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Biomedical subjects

Jürgen Hubbuch

Publications and source records attributed to Jürgen Hubbuch.

13 recordsLinked to original sources

Separation of genomic DNA, RNA, and open circular plasmid DNA from supercoiled plasmid DNA by combining denaturation, selective renaturation and aqueous two-phase extraction.

In the current study we developed a process for the capture of pDNA exploiting the ability of aqueous two-phase systems to differentiate between different forms of DNA. In these systems scpDNA exhibits a near quantitative partitioning in the salt-rich bottom phase. The successive recovery from the salt rich bottom phase is accomplished by a novel membrane step. The polish operation to meet final purity demands is again based on a system exploiting a combination of the denaturation of the nucleic acids present, specific renaturation of scpDNA, and an ATP system able to differentiate between the renatured scpDNA and the denatured contaminants such as ocpDNA and genomic host DNA. This polish step thus allows a rapid and efficient separation of scpDNA from contaminating nucleic acids which up to date otherwise only can be accomplished with much more cumbersome chromatographic methods. In a benchmark comparison, it could be shown that the newly developed process exhibits a comparable yield to an industrial standard process while at the same time showing superior performance in terms of purity and process time. Additionally it could be shown that the developed polish procedure can be applied as a standalone module to support already existing processes.

Chemical Fractionation↗

Short-cut method for the correction of light attenuation influences in the experimental data obtained from confocal laser scanning microscopy.

Based on Lambert-Beer law and the light attenuation model, a new method will be introduced in this work in order to eliminate the disturbances caused by signal attenuation in the experimental data measured by confocal laser scanning microscopy (CLSM). This new method considers the attenuation effects which depend on concentration of fluorophore-labelled protein as well as attenuation effects which are independent from protein concentration. Furthermore, no solvent additive is required in order to match the refraction index of solvent to bead material. The determination of correction factors is, thus, easily done using the currently investigated chromatographic phase system, so that the validity of the correction factors in the current system can be guaranteed. The introduced correction method has been applied for the investigation of intraparticle protein distribution inside an HIC (hydrophobic interaction chromatography) particle.

Light↗

Developing a chromatographic column model for bovine serum albumin on strong anion-exchanger Source30Q using data from confocal laser scanning microscopy.

A systematic approach for the development of a column model for protein purification is introduced. The approach includes phenomenological investigations of mass transfer and adsorption behaviour applying confocal laser scanning microscopy (CLSM). Insights from CLSM measurements are then implemented mathematically into a single particle model which is coupled afterwards with a column model (i.e. general rate model). Finally, the general rate model is used to predict the results from pulse and frontal analysis in a chromatographic column. The applied exemplary chromatographic system is bovine serum albumin (BSA) on strong anion-exchanger Source30Q at neutral pH value.

Adsorption↗

Exploitation of the coil-globule plasmid DNA transition induced by small changes in temperature, pH salt, and poly(ethylene glycol) compositions for directed partitioning in aqueous two-phase systems.

In this study, the interplay of two linked equilibria is examined, one concerning an aqueous two-phase system (ATPS) composed of poly(ethylene glycol) (PEG) and salt employed to partition plasmid DNA (pDNA), and the other a potential structural transition of pDNA depending on PEG and salt concentration and other system parameters. The boundary conditions for pDNA partitioning are set by PEG and salt concentrations, PEG molecular weight, pH, and temperature. While investigating these parameters, it was found that a small increase/decrease of the respective values led to a drastic and significant change in pDNA behavior. This behavior could be attributed to a coil-globule transition of the pDNA triggered by the respective phase conditions. The combination of this structural change, aggregation effects linked to the transition process, and the electrostatic potential difference found in PEG-salt systems thus offers a sensitive way to separate nucleic acid forms on the basis of their unique property to undergo coil-globule transitions under distinct system properties.

DNA, Bacterial↗

Direct quantification of intraparticle protein diffusion in chromatographic media.

Diffusion coefficients of proteins in chromatographic media are important parameters for the rational design of stationary phases and purification schemes. In contrast to free diffusion, intraparticle diffusion is hindered by the porous structure of the media. Direct intraparticle diffusion analysis (IDA) is a novel approach for the determination of intraparticle protein diffusion coefficients. IDA is based on the evaluation of spatially and temporally resolved intraparticle concentration profiles. To prevent adsorption and to study diffusion only, the chromatographic media are investigated in underivatized form. With IDA, intraparticle concentration profiles are measured in a microcolumn by confocal laser scanning microscopy (CLSM). From this dynamic data, the diffusion coefficients are determined by parameter estimation, using a spheric diffusion model. The boundary condition is given by the measured protein concentration in the bulk phase. IDA is applied to determine intraparticle diffusion coefficients of seven different proteins in Sepharose 6 FF. The results show excellent congruence of experimental data and simulation results. Moreover, the determined diffusion coefficients lie well within the range of data published in the literature. Given that the material in question allows optical analysis, IDA is a general approach for studying protein diffusion in porous particles and is easily adapted to different proteins, solution conditions and stationary phases.

