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| ???org.dspace.app.webui.jsptag.ItemTag.dcfield??? | Value | Language |
|---|---|---|
| dc.contributor.author | 譚建安 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:13:50Z | - |
| dc.date.available | 2021-07-01T08:13:50Z | - |
| dc.date.issued | 1984 | |
| dc.identifier.citation | Reference 1. Buchanan, R. E. and N. E. Gibbons, 1974. Bergey’s Manual of Determinative Bacteriology, 8th. ed. The Williams and Wilkins Co., Baltimore. 2. Buonocore, V., C. Capovale, M. Rosa and A. Gambcorta, 1976. J. Bacteriol., 128: 515-521. 3. Campbell, L. L., 1955. Arch. Biochem. Biophys., 54: 154-161. 4. Campbell, L. L. and P. D. Cleveland, 1961. J. Biol. Chem., 236: 2966-2969. 5. Campbell, L. L. and G. B. Manning, 1961. J. Biol. Chem., 236: 2962_2965. 6. Chandra, A. K., S. Medda and A. K. Bhadra, 1980. J. Ferment. Technol., 58. 1-10. 7. Coleman, G. and W. H. Elliott, 1962. Biochem. J., 83. 256-263. 8. Coleman, G. and M. A. Grant, 1966. .Nature, 211: 306-307. 9. Cornelis, P., A. Digneffe and K. Willemont, 1982. Mol. Gen. Genet., 186: 507-511. 10. Dawes, C. J., 1979. Biological Techniques for Transmission and. Scanning Blectron Microscopy. p.p. 205-206. The Offset Hause So., Burlington, Vt. 11. De Pinto, J. A. and L. L. Campbell, 1968.Biochemistry, 7: 114-120. 12. Erickson, R. J. 1976. Froduction of Industry Enzymes, in “Microbioloy Schlessinger, D. (ed.) Am. Soc. Microbiol., washington, D.C. 13. Fisher,E. H. and E. A. Stein, 1960. alpha-amylase, in “The Enzyme” Vol. 4, 2nd.ed. Boyer, P. D., H. Lardy and M. Myrback, (ed.) p.p. 313-340. Academic Press Inc. New York. 14. Forgarty, W. M., P. J. Griffin and A. M. Joyce, 1974. Process Hiochem., 9: 11-24. 15. Fukumoto, J., T. Yamamoto and D. Tsuru, 1957. Intern. symp. Enzyme Chem., Tokyo, Kyoto, p.p. 365-310. 16. Fuwa, H., 1954. J. Biochem. (Tokyo) 41: 583-603. 17. Horikoshi, K., 1971. Agri. Biol. Chem., 35: 1783-1791. 18. Ingle, .M. B. and R. J. Erickson, 1978. Adv. Appl. Microbiol. 24. 257-278. 19. Krishnan, T. and A. K. Chandra, 1983. Appl. Environ. Microbiol., 46: 430-437. 20. Lowry, A., N. J. Rosenbrough, A. L. Farr and R. J. Randall 1951. J. Biol. Chem., 193: 265-275. 21.Mantsala, P. and H. Zalkin, 1979. J. Biol. Chem., 24: 8540-547. 22. Manning, G. B. and L. L. Campbell, 1961. J. Biol. Chem. 236: 2952-2957. 23. Manning, G. .., L. L. Campbell and R. J. Foster, 1961. J. Biol. Chem., 236. 2958-2961. 24. Markovitz, A., H. P. Klein and E. H. Fisher, 1956. Biochem. Eiophys. Acta., 19: 267-273. 25. McWethy, S. J. and P. A. Hartman, 1977. J. Bacteriol., 129: 1537-1544. 26. Medda, S. and A. K. Chandra, 1980. J. Appl. Bacteriol., 48: 47-58. 27. Miller, B. M. and Litsky, 1976. Industrial Microbiology, p.p. 130-135. McGraw-Hill, New York. 28. Morgan, F. J. and F. G. Priest, 1981. J. Appl. Bacteriol. 50: 107-114. 29. Mulin, G. J. and P. Galzy, 1979. Agri, .Biol. Chem., 43: 1165-1171. 30. Nagata, Y. K., K. Yamaguchi and B. Maruo, 1974. J. Bacteriol., 119: 425-430. 31. Nitta, Y., N. M. Mizushima, K. Hiromi and S. Ono, 1971. J. Biochem., (Tokyo) 69: 567-576. 32. Nomura, M., B. Maruo and S. Akbori, 1956. J. Biochem., (Tokyo) 43: 143-152. 33. Ogasahara, K., K. Yatani, A. Imaniski and T. Isemura, 1970. J. Biochem., (Tokyo) 67: 83-89. 34. Qishi, M., H. Takahashi and B. Maruo, 1963. J. Bacteriol., 85: 246-249. 35. Olavarria, J. M. and M. Torres, 162. J. Biol. Chem., 237: 1746-1751. 36. Onishi, H. and K. Sonoda, 1979. Appl. Environ. Microbiol., 38: 616-620. 37. Palva, I., 1982. Gene, 19: 81-87. 38. Robyts, J. F. and W. J. he1an, 1968. The Alpha-amylase, in “Starch and its Derivatives” 4th. ed. Radley, J. A., (ed.) p.p. 430-476. Chapman and Ha1l Ltd., London. 39. Saito, N., 1973. Arch. Biochem. Biophys., 155: 290-298. 40. $aito, N. and K. Yamamoto, 175. J. Bacteriol., 121: 848-856. 