請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/37438
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 鄭淑芬(Soofin Cheng) | |
dc.contributor.author | Chih-Chuan Huang | en |
dc.contributor.author | 黃智詮 | zh_TW |
dc.date.accessioned | 2021-06-13T15:28:10Z | - |
dc.date.available | 2013-07-21 | |
dc.date.copyright | 2008-07-21 | |
dc.date.issued | 2008 | |
dc.date.submitted | 2008-07-16 | |
dc.identifier.citation | 1. H. V. Bekkum, E. M. Flanigen, and J. C. Jansen, “Introduction to zeolite Science and Practice.” Elsevier, Amsterdam, (1991).
2. R. Szostak, “Molecular Sieves: Principles of Principles of Synthesis, and Identification.” Blackie Academic and Professional, London, (1998). 3. S. Inagaki, Y. Fukushima, and K. Kuroda, J. Chem. Soc., Chem. Commun., 680 (1993). 4. C. T. Kresge, M. E. Leonowicz, W. J. Roth, J. C. Vartulli, and J. S. Beck, Nature 359, 710 (1992). 5. J. S. Beck, J. C. Vartuli, W. J. Roth, M. E. Leonowicz, C. T. Kresge, K. D. Schmitt, C. T. W. Chu, D. H. Olson, E. W. Sheppard, S. B. McCullen, J. B. Higgins, J. L. Schlen, and J. E. Ker, J. Am. Chem. Soc. 114, 10834 (1992). 6. J. Y. Ying, C. P. Mehnert, and M. S. Wong, Angew. Chem. Int. Ed. Engl. 38, 56 (1999) 7. D. Zhao, J. Feng, Q. Huo, N. Melosh, G. H. Fredrickson, B. F. Chmelka, and G. D. Stucky, Science 279, 548 (1998). 8. D. Zhao, Q. Huo, J. Feng, B. F. Chomelka, and G. D. Stucky, J. Am. Chem. Soc. 120, 6024 (1998). 9. N. Husing, F. Schwertfeger, W. Tappert, and U. Schubert, J. Non-Cryst. Sol. 186, 37 (1995). 10. A. Corma, Q. Kan, M. T. Navarro, J. Perez-Pariente, and F. Rey, Chem. Mater. 9, 2123 (1997). 11. F. Marlow, M. D. McGehee, D. Zhao, B. F. Chmelka, and G. D. Stucky, Adv. Mater. 11 632 (1999). 12. M. H. Huang, A. Choudrey, and P. Yang, Chem. Commun. 1063 (2000). 13. Y. Han, J. M. Kim, and G. D. Stucky, Chem. Mater. 12, 2068 (2000). 14. Z. Liu, Y. Sakamoto, T. Ohsuna, O. Terasaki, C. H. Ko, H. J. Shin, and R. Ryoo, Angew. Chem. Int. Ed. 39, 3107 (2000). 15. C. H. Ko and R. Ryoo, Chem. Commun. 2467 (1996). 16. J. Liu, X. Feng, G. E. Fryxell, L. Wang, A. Y. Kim, and M. L. Gong, Adv. Mater. 10, 161 (1998). 17. J. Brown, L. Mercier, and T. J. Pinnavaia, Chem. Commun. 69 (1999). 18. S. Dai, M. C. Burleigh, Y. H. Ju, H. J. Gao, J. S. Lin, S. J. Pennycook, C. E. Barnes, and Z. L. Xue, J. Am. Chem. Soc. 122, 992 (2000). 19. Y. J. Han, G. D. Stucky, and A. Butter, J. Am. Chem. Soc. 121, 989 (1999). 20. D. Zhao, C. Yu, and H. Yang, Encyclopedia of Nanoscience and Nanotechnology. 7, 263 (2004) 21. S. Y. Chen, L. Y. Jang, and S. Cheng, Chem. Mater. 16, 4174 (2004). 22. B. Borgstrom, and C. Erlanson, Eur. J. Biochem. 37, 60 (1973). 23. C. Chapus, H. Sari, M. Semeriva, and P. Desnuelle, FEBS Lett. 58, 155 (1975). 24. A. Vandermeers, M. C. Vandermeers-Piret, S. Rathe, and J. Christophe, FEBS Lett. 49, 334 (1975). 25. Kraulis, P. J. J. Appl. Crystallogr., 24,946 (1991). 26. F. K. Winkler, A. D’Arcy, and W. Hunziker, Nature 343, 771 (1990). 27. H. Van Tilbeurgh, L. Sarda, R. Verger, and C. Cambillau, Nature 359, 159 (1992). 28. Y. Bourne, C. Martinez, B. Kerfelec, D. Lombardo, C. Chapus, and C. Cambillau, J. Mol. Biol. 238,709 (1994). 