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Almeida, Renata M. R. G.

Publications and source records attributed to Almeida, Renata M. R. G..

Protective effects of non–catalytic proteins on endoglucanase activity at air and lignin interfaces

The manner in which added non-catalytic proteins during enzymatic hydrolysis of lignocellulosic substrates enhances hydrolysis mechanisms is not completely understood. Prior research has indicated that a reduction in the non-specific adsorption of enzymes on lignin, and deactivation of enzymes exposed to air–liquid interface provide rationale. This work investigated root causes including effects of the air–liquid interface on non-catalytic proteins, and effects of lignin on endoglucanase. Three different experimental designs and three variables (air–liquid interfacial area, the types of lignin (acid or enzymatic lignin), and the presence of non-enzymatic protein (bovine serum albumin [BSA] or soy proteins ) were used. The results showed that acid isolated lignin adsorbed almost all endoglucanase activity initially present in supernatant, independent of air interface conditions (25 or 250 ml flasks) with the presence of BSA preventing this effect. Endoglucanase lost 30%–50% of its activity due to an air–liquid interface in the presence of lignin while addition of non-enzymatic protein helped to preserve this enzyme's activity. Langmuir and Freundlich models applied to experimental data indicated that the adsorption increases with increasing temperature for both endoglucanase and BSA. Adsorption of the enzyme and protein were endothermic with an increase in entropy. Finally, these results, combined, show that hydrophobicity plays a strong role in the adsorption of both endoglucanase and BSA on lignin.

59 BASIC BIOLOGICAL SCIENCES↗

Enzyme interactions on lignocellulosic biomass structure

This chapter shows that, although well studied over the years, the cellulose enzymatic hydrolysis process has still many obstacles to be overcome or minimized. High enzyme loading and relatively long incubation periods are generally required for effective cellulose saccharification to be achieved. These limitations make the process unattractive from an economic perspective. Most studies show that the conversion rate of cellulose hydrolysis decreases over reaction time due to several factors that may inhibit, deactivate, or slow the work of enzymes. Some of these factors are inhibition by the product generated; inhibition/deactivation of enzymes by by-products generated during pretreatment (PT); limitation of mass transfer; shear stress by high stirring; air–liquid interfacial area; and unproductive adsorption on lignin or other compounds present in the biomass. The interaction between cellulases and the lignin present in these biomasses has a major negative impact on the process, with the source of the raw material and the type of PT used having a strong influence on it. Finally, the use of nonenzymatic proteins seems to be the best way to mitigate this problem.

20 FOSSIL-FUELED POWER PLANTS↗