• Journal of computational fluids engineering
• /
• 제16권2호
• /
• pp.62-65
• /
• 2011

Characteristics of the pressure drop in an expanded bed have been compared to those in a packed bed for numerical study of the interphase drag in gas-particle flows. A numerical analysis of the pressure drop by the particle drag has been conducted according to the tube-to-particle diameter ratios and Reynolds numbers for comparison. As the tube-to-particle diameter ratios increase at the same Reynolds number, the pressure drop tends to converge. It has been confirmed that characteristics of the pressure drop in the expanded bed are similar to those in the packed bed.

• Environmental Engineering Research
• /
• 제20권4호
• /
• pp.336-341
• /
• 2015

The industrial-scale biological treatment of Chinese nutgall processing wastewater was conducted with a $200m^3$ expanded granular sludge bed reactor and a $900m^3$ bio-contact oxidation reactor. The temperature of the two reactors was controlled under mesophilic conditions ($32-40^{\circ}C$), through changing the proportion of the dilution water, which was composed of steam condensation water and residual circulating water. The effluent COD, gallic acid, chroma, total nitrogen, total phosphorus levels and pH of both the expanded granular sludge bed and bio-contact oxidation reactors were monitored. In addition, the redox potential in the expanded granular sludge bed was recorded. The total COD removal efficiency was 87.257% when the influent COD concentration was $14\;251{\pm}3\;148mg/L$, and the ratio of wastewater: dilution water was 1:5. The removal efficiencies of gallic acid, chroma, total nitrogen, and total phosphorus were 72.221%, 43.940%, 64.151% and 39.316%, respectively. The effluent pH increased in either the expanded granular sludge bed reactor or the bio-contact oxidation reactor during the operation. The redox potential in the expanded granular sludge bed varied between -367 mV and -435 mV. The results indicate that the combined process was suitable for treating Chinese nutgall processing wastewater.

• KSBB Journal
• /
• 제16권2호
• /
• pp.146-152
• /
• 2001

To avoid the intrinsic problem of aggregation associated with the traditional solution-phase refolding process, we propose a solid-phase refolding method integrated with expanded bed adsorption chromatography. The model protein used was a fusion protein of recombinant human growth hormone and a glutathione S transferase fragment. It was demonstrated that the EBA-mediated refolding technique could simultaneously remove cellular debris and directly renature the fusion protein inclusion bodies in the cell homogenate with much higher yields and less agregation. To demonstrate the applicability of the method, we successfully tested the three representative types of starting materials, i. e., rhGH monomer, washed inclusion bodies, and the E. coli homogenate. This direct and simplified refolding process could also reduce the number of renaturation steps required and allow refolding at a higher concentration, at approximately 2 mg fusion protein per ml of resin. To the best of our knowledge, it is the first approach that has combined the solid-phase refolding method with expanded bed chromatography.

• Biotechnology and Bioprocess Engineering:BBE
• /
• 제10권3호
• /
• pp.280-283
• /
• 2005

The adsorption of a model protein bovine serum albumin (BSA) in expanded bed chromatography was undertaken by exploiting a commercially available expanded bed column (20 mm i.d.) from UpFront Chromatography and Streamline DEAE $(\rho=1.2g/cm^3)$ from Amersham Pharmacia Biotechnology. The influence of whole yeast cells on the adsorption capacity of column was explored by employing yeast cells in a concentration ranged of 0 to $15\%(w/v)$. Equilibrium isotherms for adsorption of BSA on Streamline DEAE were correlated by using Langmuir equation. The presence of yeast cells resulted in decreased of BSA binding capacity in both batch binding and expanded bed chromatography. Results indicated that the yeast cells act as competitor for proteins to bind to the sites on adsorbents.

• Journal of Microbiology
• /
• 제42권3호
• /
• pp.228-232
• /
• 2004

In this paper, we investigated the development of a simplified and rapid primary capture step for the recovery of M13 bacteriophage from particulate-containing feedstock. M13 bacteriophage, carrying an insert, was propagated and subsequently purified by the application of both conventional multiple steps and expanded bed anion exchange chromatography. In the conventional method, precipitation was conducted with PEG/NaCl, and centrifugation was also performed. In the single step expanded bed anion exchange adsorption, UpFront FastLine$\_$TM/20 (20mm i.d.) from UpFront Chromatography was used as the contactor, while 54$m\ell$ (H$\_$o/=15cm) of STREAMLINE DEAE (p=1.2 g/㎤) from Amersham Pharmacia Biotechnology was used as the anion exchanger. The performance of the two methods were evaluated, analysed, and compared. It was demonstrated that the purification of the M13 bacteriophage, using expanded bed anion exchange adsorption, yielded the higher recovery percentage, at 82.86％. The conventional multiple step method yielded the lower recovery percentage, 36.07％. The generic application of this integrated technique has also been assessed.