Animals↗

Protein-labeling effects in confocal laser scanning microscopy.

Confocal laser scanning microscopy (CLSM) is being increasingly used for observing protein uptake in porous chromatography resins. Recent CLSM studies have revealed the possible existence of a nondiffusive protein transport mechanism. Observing protein uptake with CLSM requires labeling the protein with a fluorescent probe. This study examines the effect of the probe identity on the subsequent CLSM adsorption profiles. The adsorption of lysozyme conjugated with different fluorescent probes (Cy5, BODIPY FL, Atto 635, and Atto 520) on SP Sepharose Fast Flow was measured using CLSM and zonal chromatography experiments. Results from zonal chromatography show that the retention time of lysozyme-dye conjugates differ significantly from unlabeled lysozyme. The change in retention of lysozyme upon conjugation with a fluorescent probe is consistent with the difference in net charge between the lysozyme-dye conjugate and unlabeled lysozyme. The adsorption profiles measured by CLSM show significantly different behavior depending upon whether the lysozyme-dye conjugate is retained longer or shorter than the unlabeled lysozyme. These results strongly suggest that the lysozyme concentration overshoot observed in previous CLSM experiments is the result of displacement of weaker binding labeled lysozyme by stronger binding unlabeled lysozyme.

Animals↗

Biochemical engineering aspects of expanded bed adsorption.

The economic feasibility of a biotechnological production process is directly linked to the number and efficiency of the processes required during purification in order to reach the requested product specifications. Expanded bed adsorption is an integrated process that combines solid-liquid separation and product recovery into a single unit operation. This approach suggests an increased overall yield, lower requirements for capital investments and consumables and most importantly a reduced process time. The success of an integrative process is, however, closely linked to a detailed understanding of the biochemical principles involved and the constraints arising from feedstock complexity. This paper reviews the hydrodynamic principles that expanded bed adsorption is based on, discusses current developments in resin and column design, and finally presents a methodology for targeted process development in expanded bed adsorption.

Adsorption↗

Integrated bioprocesses.

Integrated bioprocesses have been developed to optimise yield and cost-effectiveness of production of low and high molecular weight molecules. Low molecular weight products are removed from the cultivation medium with in situ extraction, in situ adsorption or crystallisation to avoid product inhibition. One-pot processes are being developed to replace two-stage reactions. Recent developments in the integrated purification of high molecular weight products focus mainly on the integration of solid/liquid separation and initial product recovery such as expanded bed adsorption or extraction in aqueous two-phase systems. Additionally, new approaches for a more efficient processing of inclusion bodies have been developed.

Bacteria↗

Scalable recovery of plasmid DNA based on aqueous two-phase separation.

Future developments in gene therapy and DNA vaccination depend on cost-effective large-scale production of pharmaceutical-grade pDNA (plasmid DNA). Given the large amount of impurities present in the feedstock, purification processes that have high specificity and capacity at a moderate cost are required. In the present study, we describe a non-chromatographic procedure based on aqueous two-phase extraction allowing a fast and simply scalable capture step. PEG [poly(ethylene glycol)] in combination with potassium citrate or potassium phosphate was tested as phase component for extraction. By increasing either PEG or salt concentration, the partitioning of nucleic acids changed from bottom to top phase. Phase systems with a composition of 15% PEG 800 and 20% potassium phosphate at pH 7.0 showed a strong partitioning of pDNA to the bottom phase, linked to a clear decrease in open circular pDNA, while proteins, genomic DNA and RNA remain at the top or at the interphase. A great advantage of the current process is that the complete procedure of lysis, precipitation, clarification and extraction can be performed in a single vessel. The number of denatured and sheared genomic DNAs in a spiking experiment was found to be depleted by more than 99%.

Chemical Fractionation↗

Mechanism and kinetics of protein transport in chromatographic media studied by confocal laser scanning microscopy. Part II. Impact on chromatographic separations.