41. Schimmer, S. and A. K. Balls, 1949. J. Biol. Chem., 180: 883-894. 42. Scott, D., 1975. in ‘Enzyme in Food Processing’ 2nd. ed. Reed, G., (ed.) p.p.5C5-508. Academic Press Inc., New York. 43. Singleton, R. Jr. and B. E. Amlunxen, 1973. .Bacteriol. Rev., 37: 320-342. 44. Shimizu, M., M. Kanno, M. Tamura and N. Suekane, 1978. Agri. Biol. Chem. 42: 1681-1688. 45. Stein, E. A. and E. H. Fisher, 1958. J. Biol. Chem., 232: 867-879. 46. Taniguchi, H., C. M. Jae, N. Yoshigi and Y. Maruyama, 1983. Agri. Biol. Chem., 47: 511-519. 47. Toda, H. and K. Narita, 167. J. Biochem., (Tokyo) 62: 767-768. 4. Tsuchi, H. M., J. Corman and H. J. Koepsell, 1950. Cereal. Chem., 27: 322-328. 49. Tsukagoshi, N. H. Ihara, H. Yamagata and S. Udaka, 1984.Vol. Gen. Genet., 193: 58-63. 50. Vallee, S. L., E. A. Stein, W. M. Summerwell and E. D. Fisher, 1959. J. Biol. Chem., 234: 2901-2905. 51. Welker, N. E. and L. L. Campbell, 1967. J. Bacterial., 94: 1124-1130. 52. Yoneda, Y., K. Yamane and B. Naruo, 1973. Biochem. Biophys. res. Commun., 50: 75-770. 53. 王孟群, 1983,實用微生物學實驗。九州圖書文物有限公司。 54. 台灣省煙酒公賣局，1983，啤酒分析法。酒類實驗所化驗系編印。 55. 蘇遠志、劉文雄、羅其濡、1974，紅?菌學及應用之研究。六十三年度酒廠年報。p.p103~127 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75553 | - |
| dc.description.abstract | 中文摘要 由土壤分離出一株能產生對熱穩定之澱粉液化?的細菌，經鑑定並命名為Bacillus licheniformis 7。此一菌株生產澱粉液化?所需條件為50℃培養七天。此菌株在以Starch 2.5%,FeCl3-6H2O 0.05%， peptone 0.35%, yeast extract 0.6%，Na-citrate 0.2%，CaCl2.2H2O 0.008% 作培養基時，可獲得最佳酵素產量，產生之澱粉液化?經四個步驟純化，可純化26倍，回收率為21% ，純化酵素最適作用PH為9.0，最適作用溫度為90℃, PH6~9時很穩定。Hg+, Zn++，Mg++, Ni++, Mn++ 等金屬離子對酵素作用有抑制作用，而Na十，Fe+++, Cu++，Ba++ 則有促進作用，化學藥品K2MnO4之添加有抑制酵素活性之作用，2-Mercaptoethanol則可以促進酵素活性。 | zh_TW |
| dc.description.abstract | ABSTRACT A thermostable alpha-amylase producing bacteria has been isolated from soil and identified as Bacillus licheniformis. 7.Cultural conditions of this strain for alpha-amylase production were studied. The optimum temperature and incubation period for enzyme production were 50°C and 7 days respectively. Starch with a concentration of 2.5% was the best carbon source for enzyme production. Beside the above components, the addition of FeCl3.6H2O 0.05%, yeast extract 0.6%, peptone 0.35%, Na-citrate 0.2% and CaCl2.2HO 0.008% to the incubation medium could produce maximum enzyme activity. The enzyme was purified 26-fold with 21% recovery by a series of four steps. The purified enzyme showed maximal activity at 90℃ and pH9.0.91% of this activity remained at 97℃, even at 110℃, there was still 45% activity remained. The enzyme showed 100% stability at 40°C-70°C. Of the cations, Ba2+ Cu2+ Fe3+ Na+ showed stimulatory effect; whereas Hg2+, Mg2+, Mn2+, Ni2+, Zn2+ were inhibitory. K2MnO4 addition resulted in the complete loss of enzyme activity; whereas 2-Mercaptoethanol afforded protection of the enzyme activity. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:13:50Z (GMT). No. of bitstreams: 0 Previous issue date: 1984 | en |
| dc.description.tableofcontents | 目錄 I、緒言• • • • • • • • • • • • • • • • 1 II、材料與方法• • • • • • • • • • • • • • • • 5 III、結果• • • • • • • • • • • • • • • • 12 一、澱粉液化?生產菌的分離及鑑定• • • • • • • • • • • • • • • • 12 二、保存用培養基對酵素生產的影響• • • • • • • • • • • • • • • • 19 三、培養條件的探討• • • • • • • • • • • • • • • • 21 四、培養基組成對酵素生產之影響• • • • • • • • • • • • • • • • 25 五、酵素之部份純化• • • • • • • • • • • • • • • • 35 六、部份純化酵素之特性• • • • • • • • • • • • • • • • 37 VI、討論• • • • • • • • • • • • • • • • 52 V、參考資料• • • • • • • • • • • • • • • • 60 | |
| dc.language.iso | zh-TW | |
| dc.title | Bacillus Iicheniformis 7 的細胞外耐熱性澱粉液化酵素 | zh_TW |
| dc.date.schoolyear | 73-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 68 | |
| dc.rights.note | 未授權 | |
| dc.contributor.author-dept | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 植物科學研究所 | zh_TW |
| Appears in Collections: | 植物科學研究所 | |
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