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Study on the Mass Transfer Process of Mambrane Crystallization of Protein

Author: SongHengKai
Tutor: LiuLiYing
School: Beijing University of Chemical Technology
Course: Chemical Engineering
Keywords: Film crystallization Protein Transmembrane flux Overall mass transfer coefficient
CLC: Q51
Type: Master's thesis
Year: 2009
Downloads: 66
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Abstract


With the development of recombinant DNA technology and the perfection of the expression system, greatly increase the number of known protein. Determine the protein structure of the research you have mentioned on the agenda, X-ray diffraction to determine the most effective method of protein structure, and application of X-ray crystallography, macromolecular crystals have a large enough size (greater than 0.1mm) and perfect quality. to obtain accurate diffraction data. However, many macromolecular crystallography is often difficult to grow, generally small molecule crystallization methods are not suitable for the growth of macromolecular crystals. Therefore, the perfect quality protein crystals become a major bottleneck for protein structure determination, crystals need to explore new crystallization method for the preparation of proteins and other biological macromolecules. Protein crystals suitable for diffraction analysis of a large size can be obtained with the film crystallization technology crystallization protein. Polyvinylidene fluoride (PVDF), the hollow fiber membrane lysozyme static film crystallization process experimental study investigated the concentration of the precipitating agent, the eluent concentration and crystallization solution protein of the initial concentration of the film crystallization process. The results show that: the solvent transmembrane flux increases with decreasing the concentration of precipitating agent; cause a higher solvent transmembrane flux of the high eluent concentration in the beginning of the experiment, and the transmembrane flux of the solvent in the experimental process used decreased rapidly; solvent transmembrane flux with lysozyme initial concentration decreases. Combined with lysozyme crystal size distribution and crystal microscope, to obtain the optimum operating conditions for the precipitating agent has a NaCl concentration of 4% (w / v), the eluent mM MgCl 2 concentration of 20% (w / v), lysozyme initial concentration of 20mg/ml. Lysozyme dynamic membrane crystallization process research investigated the crystallization solution and eluent flow rate of film crystallization process solvent transmembrane flux and overall mass transfer coefficient. The results show that: under various operating conditions, the flux and the overall mass transfer coefficient of the solvent transmembrane As the experiment progresses, continuously decreases, and the flow rate of the greater reduced faster; small flow rate of the larger crystal size the number; flow rate is small crystal a small number of larger size, but prone to injury; dynamic membrane crystallization process, the mass transfer resistance of the membrane on both sides of the interface at a similar level, and the crystallization solution side of the resistance is slightly larger than the elution The liquid-side mass transfer resistance. In addition, the study of bovine serum albumin static film crystallization process, temperature and initial membrane area of ??film crystallization process. The results show that: within the scope of the experiment, the solvent transmembrane flux increases with the decrease of the initial membrane area; smaller transmembrane flux solvent at low temperature, the crystallization induction time of the solution is also longer; 15 ° C under the film is crystallized the bovine serum albumin obtained in crystal shape is fixed, the large size and uniform, suitable for X-ray diffraction analysis.

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CLC: > Biological Sciences > Biochemistry > Protein
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