Continuous bioethanol fermentation from wheat straw hydrolysate with high suspended solid content using an immersed flat sheet membrane bioreactor.

Finding a technological approach that eases the production of lignocellulosic bioethanol has long been considered as a great industrial challenge. In the current study a membrane bioreactor (MBR) set-up using integrated permeate channel (IPC) membrane panels was used to simultaneously ferment pentose and hexose sugars to ethanol in continuous fermentation of high suspended solid wheat straw hydrolysate. The MBR was optimized to flawlessly operated at high SS concentrations of up to 20% without any significant changes in the permeate flux and transmembrane pressure. By the help of the retained high cell concentration, the yeast cells were capable of tolerating and detoxifying the inhibitory medium and succeeded to co-consume all glucose and up to 83% of xylose in a continuous fermentation mode leading to up to 83% of the theoretical ethanol yield.

Reverse membrane bioreactor: Introduction to a new technology for biofuel production.

The novel concept of reverse membrane bioreactors (rMBR) introduced in this review is a new membrane-assisted cell retention technique benefiting from the advantageous properties of both conventional MBRs and cell encapsulation techniques to tackle issues in bioconversion and fermentation of complex feeds. The rMBR applies high local cell density and membrane separation of cell/feed to the conventional immersed membrane bioreactor (iMBR) set up. Moreover, this new membrane configuration functions on basis of concentration-driven diffusion rather than pressure-driven convection previously used in conventional MBRs. These new features bring along the exceptional ability of rMBRs in aiding complex bioconversion and fermentation feeds containing high concentrations of inhibitory compounds, a variety of sugar sources and high suspended solid content. In the current review, the similarities and differences between the rMBR and conventional MBRs and cell encapsulation regarding advantages, disadvantages, principles and applications for biofuel production are presented and compared. Moreover, the potential of rMBRs in bioconversion of specific complex substrates of interest such as lignocellulosic hydrolysate is thoroughly studied.

Fermentation of lignocellulosic hydrolyzate using a submerged membrane bioreactor at high dilution rates.

A submerged membrane bioreactor (sMBR) was developed to ferment toxic lignocellulosic hydrolyzate to ethanol. The sMBR achieved high cell density of Saccharomyces cerevisiae during continuous cultivation of the hydrolyzate by completely retaining all yeast cells inside the sMBR. The performance of the sMBR was evaluated based on the ethanol yield and productivity at the dilution rates 0.2, 0.4, 0.6, and 0.8h(-1) with the increase of dilution rate. Results show that the yeast in the sMBR was able to ferment the wood hydrolyzate even at high dilution rates, attaining a maximum volumetric ethanol productivity of 7.94 ± 0.10 g L(-1)h(-1) at a dilution rate of 0.8h(-1). Ethanol yields were stable at 0.44 ± 0.02 g g(-1) during all the tested dilution rates, and the ethanol productivity increased from 2.16 ± 0.15 to 7.94 ± 0.10 g L(-1)h(-1). The developed sMBR systems running at high yeast density demonstrate a potential for a rapid and productive ethanol production from wood hydrolyzate.

Characterization and optimization of ß-galactosidase immobilization process on a mixed-matrix membrane.

ß-Galactosidase is an important enzyme catalyzing not only the hydrolysis of lactose to the monosaccharides glucose and galactose but also the transgalactosylation reaction to produce galacto-oligosaccharides (GOS). In this study, ß-galactosidase was immobilized by adsorption on a mixed-matrix membrane containing zirconium dioxide. The maximum ß-galactosidase adsorbed on these membranes was 1.6 g/m², however, maximal activity was achieved at an enzyme concentration of around 0.5 g/m². The tests conducted to investigate the optimal immobilization parameters suggested that higher immobilization can be achieved under extreme parameters (pH and temperature) but the activity was not retained at such extreme operational parameters. The investigations on immobilized enzymes indicated that no real shift occurred in its optimal temperature after immobilization though the activity in case of immobilized enzyme was better retained at lower temperature (5 °C). A shift of 0.5 unit was observed in optimal pH after immobilization (pH 6.5 to 7). Perhaps the most striking results are the kinetic parameters of the immobilized enzyme; while the Michaelis constant (K(m)) value increased almost eight times compared to the free enzyme, the maximum enzyme velocity (V(max)) remained almost constant.