Downstream extraction process development for recovery of organic acids from a fermentation broth.

The present study focused on organic acids (OAs) recovery from an acidogenic fermentation broth, which is the main problem regarding the use of OAs for production of ester-based new generation biofuels or other applications. Specifically, 10 solvents were evaluated for OAs recovery from aqueous media and fermentation broths. The effects of pH, solvent/OAs solution ratios and application of successive extractions were studied.

Economic evaluation of technology for a new generation biofuel production using wastes.

An economic evaluation of an integrated technology for industrial scale new generation biofuel production using whey, vinasse, and lignocellulosic biomass as raw materials is reported. Anaerobic packed-bed bioreactors were used for organic acids production using initially synthetic media and then wastes. Butyric, lactic and acetic acid were predominately produced from vinasse, whey, and cellulose, respectively.

New generation biofuel: continuous acidogenesis of sucrose-raffinose mixture simulating vinasse is promoted by γ-alumina pellets.

Background: This investigation comprises a contribution on the production of a new generation biofuel using the industrial liquid waste of bioethanol distilleries, known as vinasse. This study focuses on the exploitation of vinasse as an acidogenesis substrate for volatile fatty acids and simultaneous ethanol production. These products can be used for ester production, which is the new generation biofuel.

Continuous acidogenesis of sucrose, raffinose and vinasse using mineral kissiris as promoter.

The use of kissiris as promoter (culture immobilization carrier) in anaerobic acidogenesis of sucrose, raffinose and vinasse is reported. Initially, the effect of pH (4-8) and fermentation temperature (18-52 °C) on the accumulation of low molecular weight organic acids (OAs) during sucrose acidogenesis, was evaluated. The promoting effect of kissiris was confirmed compared to free cells, resulting in 80% increased OAs production.

Tailoring structure-function properties of L-asparaginase: engineering resistance to trypsin cleavage.

Bacterial L-ASNases (L-asparaginases) catalyse the conversion of L-asparagine into L-aspartate and ammonia, and are widely used for the treatment of ALL (acute lymphoblastic leukaemia). In the present paper, we describe an efficient approach, based on protein chemistry and protein engineering studies, for the construction of trypsin-resistant PEGylated L-ASNase from Erwinia carotovora (EcaL-ASNase). Limited proteolysis of EcaL-ASNase with trypsin was found to be associated with a first cleavage of the peptide bond between Lys53 and Gly54, and then a second cleavage at Arg206-Ser207 of the C-terminal fragment, peptide 54-327, showing that the initial recognition sites for trypsin are Lys53 and Arg206.