Novel Short Process for p-Xylene Production Based on the Selectivity Intensification of Toluene Methylation with Methanol.
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ABSTRACT:
SUBMITTER: Wang D
PROVIDER: S-EPMC8757337 | biostudies-literature |
REPOSITORIES: biostudies-literature
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Project description:Methylation of toluene with methanol to produce p-xylene has been investigated for decades, but the origin of selectivity is still under debate. Here we report computational studies based on ab initio molecular dynamics simulations and free energy sampling methods to identify the key steps determining the selectivity. The steps of toluene methylation to protonated-xylene, deprotonation of protonated-xylenes, and diffusion of xylene in HZSM-5 channels are compared. We find the pathways of formation for protonated p-/m-xylenes have similar free energy barriers. Meanwhile, the methylation is found rate-determining, thus the probability to generate p-/m-xylenes at the active site are similar. We then find that the diffusion for m-xylene along the zigzag channel is more difficult than its isomerization to p-xylene, which in turn further promotes the selectivity of p-xylene formation. These insights obtained at the molecular level are crucial for further development of high-performance zeolite catalysts for toluene methylation.
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Project description:Toluene methylation with methanol to produce xylene has been widely investigated. A simultaneous side reaction of methanol-to-olefin over zeolites is hard to avoid, resulting in an unsatisfactory methylation efficiency. Here, CO2 and H2 replace methanol in toluene methylation over a class of ZnZrO x -ZSM-5 (ZZO-Z5) dual-functional catalysts. Results demonstrate that the reactive methylation species (H3CO*; * represents a surface species) are generated more easily by CO2 hydrogenation than by methanol dehydrogenation. Catalytic performance tests on a fixed-bed reactor show that 92.4% xylene selectivity in CO-free products and 70.8% para-xylene selectivity in xylene are obtained on each optimized catalyst. Isotope effects of H2/D2 and CO2/13CO2 indicate that xylene product is substantially generated from toluene methylation rather than disproportionation. A mechanism involving generation of reactive methylation species on ZZO by CO2 hydrogenation and migration of the methylation species to Z5 pore for the toluene methylation to form xylene is proposed.
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Project description:The multicomponent protein toluene/o-xylene monooxygenase (ToMO) activates molecular oxygen to oxidize aromatic hydrocarbons. Prior to dioxygen activation, two electrons are injected into each of two diiron(III) units of the hydroxylase, a process that involves three redox active proteins: the ToMO hydroxylase (ToMOH), Rieske protein (ToMOC), and an NADH oxidoreductase (ToMOF). In addition to these three proteins, a small regulatory protein is essential for catalysis (ToMOD). Through steady state and pre-steady state kinetics studies, we show that ToMOD attenuates electron transfer from ToMOC to ToMOH in a concentration-dependent manner. At substoichiometric concentrations, ToMOD increases the rate of turnover, which we interpret to be a consequence of opening a pathway for oxygen transport to the catalytic diiron center in ToMOH. Excess ToMOD inhibits steady state catalysis in a manner that depends on ToMOC concentration. Through rapid kinetic assays, we demonstrate that ToMOD attenuates formation of the ToMOC-ToMOH complex. These data, coupled with protein docking studies, support a competitive model in which ToMOD and ToMOC compete for the same binding site on the hydroxylase. These results are discussed in the context of other studies of additional proteins in the superfamily of bacterial multicomponent monooxygenases.
