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| 研究生： |
翁郁婷 Yu-ting Weng |
|---|---|
| 論文名稱： |
次微米高分子粒子與蛋白質混和溶液之交互作用 Interactions between Submicron Polymer Particles and Binary Proteins |
| 指導教授： |
陳崇賢
Chorng-Shyan Chern |
| 口試委員: |
戴子安
Chi-An Dai 李振綱 Cheng-Kang Lee |
| 學位類別： |
碩士 Master |
| 系所名稱： |
工程學院 - 化學工程系 Department of Chemical Engineering |
| 論文出版年： | 2007 |
| 畢業學年度： | 95 |
| 語文別： | 中文 |
| 論文頁數： | 80 |
| 中文關鍵詞： | 雙蛋白質混和溶液 、等電點 、疏水作用力 、靜電交互作用力 |
| 外文關鍵詞： | Binary proteins, Isoelectric point, Hydrophbic force, Electrostatic interaction |
| 相關次數： | 點閱：233 下載：8 |
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本研究以甲基丙烯酸甲酯（MMA）為疏水性單體，並以過硫酸鈉作為起始劑，HS-10作為界面活性劑，以乳化聚合反應合成乳漿粒子，而這些次微米粒子的表面具有-SO4- 及-SO3- 官能基，因此即使是在不同的pH之下，其粒子表面仍帶負電，故具有對pH較不敏感的特性。
在不同pH值之下，單一BSA及Lysozyme蛋白質溶液對乳漿粒子均會在其等電點的附近有最大吸附量，而在雙蛋白質混合溶液中，則會在pH = 7∼8之間有最大的總吸附量，推測有可能是Lysozym會先吸附在膠體粒子的表面，使得膠體粒子的表面因為Lysozym的關係而呈現正電性的分布，再進而藉由BSA與Lysozym之間的靜電交互吸引作用力而造成BSA的吸附量增加，亦有可能是Lysozym會因為靜電吸引作用力的關係而先與BSA連結在一起，之後再由於Lysozym表面所帶有的正電荷而再與膠體粒子產生靜電吸引力，使得混和後蛋白質總吸附量在pH = 7∼8之間時，有一最大的吸附量。在 pH = 4∼5之間，隨著溶液中離子強度的增加而使得粒子與蛋白質之間的靜電作用力下降，且由於pH值在BSA的等電點附近，此時BSA 具有較強的疏水作用，而此疏水作用力較此時Lysozym的靜電吸引作用力來得強，故使得混和溶液中BSA的吸附量較為單一BSA的吸附情形來得好，而在 pH = 10∼10.5之間時，隨著溶液中離子強度的增加，由於此時Lysozyme的疏水作用力會相較BSA微弱，故會造成混合溶液中BSA受到Lysozyme的影響而使其吸附量增加。
Submicron polymer particles were prepared by emulsion polymerization with methyl methacrylate (MMA) as the hydrophobic monomer, sodium persulfate as the initiator, and HS-10 as the surfactant. These particle surfaces have sulfate groups (-SO4-) and sulfonate groups (-SO3-) at the same time. Therefore, they are relatively insensitive to changes in pH.
The adsorption of binary proteins (BSA and lysozyme) on the particles was studied. Isothermal adsorption of binary proteins onto the particles leads to changes in the zeta potential, particle size and turbidity. At the low ionic strength, the total maximum protein adsorption occurs in the pH range of 7－8. This may well be due to lysozyme adsorption onto the particles first and this will result in increased net negative charge particles and therefore promote the adsorption of BSA. Another reason is that BSA and lysozyme have opposite net charges, they’ll aggregate with each other first by electrostatic attraction forces. Then electrostatic attraction forces between lysozyme of the binary proteins mixture and submicron latex particles bring about the enhanced total adsorbed amount.
1. 徐治平, 林天賜, 化工, 第45卷, 第2期, 14 (1998).
2. V. K. LaMer, J. Colloid Sci., 19, 291, (1964).
3. M. W. Thompson, “Polymer Colloids”, R. Buscall, T. Corner, J. F. Stageman(Ed), 1-43, (1985).
4. D. Myers, “Surfaces Interfaces and Colloids : Principles and Applications”, 214-248, (1999).
5. T. Satsuo, R. Ruch, “Stabilization of Colloidal Dispersion by Polymer Adsorption”, T. Satsuo, R. Ruch(Ed),New York, 65-119, (1980).
