Insecticidal Activity of Organic Extracts of and Its Main Metabolites (Quercetin and Chlorogenic Acid) against : An In Vitro and In Silico Approach.

() remains a global primary pest of maize. Therefore, new options to combat this pest are necessary. In this study, the insecticidal activity of three crude foliar extracts (ethanol, dichloromethane, and hexane) and their main secondary metabolites (quercetin and chlorogenic acid) of the species () by ingestion bioassays against larvae was analyzed.

On-line monitoring of Aspergillus niger GH1 growth in a bioprocess for the production of ellagic acid and ellagitannase by solid-state fermentation.

The present work describes the monitoring of CO production by Aspergillus niger GH1 in a bioprocess for the production of ellagitannase (EAH) and ellagic acid by solid state fermentation. Pomegranate ellagitannins, mainly punicalagin, were used as carbon source and EAH inducer. A second condition, using ellagitannins and maltose as growth promoting carbon source, was tested.

Soluble and bound hydroxycinnamates in coffee pulp (Coffea arabica) from seven cultivars at three ripening stages.

The contents of soluble and bound hydroxycinnamates (HCAs) were analyzed in coffee pulp (CP) of seven cultivars of Coffea arabica at three different ripening stages. Methodologies for the extraction and analysis of HCAs were evaluated and improved. HCAs were present mainly in the soluble fraction (68-97%).

Interaction of tannase from Aspergillus niger with polycations applied to its primary recovery.

The interaction of tannase (TAH) with chitosan, polyethyleneimine and Eudragit(®)E100 was studied. It was found that TAH selectively binds to these polycations (PC), probably due to the acid nature of the target protein. TAH could interact with these PC depending on the medium conditions.

Partition in aqueous two-phase system: its application in downstream processing of tannase from Aspergillus niger.

Tannase from Aspergillus niger was partitioned in aqueous two-phase systems composed by polyethyleneglycol of molar mass 400, 600 and 1000 and potassium phosphate. Tannase was found to be partitioned toward the salt-rich phase in all systems, with partition coefficients lower than 0.5.

Optimization of tannase production by Aspergillus niger in solid-state packed-bed bioreactor.

Tannin acyl hydrolase, also known as tannase, is an enzyme with important applications in the food, feed, pharmaceutical, and chemical industries. However, despite a growing interest in the catalytic properties of tannase, its practical use is very limited owing to high production costs. Several studies have already demonstrated the advantages of solid-state fermentation (SSF) for the production of fungal tannase, yet the optimal conditions for enzyme production strongly depend on the microbial strain utilized.

Novel strategies for upstream and downstream processing of tannin acyl hydrolase.

Tannin acyl hydrolase also referred as tannase is an enzyme with important applications in several science and technology fields. Due to its hydrolytic and synthetic properties, tannase could be used to reduce the negative effects of tannins in beverages, food, feed, and tannery effluents, for the production of gallic acid from tannin-rich materials, the elucidation of tannin structure, and the synthesis of gallic acid esters in nonaqueous media. However, industrial applications of tannase are still very limited due to its high production cost.

Catalytical Properties of Free and Immobilized Aspergillus niger Tannase.

A fungal tannase was produced, recovered, and immobilized by entrapment in calcium alginate beads. Catalytical properties of the immobilized enzyme were compared with those of the free one. Tannase was produced intracellularly by the xerophilic fungus Aspergillus niger GH1 in a submerged fermentation system.

Catalytic and thermodynamic properties of a tannase produced by Aspergillus niger GH1 grown on polyurethane foam.

Tannase is an inducible enzyme with important applications in the food and pharmaceutical industries. This enzyme was produced by the fungus Aspergillus niger GH1 under solid-state fermentation using polyurethane foam as solid support and tannic acid as sole carbon source and tannase inducer. Physicochemical properties of A.

Differential properties of Aspergillus niger tannase produced under solid-state and submerged fermentations.

Significant differences on structure, stability, and catalytic properties of tannase were found when this enzyme was produced under solid-state and submerged fermentations (SSF and SmF) by Aspergillus niger. The specific activity was 5.5 times higher on SSF than in SmF.