Non-ionic surfactant formulation sequentially enhances the enzymatic hydrolysis of cellulignin from sugarcane bagasse and the production of Monascus ruber biopigments.

The effect of a non-ionic surfactant optimized formulation (SOF) obtained from an experimental design was evaluated for different influencing variables in the processing of sugarcane bagasse cellulignin to produce biopigments. The major findings in the saccharification stage using the SOF point that: at same enzyme loading, the highest glucan hydrolysis yield was 63 % (2-fold higher compared to control); the enzyme loading of 2.5 FPU/g resulted in similar yield compared to 10 FPU/g (control); 15 % (m/v) of total solids loading maintained the yield in fed-batch configuration; the hydrolysis yield is maintained at high shear force stress (800 rpm of stirring rate) and temperatures (50-70 °C). Besides, under separate and semi-simultaneous hydrolysis and fermentation, the maximum biopigments production were of 10 AU510nm/mL and 17.84 AU510nm/mL, respectively. The SOF used in this study was found to be a promising additive either in a single or sequential steps to produce biopigments in biorefineries.

A review on recent developments in hydrodynamic cavitation and advanced oxidative processes for pretreatment of lignocellulosic materials.

Environmental problems due to utilization of fossil-derived materials for energy and chemical generation has prompted the use of renewable alternative sources, such as lignocellulose biomass (LB). Indeed, the production of biomolecules and biofuels from LB is among the most important current research topics aiming to development a sustainable bioeconomy. Yet, the industrial use of LB is limited by the recalcitrance of biomass, which impairs the hydrolysis of the carbohydrate fractions. Hydrodynamic cavitation (HC) and Advanced Oxidative Processes (AOPs) has been proposed as innovative pretreatment strategies aiming to reduce process time and chemical inputs. Therefore, the underlying mechanisms, procedural strategies, influence on biomass structure, and research gaps were critically discussed in this review. The performed discussion can contribute to future developments, giving a wide overview of the main involved aspects.

Commercial Washing Detergents-Assisted Alkaline Pretreatment for Lignocellulosic Sugars Production: A First Report.

Lignocellulosic sugars are the major renewable building blocks for green fuels and chemicals production. However, the implication of an effective pretreatment process is an inevitable process to access the biomass sugars. Alkaline pretreatment is a viable pretreatment process, causing a selective removal of lignin, with a minimum degradation of carbohydrates, increasing porosity and surface area, eventually enhancing enzymatic hydrolysis. Here, we have assessed commercial cloth washing detergents as catalytic agents, for the lignin removal from sugarcane bagasse. Three different detergents (Brilhiante® (B), Omo® (O), Sabonito Flash® (F)) were tested using three different concentrations (5, 10 and 15%) with and without pH adjustment. Pretreatment with O5pH (5% Omo®, pH 12) showed the maximum lignin removal (81.14%) and retainment of cellulose (44.15%), and hemicellulose (29.71%) in the pretreated bagasse. The maximum sugars (26.62 g/L) were released from the O10pH-pretreated sugarcane bagasse. This study shows the potential of washing detergents as the new potential catalytic agents for the pretreatment of biomass for efficient sugars recovery and retaining maximum lignin in the pretreated substrate.

Interaction between the transcription factor SPBP and the positive cofactor RNF4. An interplay between protein binding zinc fingers.

The activator of stromelysin 1 gene transcription, SPBP, interacts with the RING finger protein RNF4. Both proteins are ubiquitously expressed and localized in the nucleus. RNF4 facilitates accumulation of specific SPBP-DNA complexes in vitro and acts as a positive cofactor in SPBP-mediated transactivation. SPBP harbors an internal zinc finger of the PHD/LAP type. This domain can form intra-chain protein-protein contacts in SPBP resulting in negative modulation of SPBP-RNF4 interaction.