The impact of different transport mechanism on chromatographic performance was studied by confocal laser scanning microscopy (CLSM) for solutions containing bovine serum albumin (BSA) and monoclonal IgG 2a under different solid- and fluid-phase conditions. During this investigation, a clear influence of the uptake mechanism on the affinity of the respective proteins for the different adsorbents and thus separation performance of the chromatographic process could be observed. For the system SP Sepharose Fast Flow at pH 4.5 pore diffusion could be ascribed to be the dominant transport mechanism for both proteins and the adsorption profiles resembled a pattern similar to that described by the 'shrinking core' model. Under these conditions a significantly higher affinity towards the adsorbent was found for BSA when compared to IgG 2a. With changing fluid- and solid-phase conditions, however, a change of the transport mode for IgG 2a could be detected. While the exact mechanism is still unresolved it could be concluded that both occurrence and magnitude of the now governing transport mechanism depended on protein properties and interaction with the adsorbent surface. For the system SP Sepharose XL at pH 5.0 both parameters leading to the change in IgG 2a uptake were combined resulting in a clear change of the system affinity towards the IgG 2a molecule, while BSA adsorption was restricted to the most outer shell of the sorbent.

Chromatography, Ion Exchange↗

Mechanism and kinetics of protein transport in chromatographic media studied by confocal laser scanning microscopy. Part I. The interplay of sorbent structure and fluid phase conditions.

An experimental study on the interplay of sorbent structure and fluid phase conditions (pH) has been carried out examining adsorption and transport of bovine serum albumin (BSA) and a monoclonal antibody (IgG 2a) on SP Sepharose Fast Flow and SP Sepharose XL. SP Sepharose Fast Flow is characterised by a relatively open pore network, while SP Sepharose XL is a composite structure with ligand-carrying dextran chains filling the pore space. Both adsorbents have similar ionic capacity. Protein transport and adsorption profiles were evaluated using confocal laser scanning microscopy. Under all investigated conditions, BSA uptake could be adequately explained by a pore diffusion mechanism. The adsorption profiles obtained for IgG 2a, however, indicated that changes in fluid phase conditions as well as a change in the solid phase structure could result in a more complex uptake mechanism as compared to pore diffusion alone. This mechanism results in a fast transport of proteins into the adsorbent, followed by an overshoot of protein in the center of the sorbent and a setback towards a homogeneous adsorption profile.

Adsorption↗

Dynamics of protein uptake within the adsorbent particle during packed bed chromatography.

A new experimental set-up for on-line visualization of the intra-particle uptake kinetics during packed bed chromatography has been designed and tested. Confocal laser scanning microscopy was used to analyze the dynamics of protein adsorption to porous stationary phases. In combination with this, a flow cell was developed that could be packed with chromatography media and operated as a fully functional mini-scale chromatography column. Adsorption profiles of single- and two-component mixtures containing BSA and IgG 2a during packed bed cation-exchange chromatography were investigated. The two proteins appear to exhibit different transport characteristics. For BSA a classical "shrinking core" behavior could be detected. The profiles obtained during IgG 2a adsorption point toward a different transport mode, which deviates from the classical pore-diffusion picture. For the two-component system, a superposition of the single-component profiles combined with a classical displacement of the weaker bound protein species was found. The results indicate that depending on the adsorbed protein the uptake can vary tremendously, even for adsorption to the same chromatographic support. It is clearly shown that the new microcolumn allows in situ quantitative investigations of protein adsorption dynamics within a single particle, which adds a new tool to the available methods for characterizing and optimizing protein adsorption chromatography.

Adsorption↗

Generation of equally sized particle plaques using solid-liquid suspensions.

A device is presented for the generation of equally sized plaques of sensitive particles in a 96-well format. The resulting particle plaques can be used for the measurement of adsorption isotherms and uptake kinetics in protein chromatography or for immobilization reactions. The particle plaques are formed from suspensions with a vacuum device that is designed as a reusable sandwich module. The particles are retained by a mesh while the solvent is removed by the vacuum. As most particles used for protein chromatography are sensitive to mechanical stress and dehydration, the vacuum device is gentle enough to allow the use of these particles, thus eliminating the uncertainty of slurry preparation and pipetting. Apparatus characteristics and preparation procedures are described precisely. The physical intactness of the particles after the preparation procedure is proved by microscopic analysis. Data on the uniformity of the obtained resin plaques with respect to the reproducibility of their adsorption performance is given. Finally, adsorption isothermal and kinetic data of BSA on an ordinary HIC system obtained by high-throughput measurements are shown as an application example.

Adsorption↗