Limited life cycle and cost assessment for the bioconversion of lignin-derived aromatics into adipic acid

Lignin is an abundant and heterogeneous waste byproduct of the cellulosic industry, which has the potential of being transformed into valuable biochemicals via microbial fermentation. In this study, we applied a fast-pyrolysis process using softwood lignin resulting in a two-phase bio-oil containing monomeric and oligomeric aromatics without syringol. We demonstrated that an additional hydrodeoxygenation step within the process leads to an enhanced thermochemical conversion of guaiacol into catechol and phenol. After steam bath distillation, Pseudomonas putida KT2440-BN6 achieved a percent yield of cis, cis-muconic acid of up to 95 mol% from catechol derived from the aqueous phase. We next established a downstream process for purifying cis, cis-muconic acid (39.9 g/L) produced in a 42.5 L fermenter using glucose and benzoate as carbon substrates. On the basis of the obtained values for each unit operation of the empirical processes, we next performed a limited life cycle and cost analysis of an integrated biotechnological and chemical process for producing adipic acid and then compared it with the conventional petrochemical route. The simulated scenarios estimate that by attaining a mixture of catechol, phenol, cresol, and guaiacol (1:0.34:0.18:0, mol ratio), a titer of 62.5 (g/L) cis, cis-muconic acid in the bioreactor, and a controlled cooling of pyrolysis gases to concentrate monomeric aromatics in the aqueous phase, the bio-based route results in a reduction of CO2 -eq emission by 58% and energy demand by 23% with a contribution margin for the aqueous phase of up to 88.05 euro/ton. We conclude that the bio-based production of adipic acid from softwood lignins brings environmental benefits over the petrochemical procedure and is cost-effective at an industrial scale. Further research is essential to achieve the proposed cis, cis-muconic acid yield from true lignin-derived aromatics using whole-cell biocatalysts

Polychromatic solitons in a quadratic medium

We introduce the simplest model to describe parametric interactions in a quadratically nonlinear optical medium with the fundamental harmonic containing two components with (slightly) different carrier frequencies [which is a direct analog of wavelength-division multiplexed (WDM) models, well known in media with cubic nonlinearity]. The model takes a closed form with three different second-harmonic components, and it is formulated in the spatial domain. We demonstrate that the model supports both polychromatic solitons (PCSs), with all the components present in them, and two types of mutually orthogonal simple solitons, both types being stable in a broad parametric region. An essential peculiarity of PCS is that its power is much smaller than that of a simple (usual) soliton (taken at the same values of control parameters), which may be an advantage for experimental generation of PCSs. Collisions between the orthogonal simple solitons are simulated in detail, leading to the conclusion that the collisions are strongly inelastic, converting the simple solitons into polychromatic ones, and generating one or two additional PCSs. A collision velocity at which the inelastic effects are strongest is identified, and it is demonstrated that the collision may be used as a basis to design a simple all-optical XOR logic gate.Comment: 9 pages, 8 figures, accepted to Phys. Rev.

Characterization of fructose 1,6-bisphosphatase and sedoheptulose 1,7-bisphosphatase from the facultative ribulose monophosphate cycle methylotroph Bacillus methanolicus

Stolzenberger J, Lindner S, Persicke M, Brautaset T, Wendisch VF. Characterization of fructose 1,6-bisphosphatase and sedoheptulose 1,7-bisphosphatase from the facultative ribulose monophosphate cycle methylotroph Bacillus methanolicus. Journal of Bacteriology. 2013;195(22):5112-5122

Fructose-1,6-bisphosphate aldolase (FBA)–a conserved glycolytic enzyme with virulence functions in bacteria: ‘ill met by moonlight’

© 2014 Biochemical Society. Moonlighting proteins constitute an intriguing class of multifunctional proteins. Metabolic enzymes and chaperones, which are often highly conserved proteins in bacteria, archaea and eukaryotic organisms, are among the most commonly recognized examples of moonlighting proteins. Fructose-1,6-bisphosphate aldolase (FBA) is an enzyme involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Increasingly, it is also recognized that FBA has additional functions beyond its housekeeping role in central metabolism. In the present review, we summarize the current knowledge of the moonlighting functions of FBA in bacteria