29. N. Mahe-Gouhier, and C. Leger, Biochim. Biophys. Acta. 962, 91 (1988). 30. A. Abousalham, C. Chaillan, B. Kerfelec, E. Foglizzo, and C. Chapus, Protein Eng. 5, 105 (1992). 31. H. Van Tilbeurgh, M. P. Egloff, C. Martinez, N. Rugani, R. Verger, and C. Cambillau, Nature 362, 814 (1993). 32. M. P. Egloff, F. Marguet, G. Buono, R. Verger, C. Cambillau, and H. Van Tilbeurgh, Biochemistry 34, 2751 (1995). 33. C. Withers-Martinez, F. Carriere, R. Verger, D. Bonrgeois, and C. cambillau, structure, 4, 1363 (1996). 34. M. P. Egloff, L. Sarda, R. Verger, C. Cambillau, and H. Van Tilbeurgh, Protein Sci. 4, 44 (1995). 35. S. Granon, Biochim. Biophys. Acta 874 (1986). 36. C. Chaillan, E. Rogalska, C. Chapus, and D. Lombardo, FEBS Lett. 257, 443 (1989). 37. C. Chaillan, E. Rogalska, C. Chapus, and D. Lombardo, FEBS Lett. 257, 443 (1989). 38. D. Yu, Z. Wang, L. Zhao, Y. Cheng, S. Cao, J. Mol. Catal. B: Enzymatic, 48, 64 (2007). 39. J. F. Diaz, J. K. Balkus, J. Mol. Catal. B:Enzym. 2, 115 (1996). 40. Y. X. Bai, Y. F. Li, Y. Yang, L. X. Yi, Process Biochem. 41, 770 (2006). 41. C. Lei, J. Am. Chem. Soc. 124, 11242 (2000). 42. P. Wang, and F. Caruso, Chem. Mater. 17, 953 (2005). 43. M. I. Kim, J. Kim, J. Lee, H. Jia, H. B. Na, J. K. Youn, J. H. Kwak, A. Dohnalkova, J. W. Grate, P. Wang, T. Hyeon, H. G. Park, H. N. Chang, Biotech. and Bioeng. 96, 2, 210 (2007). 44. A. Vinu. V. Murugesan, M. Hartmann, J. Phys. Chem. B 108,7323 (2004). 45. P. Jörg, T. Jürgen, S. Murielle, K. Heike, Soil Biology & Biochemistry 39,877 (2007). | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/37438 | - |
dc.description.abstract | 在合成溶液中藉由加入少量鋯(IV),可以合成出短通道之SBA-15。此外,變化合成中之水熱溫度,合成出三種不同孔徑之SBA-15 (7 nm, 8 nm, 9.2 nm),並且在孔洞材料上修飾各種不同官能基,例如,苯基、丙基硫、羧基、丙基胺和辛基。上述之孔洞材料皆用來當作解脂酵素(來自猪的胰臟)的載體,使解脂酵素固定在上面。
實驗結果發現,越大孔徑之SBA-15,對解脂酵素有越快的吸附效果。改變固定解脂酵素之pH 值發現,pH 為5 時,較適合含苯基、丙基硫、和羧基之SBA-15吸附解脂酵素,而pH 為7.4 時,較適合含丙基胺之SBA-15 吸附解脂酵素。在催化三乙酸甘油酯方面,自由解脂酵素在pH 為7.4 下活性最好,並且可以藉由再加入疏水之甲苯增加約1 倍的活性。 固定解脂酵素後之SBA-15,有著最高活性之材料為含丙基胺和辛基之SBA-15,在pH 為7.4 下催化三乙酸甘油酯水解,保有自由解脂酵素活性的五分之四。可能的原因為,丙基胺較不容易讓解脂酵素的結構變形而導致失活。此外,辛基為疏水性之官能基,三乙酸甘油酯較容易接近解脂酵素的活性中心。 | zh_TW |
dc.description.abstract | Short-channel SBA-15 with three different pore diameters (7.0, 8.2, and 9.2 nm) were synthesized by hydrothermal reaction at different temperatures with the aid of a
small amount of Zr(IV) in the synthesis solution. The mesoporous silica with various functional groups including phenol, thio, carboxylic acid, amino, and octyl were also prepared. They were used as the supports for lipase (from porcine pancreas) immobilization. The large pore facilitated the adsorption of the enzyme. The optimal pH value for immobilization of lipase changed with the functional groups, and pH 5 is the best for pure siliceous SBA-15 and those functionalized with phenol, thiol, and carboxylic acid while pH 7.4 is the best for amino functionalized SBA-15. In catalytic hydrolysis of triacetin, highest catalytic activity was achieved at pH 7.4 and in the presence of a small amount of hydrophobic co-solvent. Among the functionalized SBA-15 materials, the one functionalized with amino or octyl groups gave the highest catalytic activity. It is attributed to the amino group could keep in lipase at pH 7.4 through the electrostatic interaction and the octyl group facilitates the approach of triacetin to the active sites of lipase. | en |
