RESUMEN
We have performed a combined quantum mechanical and microkinetic modeling study to understand the nascent decomposition pathways of methane pyrolysis, catalyzed by gas-phase ZnCl2, in a constant pressure batch reactor at 1273 K. We find that ZnCl2 catalyzes methane pyrolysis with an apparent activation energy of 227 kJ/mol. We have also performed sensitivity analysis on a reaction network comprising initiation, termination, and primary propagation reactions. The results suggest that the whole reaction network can be simplified to four reactions, which contributes to the initial rate of methane decomposition. Based on these insights, we have also explored the catalyzing effects of gas-phase AlCl3, CoCl2, CuCl2, FeCl2, and NiCl2 for methane decomposition. Our calculations suggest that gas-phase CuCl2 and NiCl2 are the most active catalysts among the metal halides studied in this work.
RESUMEN
This work uses a coupled experimental and modeling approach to explore the effects of macro- and micro-mixing on the kinetics and the dynamics of two-phase enzymatic hydrolysis of hemicellulose. Reactor mixing does not alter the non-competitive nature of product inhibition in hemicellulose hydrolysis by endoxylanase, but produces stronger inhibition that reduces the soluble sugar yield by 8-14.5%, as the mixing speed increases from 0 to 200â¯rpm. The kinetic constants (Km, Vmax, Kx) assume mass-transfer disguised values at 0-200â¯rpm. An optimal mixing strategy, comprising of 55-70â¯min of initial rapid convective macromixing followed by diffusive micromixing (without any macromixing) for the rest of the hydrolysis, increases xylose and reducing sugar yields by 6.3-8% and 13-20%, respectively, over continuous mixing at 200â¯rpm, for 1-5â¯mg/ml substrate loading at an optimum enzyme to substrate ratio of 1:20, with an energy saving of 94-96% over 24â¯h.
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Biocombustibles , Polisacáridos , Hidrólisis , CinéticaRESUMEN
Hemicelluloses are the earth's second most abundant structural polymers, found in lignocellulosic biomass. Efficient enzymatic depolymerization of xylans by cleaving their ß-(1 â 4)-glycosidic bonds to produce soluble sugars is instrumental to the cost-effective production of liquid biofuels. Here we show that the multi-scale two-phase process of enzymatic hydrolysis of amorphous hemicelluloses is dominated by its smallest scale-the pores. In the crucial first five hours, two to fourfold swelling of the xylan particles allow the enzymes to enter the pores and undergo rapid non-equilibrium adsorption on the pore surface before they hydrolyze the solid polymers, albeit non-competitively inhibited by the products xylose and xylobiose. Rapid pore-scale reactive dissolution increases the solid carbohydrate's porosity to 80-90%. This tightly coupled experimental and theoretical study quantifies the complex temporal dynamics of the transport and reaction processes coupled across scales and phases to show that this unique pore-scale phenomenon can be exploited to accelerate the depolymerization of hemicelluloses to monomeric sugars in the first 5-6 h. We find that an 'optimal substrate loading' of 5 mg/ml (above which substrate inhibition sets in) accelerates non-equilibrium enzyme adsorption and solid hemicellulose depolymerization at the pore-scale, which contributes three-quarters of the soluble sugars produced for bio-alcohol fermentation.
Asunto(s)
Biocombustibles , Disacáridos/química , Endo-1,4-beta Xilanasas/química , Proteínas Fúngicas/química , Polisacáridos/química , Trichoderma/enzimología , Xilosa/química , HidrólisisRESUMEN
We present a coupled experimental and theoretical framework for quantifying the kinetics of two-phase enzymatic hydrolysis of hemicellulose. For xylan loading of 1-5mg/ml, the nature of inhibition by the product xylose (non-competitive), the kinetic constants (Km=3.93 mg/ml, Vmax=0.0252 mg/ml/min) and the xylose inhibition constant (Kx=0.122 mg/ml) are experimentally determined. Our multi-step two-phase kinetic model incorporating enzyme adsorption to the solid substrate and non-competitive product inhibition is simulated using our kinetic data and validated against our experimentally measured temporal dynamics of xylose and reducing sugars. Further experiments show that higher substrate loading reduces the specific adsorption of the endoxylanase to the solid xylan and the enzyme's solid-liquid distribution ratio, which decelerates the solid hydrolysis and accelerates the liquid phase reactions. Thus, the xylose yield increases with substrate loading, which increases product inhibition and decreases reducing sugar yields. An operating cost analysis gives 3mg/ml as the optimal substrate loading.