6. H. Tamai, A. Fujii, T. Suzawa, “Colloidal Stability of Polymer Latices Coated with Bovine Serum Albumin”, J. Colloid and Interface sci., 118, 176-181, (1987).
7. R. J. Hunter (Ed.), “ Zeta Potential in Colloid Science”, Academic Press, London, (1981).
8. D. J. Shaw (Ed.), “ Introduction to Colloid & Surface Chemistry 4/E”, Butterworth, Heinemann Press, (1992).
9. 蘇家豪, 碩士論文, 國立成功大學化學工程研究所, (2003).
10. R. J. Hunter (Ed.), “Zeta Potential in Colloid Science”, Academic Press, London, (1981).
11. Boyer, R.F., “Chapter 5：Protein architecture and biological function”, in Biochemistry, Brooks/Cole Publishing Company, (1999).
12. Nölting, B., “Chapter 3 : Physical interaction that determine the properties of protein” , in Protein Folding Kinetic, Springer-Verlag Berlin Heidelberg, New York, (1999).
13. Campbell, M. K., “Chapter 4：The three-dimensional structure of protein”, in Biochemistry, Campbell, M. K.,Saunders College Publishing, (1995).
14. Fleming, A., “On a remarkable bacteriolytic element found in tissues and secretions”, Proc. Roy. Soc. Lond.,B93,306, (1922).
15. Proctor, V. A., and Cunningham, F. E. “The chemistry of lysozyme and its use as a food preservative and a pharmaceutical”, CRC Crit. Rev. Food Sci. Nutr.,26,359, (1988).
16. Rothwarf, D. M., and Scheraga, H. A. “Role of non-native and hydrophobic interactions in the folding of hen egg white lysozyme”, Biochemistry., 35, 13797, (1996).
17. Berges, H., Kassab, E., Conte, D., Adjadj, E., and Houee-Levin, C. “Ab-Initio calculations on arginine-disulfide complexes modeling the one-electron reduction of lysozyme. comparison to an experimental reinvestigation.”, J. Phys. Chem., 101, 7809, (1997).
18. Hamaguchi, K. “Conformation and enzymatic activity of lysozyme”, Tampakushitsu. Kakusan Kosa., 13, 98, (1968).
19. Jr Peters T, Serum albumin, Adv Protein Chem., 37, 161-245, (1985).
20. Foster, J. F. Albumin Structure, Function and Uses, 53-84. Pergamon, OxfordFoster, (1977)
21. Duracher, R. Veyret, A. Elaissari, C. Pichot,”Adsorption of Bovine Serum Albumin Protein onto Amino-Containing Thermosensitive Core-Shell”, Polym Int., 53, 618-626, (2004).
22. D. Andrade, “Surface and Interfacial Aspects of Biomedical Polymers--v.2 Protein Adsorption”, 1-80, (1985).
23. Suzawa, T. Murakami, “Adsorption of Bovine Serum Albumin on Synthetic Polymer Latices”, J. Colloid and Interface sci., 266-268, (1980).
24. R. K. Scopes, “Protein Purification : Principles and Practice”, 41-71,(1987).
25. H. Shirahama, T. Suzawa, “Adsorption of Bovine Serum Albumin onto Styrene/2-Hydroxyethyl Methacrylate Copolymer Latex”, J. Colloid and Interface sci., 416-421, (1985).
26. H. Shirahama, K. Takeda, and T. Suzawa, “Adsorption of Bovine Serum Albumin onto Polystyrene Latex : Effects of Coexistent Electrolyte Anions”, J. Colloid and Interface sci., 552-556, (1986).
27. T. Suzawa, H. Shirahama, and T. Fujimoto, “Effect of Urea on the Adsorption of Bovine Serum Albumin onto Polymer Latices”, J. Colloid and Interface sci., 498-503, (1983).
28. M. van der Veen, N. Willem, M. C. Stuart, “Electrostatic interactions in protein adsorption probed by comparing lysozyme and succinylated lysozyme”, Colloids and Surfaces B : Biointerfaces., 33-40, (2004).
