Although there are already commercial-scale productions of second generation (2G) ethanol, focusing efforts on process optimization can be of key importance to make the production cost-effective in large scale. In this scenario, mathematical models may be useful in design, scale-up, optimization, and control of bioreactors. For this reason, the aim of this work was to study the kinetics of the enzymatic hydrolysis of cellulose from sugarcane straw. Experiments using hydrothermally pretreated sugarcane (HPS) straw (195 °C, 10 min, 200 rpm) with and without alkaline delignification (4 % NaOH m/v, 30 min, 121 °C) were carried out in shake flasks (50 °C, pH 5.0, 200 rpm). Solid load was varied in a range of 0.8 to 10 % (m/v), in initial velocity and long-term assays. Enzyme concentration (Cellic®CTec2) was varied from 5 to 80 filter paper unit (FPU) gcellulose (-1). It was possible to fit Michaelis-Menten (MM), modified MM, with and without competitive inhibition by glucose, and Chrastil models. Chrastil model and modified MM with inhibition (both suitable for heterogeneous system, with high resistance to internal diffusion) showed more appropriate than pseudo-homogeneous MM model. The fitted models were able to identify key features of the hydrolysis process and can be very useful within the perspective of bioreactors engineering.
-Partial hydrolysis of whey proteins by enzymes immobilized on an inert support can either change or evidence functional properties of the produced peptides, thereby increasing their applications. The hydrolysis of sweet cheese whey proteins by alcalase, which is multipoint-immobilized on agarose gel, is studied here. A MichaelisMenten model that takes into account competitive inhibition by the product was fitted to experimental data. The influence of pH on the kinetic parameters in the range 6.0 to 11.0 was assessed, at 50 o C. Initial reaction-rate assays in a pHstat at different concentrations of substrate were used to estimate kinetic and Michaelis-Menten parameters, k and K M . Experimental data from long-term batch assays were used to quantify the inhibition parameter, K I . The fitting of the model to the experimental data was accurate in the entire pH range.
-This work presents a kinetic study of the enzymatic hydrolysis of three cellulosic substrates: filter paper (FP), used as a low recalcitrance substrate model; steam exploded sugarcane bagasse (SB); and weak acid pretreated SB (1:20 dry bagasse:H 2 SO 4 solution 1% w/w), the last two delignified with 4% NaOH (w/w). The influence of substrate concentration was assessed in hydrolysis experiments in a shaker, using Accellerase® 1500, at pH 4.8, in 50 mM sodium citrate buffer. Cellulose loads (weight substrate /weight total ) were changed between 0.5%-13% (for FP) and 0.99%-9.09% (for SB). For FP and low loads of steam exploded SB, it was possible to fit pseudo-homogeneous Michaelis-Menten models (with inhibition). For FP and higher loads of steam exploded SB, modified Michaelis-Menten models were fitted. Besides, it was observed that, after retuning of the model parameters, it is possible to apply a model fitted for one situation to a different case. Chrastil models were also fitted and they were the only feasible approach for the highly recalcitrant acid-treated SB.
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