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Project description:Although process intensification by continuous operation has been successfully applied in the chemical industry, the biopharmaceutical industry primarily uses fed-batch, rather than continuous or perfusion methods, to produce stable monoclonal antibodies (mAbs) from Chinese hamster ovary (CHO) cells. Conventional fed-batch bioreactors may start with an inoculation viable cell density (VCD) of ~0.5 × 106 cells/mL. Increasing the inoculation VCD in the fed-batch production bioreactor (referred to as N stage bioreactor) to 2-10 × 106 cells/mL by introducing perfusion operation or process intensification at the seed step (N-1 step) prior to the production bioreactor has recently been used because it increases manufacturing output by shortening cell culture production duration. In this study, we report that increasing the inoculation VCD significantly improved the final titer in fed-batch production within the same 14-day duration for 3 mAbs produced by 3 CHO GS cell lines. We also report that other non-perfusion methods at the N-1 step using either fed batch or batch mode with enriched culture medium can similarly achieve high N-1 final VCD of 22-34 × 106 cells/mL. These non-perfusion N-1 seeds supported inoculation of subsequent production fed-batch production bioreactors at increased inoculation VCD of 3-6 × 106 cells/mL, where these achieved titer and product quality attributes comparable to those inoculated using the perfusion N-1 seeds demonstrated in both 5-L bioreactors, as well as scaled up to 500-L and 1000-L N-stage bioreactors. To operate the N-1 step using batch mode, enrichment of the basal medium was critical at both the N-1 and subsequent intensified fed-batch production steps. The non-perfusion N-1 methodologies reported here are much simpler alternatives in operation for process development, process characterization, and large-scale commercial manufacturing compared to perfusion N-1 seeds that require perfusion equipment, as well as preparation and storage vessels to accommodate large volumes of perfusion media. Although only 3 stable mAbs produced by CHO cell cultures are used in this study, the basic principles of the non-perfusion N-1 seed strategies for shortening seed train and production culture duration or improving titer should be applicable to other protein production by different mammalian cells and other hosts at any scale biologics facilities.
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Project description:Toluene/o-xylene monooxygenase (ToMO) is a bacterial multicomponent monooxygenase capable of oxidizing aromatic substrates. The carboxylate-rich diiron active site is located in the hydroxylase component of ToMO (ToMOH), buried 12 Å from the surface of the protein. A small, hydrophilic pore is the shortest pathway between the diiron active site and the protein exterior. In this study of ToMOH from Pseudomonas sp. OX1, the functions of two residues lining this pore, N202 and Q228, were investigated using site-directed mutagenesis. Steady-state characterization of WT and the three mutant enzymes demonstrates that residues N202 and Q228 are critical for turnover. Kinetic isotope effects and pH profiles reveal that these residues govern the kinetics of water egress and prevent quenching of activated oxygen intermediates formed at the diiron active site. We propose that this activity arises from movement of these residues, opening and closing the pore during catalysis, as seen in previous X-ray crystallographic studies. In addition, N202 and Q228 are important for the interactions of the reductase and regulatory components to ToMOH, suggesting that they bind competitively to the hydroxylase. The role of the pore in the hydroxylase components of other bacterial multicomponent monooxygenases within the superfamily is discussed in light of these conclusions.
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Project description:Rhodococcus sp. strain DK17 is able to grow on o-xylene, benzene, toluene, and ethylbenzene. DK17 harbors at least two megaplasmids, and the genes encoding the initial steps in alkylbenzene metabolism are present on the 330-kb pDK2. The genes encoding alkylbenzene degradation were cloned in a cosmid clone and sequenced completely to reveal 35 open reading frames (ORFs). Among the ORFs, we identified two nearly exact copies (one base difference) of genes encoding large and small subunits of an iron sulfur protein terminal oxygenase that are 6 kb apart from each other. Immediately downstream of one copy of the dioxygenase genes (akbA1a and akbA2a) is a gene encoding a dioxygenase ferredoxin component (akbA3), and downstream of the other copy (akbA1b and akbA2b) are genes putatively encoding a meta-cleavage pathway. RT-PCR experiments show that the two copies of the dioxygenase genes are operonic with the downstream putative catabolic genes and that both operons are induced by o-xylene. When expressed in Escherichia coli, AkbA1a-AkbA2a-AkbA3 transformed o-xylene into 2,3- and 3,4-dimethylphenol. These were apparently derived from an unstable o-xylene cis-3,4-dihydrodiol, which readily dehydrates. This indicates a single point of attack of the dioxygenase on the aromatic ring. In contrast, attack of AkbA1a-AkbA2a-AkbA3 on ethylbenzene resulted in the formation of two different cis-dihydrodiols resulting from an oxidation at the 2,3 and the 3,4 positions on the aromatic ring, respectively.