• Journal of Microbiology and Biotechnology
• /
• 제11권5호
• /
• pp.776-780
• /
• 2001

Based on the static and dynamic adsorption of Streamline DEAE, a modified tank-in-series model including particle size distribution was used to describe the adsorption performance of bovine serum albumin in an expanded bed. The calculated results indicated that the suggested model was able to simulate breakthrough curves under various conditions.

• Biotechnology and Bioprocess Engineering:BBE
• /
• 제11권5호
• /
• pp.466-469
• /
• 2006

The bed stability of Streamline DEAE (p = 1.2 g/mL) in a 20mm (i.d.) glass expanded bed contactor, and its performance on the recovery of glucose 6-phosphate dehydrogenase (G6PDH) from unclarified yeast homogenate were investigated. A residence time distribution study showed that a stable expanded bed was achieved. The theoretical plate and Bodenstein numbers determined were 25 and 53, respectively. A recovery yield of 87% and purification factor of 4.1 were achieved in the operation using 5% (w/v) biomass concentration feedstock. The performance of the anion exchange EBAC was still considerable good at a biomass concentration as high as 15% (w/v).

• Biotechnology and Bioprocess Engineering:BBE
• /
• 제10권2호
• /
• pp.128-135
• /
• 2005

Mixed-mode hydrophobic/ionic matrices exhibit a salt-tolerant property for adsorbing target protein from high-ionic strength feedstock, which allows the application of undiluted feedstock via an expanded bed process. In the present work, a new type of mixed-mode adsorbent designed for expanded bed adsorption, Fastline $PRO^{\circledR}$, was challenged for the capture of nattokinase from the high ionic fermentation broth of Bacillus subtilis. Two important factors, pH and ion concentration, were investigated with regard to the performance of nattokinase ad-sorption. Under initial fermentation broth conditions (pH 6.6 and conductivity of 10 mS/cm) the adsorption capacity of nattokinase with Fastline PRO was high, with a maximum capacity of 5,350 U/mL adsorbent. The elution behaviors were investigated using packed bed adsorption experiments, which demonstrated that the effective desorption of nattokinase could be achieved by effecting a pH of 9.5. The biomass pulse response experiments were carried out in order to evaluate the biomass/adsorbent interactions between Bacillus subtilis cells and Fastline PRO, and to demonstrate a stable expanded bed in the feedstock containing Bacillus subtilis cells. Finally, an EBA process, utilizing mixed-mode Fastline PRO adsorbent, was optimized to capture nattokinase directly from the fermentation broth. The purification factor reached 12.3, thereby demonstrating the advantages of the mixed-mode EBA in enzyme separation.

• KSBB Journal
• /
• 제18권6호
• /
• pp.500-505
• /
• 2003

‘LK (lipoprotein kringle) 68’is a polypeptide of a modified ansiostatin consisting of three kringle structures that might be clinically useful as a potential cancer therapeutics. It can be produced by overexpressing it as inclusion body in recombinant E. coli. In this study, solid-phase refolding processes using packed bed adsorption (PBA) and expanded bed adsorption (EBA) column were carried out to compare their refolding yields with that of the conventional, solution-phase refolding process, For the solution-phase and the PBA-mediated processes employing Q-Sepharose, washed inclusion body was used as the starting material, whereas both washed inclusion body and E. coli homogenate were used for the EBA-mediated process employing streamline DEAE. On the final recovery LK68 per unit mass of wet cell basis, the EBA- and PBA-mediated processes showed about 2.7- and 1.5-fold higher yields, respectively, than the solution-phase refolding method. The solid-phase refolded LK68 demonstrated the same Iysine binding bioactivity and the retention time in the RP-and SEC-HPLC as those of the native protein.

• Journal of Microbiology and Biotechnology
• /
• 제19권4호
• /
• pp.416-423
• /
• 2009

Hepatitis B core antigen(HBcAg) is an important serological marker used in the diagnosis of hepatitis B virus(HBV) infections. In the current study, a fast and efficient preparative purification protocol for truncated HBcAg from Escherichia coli disruptate was developed. The recombinant HBcAg was first captured by anion exchange expanded bed adsorption chromatography integrated with a cell disruption process. This online capture process has shortened the process time and eliminated the "hold-up" period that may be detrimental to the quality of target protein. The eluted product from the expanded bed adsorption chromatography was subsequently purified using size-exclusion chromatography. The results showed that this novel purification protocol achieved a recovery yield of 45.1% with a product purity of 88.2%, which corresponds to a purification factor of 4.5. The recovered HBcAg is still biologically active as shown by ELISA test.