dc.description.provenance | Made available in DSpace on 2021-06-13T15:28:10Z (GMT). No. of bitstreams: 1 ntu-97-R95223050-1.pdf: 2959102 bytes, checksum: a9e4b81711d86daab9b0459a6f2f08c9 (MD5) Previous issue date: 2008 | en |
dc.description.tableofcontents | 第一章 緒論…………………………………………………………………………..1
1.1介孔材料簡介……………………………………………………………………..1 1.2介孔材料相(the phase of mesoporous materials)之控制…………………………6 1.3外形(Morphology)之控制…………………………………………………………7 1.4孔洞尺寸之控制…………………………………………………………………..8 1.5解脂酵素的簡介…………………………………………………………………..9 1.6酵素固定的簡介…………………………………………………………………12 1.7 動機……………………………………………………………………………...17 第二章 實驗部分……………………………………………………………………18 2.1化學藥品…………………………………………………………………………18 2.2介孔材料之製備…………………………………………………………………19 2.3 Bradford法定量酵素濃度……………………………………………….………23 2.4利用氣相層析儀(Gas Chromatograph ; GC)測定解脂酵素的活性…….………25 2.5測試高溫使解脂酵素失活………………………………………………………26 2.6 自由解脂酵素(Free lipase)的活性測試…………………………………….…..26 2.7 甲苯對自由解脂酵素的活性測試……………………………………….……..26 2.8 放置時間對解脂酵素活性的影響…………………………………………..….27 2.9 解脂酵素吸附到孔洞材料的時間……………………………………………...27 2.10 解脂酵素固定到孔洞材料…………………………………………………….27 2.11 固定後孔洞材料的活性測試……………………………………………...…..28 2.12 固定後孔洞材料的重複使用性…………………………………………...…..28 2.13固定後孔洞材料的耐熱度……………………………………………………..28 2.14 樣品的鑑定與分析…………………………………………………...………..29 第三章 結果與討論……………………………………………………………...….34 3.1 介孔材料結構鑑定與分析…………………………………………………..….34 3.1.1 XRD…………………………………………………………………………34 3.1.2 氮氣吸附-脫附等溫曲線……………………………………………..…….42 3.1.3 TGA…………………………………………………………………….……54 3.1.4 掃描式電子顯微鏡(SEM)…………………………………………...……..61 3.1.5 穿透式電子顯微鏡(TEM)………………………………………...………..66 3.1.6 Fourier Transform Infrared Spectroscopy (FT-IR)…………………………..69 3.1.7 近場X光吸收光譜(XANES)………………………………………….…..72 3.2 自由解脂酵素活性測試…………………………………………………….…..75 3.2.1 氣相層析儀之測量…………………………………………………………75 3.2.2 測試高溫使解脂酵素失活…………………………………………………77 3.2.3 自由解脂酵素的活性測試……………………………………………...….78 3.2.4 甲苯對自由解脂酵素的活性測試……………………………………..…..80 3.2.5 放置時間對解脂酵素之影響………………………………………...…….82 3.2.6 解脂酵素與介孔材料之介面電位…………………………………………83 3.2.7 解脂酵素吸附到孔洞材料的時間…………………………………………85 3.2.8 固定後孔洞材料的活性測試……………………………………..………..91 3.2.9 固定後孔洞材料的重複使用性……………………………………………96 3.2.10 固定後孔洞材料的耐熱度……………………………………………..…97 第四章 結論……………………………………………………………………...….98 參考文獻…………………………………………………………………………..100 附錄…………………………………………………………………………………103 | |
dc.language.iso | zh-TW | |
dc.title | 解脂酵素固定在不同官能基及孔徑之短通道介孔材料SBA-15上的應用與鑑定 | zh_TW |
dc.title | Immobilization of Lipase in Short-channel Mesoporous
SBA-15 Functionalized with Different Groups and Pore Diameters | en |
dc.type | Thesis | |
dc.date.schoolyear | 96-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 陳昭岑(Chao-Tsen Chen),張文章(Wen-Chang Chang) | |
dc.subject.keyword | 解脂酵素,三乙酸甘油酯,官能基,孔徑, | zh_TW |
dc.subject.keyword | lipase,triacetin,functionalized,pore size, | en |
dc.relation.page | 104 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2008-07-17 | |
dc.contributor.author-college | 理學院 | zh_TW |
dc.contributor.author-dept | 化學研究所 | zh_TW |
顯示於系所單位: | 化學系 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-97-1.pdf 目前未授權公開取用 | 2.89 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。