecithin by Enzyme Cascade Reactions Including a Phospholipase A2, a Fatty Acid Double-Bond Hydratase, and/or a Photoactivated Decarboxylase

Kwon

Choi

et al. 2022

J. Agric. Food Chem.

“…Generally, the log P, which is a qualitative parameter, can be used to determine the impact of solvents on catalytic activity. Solvents with low log p values are hydrophilic that exhibit enzyme inhibition, whereas solvents with high log p values are hydrophobic solvents, which favor highly active enzymes in nonpolar compounds [ 119 ]. Despite the fact that polar solvents contribute to the solubility of some monomers, their hydrophilic character may lead to the loss of the hydrated layer of the enzyme, which can result in its inactivation or denaturation, hence reducing its catalytic activity [ 120 ].…”

Section: Solvent System For Enzyme-catalyzed Synthesis Of Polyestersmentioning

confidence: 99%

Recent Advances in the Enzymatic Synthesis of Polyester

Wang

Liu²,

et al. 2022

Polymers

Polyester is a kind of polymer composed of ester bond-linked polybasic acids and polyol. This type of polymer has a wide range of applications in various industries, such as automotive, furniture, coatings, packaging, and biomedical. The traditional process of synthesizing polyester mainly uses metal catalyst polymerization under high-temperature. This condition may have problems with metal residue and undesired side reactions. As an alternative, enzyme-catalyzed polymerization is evolving rapidly due to the metal-free residue, satisfactory biocompatibility, and mild reaction conditions. This article presented the reaction modes of enzyme-catalyzed ring-opening polymerization and enzyme-catalyzed polycondensation and their combinations, respectively. In addition, the article also summarized how lipase-catalyzed the polymerization of polyester, which includes (i) the distinctive features of lipase, (ⅱ) the lipase-catalyzed polymerization and its mechanism, and (ⅲ) the lipase stability under organic solvent and high-temperature conditions. In addition, this article also focused on the advantages and disadvantages of enzyme-catalyzed polyester synthesis under different solvent systems, including organic solvent systems, solvent-free systems, and green solvent systems. The challenges of enzyme optimization and process equipment innovation for further industrialization of enzyme-catalyzed polyester synthesis were also discussed in this article.

“…To increase the production of 8–16 α,ω‐dicarboxylic acids from ω‐hydroxycarboxylic acids, aldehyde dehydrogenase (ALDH), and NAD(P)H oxidase (NOX), including NAD(P)H flavin oxidoreductase (NFO), have been introduced into the cells expressing ADH to enhance the oxidization activity of ADH for ω‐hydroxycarboxylic acids and regenerate NAD(P) + as a co‐factor for ADH and ALDH reactions (Kang et al, 2020; Kim, Kang, Park, et al, 2020; Lee et al, 2019). The selection and combined expression of highly active ADH, ALDH, and NOX in E. coli cells have resulted in markedly increased production of nonanedioic acid, decanedioic acid, undecanedioic acid, and dodecanedioic acid (Kang et al, 2020; Kim, Kang, Park,et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

Pentadecanedioic acid production from 15‐hydroxypentadecanoic acid using an engineered biocatalyst with a co‐factor regeneration system

Shin

Kang

et al. 2022

J Americ Oil Chem Soc

α,ω-Dicarboxylic acids are valuable precursors in various chemical industries and have recently been produced using biotechnological methods to overcome the limitations of chemical synthesis. Nonanedioic acid, decanedioic acid, undecanedioic acid, and dodecanedioic acid have been produced at high concentrations from ω-hydroxycarboxylic acids using engineered biocatalysts. However, no study has been attempted on the efficient production of pentadecanedioic acid. Here, the production of pentadecanedioic acid from 15-hydroxypentadecanoic acid was carried out with alcohol dehydrogenases (ADHs), aldehyde dehydrogenases (ALDHs), and NAD(P)H oxidases, including NAD(P)H flavin oxidoreductase (NFO), that used a co-factor regeneration system, derived from several species and expressed in Escherichia coli. Among the enzymes, Kangiella koreensis ADH (KkADH), Geobacillus kaustophilus ALDH (GkALDH), and Deinococcus radiodurans NFO (DrNFO) were selected because they had the highest activity. E. coli expressing pRSF-DrNFO and pACYC-KkADH/GkALDH as the best distribution of three genes in two plasmids was used as a biocatalyst to produce pentadecanedioic acid. The optimal conditions for producing pentadecanedioic acid from 15-hydroxypentadecanoic acid by the biocatalyst were pH 8.0, 35 C, 5% (v/v) methanol, 40 g L À1 cells, and 60 mM 15-hydroxypentadecanoic acid with agitation at 250 rpm. Under these optimized conditions, 57.4 mM pentadecanedioic acid was produced after 3 h, with a molar yield of 95.6% and a productivity of 19.1 mM h À1 . The molar yield and concentration of pentadecanedioic acid showed the highest values among the reported biotechnological production of pentadecanedioic acid.