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Project description:Monocyclic phenols and catechols are important antioxidant compounds for the food and pharmaceutic industries; their production through biotransformation of low-added value starting compounds is of major biotechnological interest. The toluene o-xylene monooxygenase (ToMO) from Pseudomonas sp. OX1 is a bacterial multicomponent monooxygenase (BMM) that is able to hydroxylate a wide array of aromatic compounds and has already proven to be a versatile biochemical tool to produce mono- and dihydroxylated derivatives of aromatic compounds. The molecular determinants of its regioselectivity and substrate specificity have been thoroughly investigated, and a computational strategy has been developed which allows designing mutants able to hydroxylate non-natural substrates of this enzyme to obtain high-added value compounds of commercial interest. In this work, we have investigated the use of recombinant ToMO, expressed in cells of Escherichia coli strain JM109, for the biotransformation of non-natural substrates of this enzyme such as 2-phenoxyethanol, phthalan and 2-indanol to produce six hydroxylated derivatives. The hydroxylated products obtained were identified, isolated and their antioxidant potential was assessed both in vitro, using the DPPH assay, and on the rat cardiomyoblast cell line H9c2. Incubation of H9c2 cells with the hydroxylated compounds obtained from ToMO-catalyzed biotransformation induced a differential protective effect towards a mild oxidative stress induced by the presence of sodium arsenite. The results obtained confirm once again the versatility of the ToMO system for oxyfunctionalization reactions of biotechnological importance. Moreover, the hydroxylated derivatives obtained possess an interesting antioxidant potential that encourages the use of the enzyme for further functionalization reactions and their possible use as scaffolds to design novel bioactive molecules.
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Project description:To produce biodiesel cost-effective, low-cost, high free fatty acid (FFA) oil feedstock is desirable. But high FFA creates difficulty during the base-catalyzed transesterification process by yield loss due to the formation of soap. However, these problems are overcome by the use of an acid catalyst. The acid catalysts can directly convert both triglycerides and FFAs into biodiesel without the formation of soaps or emulsions. The shortcomings of mostly used inorganic acids are that they work well for esterification of FFA present in low-cost oil, but their kinetics for transesterification of triglycerides present in oils is considerably slower. Corrosion of equipment is another major problem associated with an inorganic acid catalyst. The usage of an organic acid catalyst of the alkyl benzene sulfonic type, like 4-dodecyl benzene sulfonic acid (DBSA) minimizes these disadvantages of inorganic acid-catalyzed transesterification. The aim of the present investigation was to reduce the reaction time of transesterification of triglycerides further by using microwaves as a heating source in the presence of DBSA catalyst to achieve higher conversions under mild operating conditions. To optimize the transesterification variables for the higher conversion of biodiesel, the response surface methodology was employed to design the experiment. By using the DBSA catalyst under microwave heating at a temperature of 76 °C, conversion close to 100% in only 30 min of reaction time was obtained using a 0.09 molar ratio of catalyst to oil and 9.0 molar ratio of methanol to oil. A modified polynomial model was developed and was adequately fitted with the experimental data and could be used for understanding the effect of various process parameters. The catalyst to oil molar ratio and reaction temperature created a stronger effect on the biodiesel production than that exhibited by the methanol to oil molar ratio. It was observed that the microwave heating process outperformed conventional heating, providing a rapid, easy method for biodiesel synthesis from triglycerides in the presence of DBSA, an organic acid catalyst. The produced biodiesel was of good quality, as all the properties were within the prescribed limits of the ASTM D6751 standard.
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Project description:Organic compounds such as methanol are widely used for enhancing denitrification at wastewater treatment plants (WWTPs) to meet effluent water quality permits. On the other hand, methane, which is the main feedstock for industrial methanol production, is also generated during anaerobic digestion in WWTPs, but is often flared to mitigate its greenhouse impacts. The overarching goal herein was to develop a novel continuous process for methanol production from methane using nitrifying activated sludge. The maximum AOB specific methanol production rate using hydroxylamine as electron donor was 1.61 ± 0.15 and 1.27 ± 0.15 mg-COD-CH3OH/(mg-COD-AOB*d), for hydraulic retention times (HRTs) of 7.5 h and 2 h, respectively. The corresponding production rate using ammonia as electron donor was 0.31 ± 0.08 mg-COD-CH3OH/(mg-COD-AOB*d) at a HRT of 2 h. These results show that nitrifier-mediated methanol production in a continuous-flow system can enhance the efficiency of WWTPs through internal production of biomethanol for denitrification, while simultaneously minimizing wasteful biogas flaring.
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