:::

| | | | | | 第 | | 筆

詳目顯示區塊

第 20 筆
| (以作者名查詢海洋大學圖書館館藏系統)
| (以作者名查詢全國圖書書目資訊網)
| (以作者名查詢全國博碩士系統)
論文名稱: | Aeromonas salmonicida MAEF108 菌株所產洋菜酶的純化與性質之探討
| Studies on Purification and Properties of Agarases from Aeromonas salmonicida MAEF108
研究生: | 陳姿元 Tze-Yuan Chen
指導教授: | 潘崇良 Chorng-Liang Pan
學位類別: | 碩士
學校名稱: | 國立臺灣海洋大學
系所名稱: | 食品科學系
學號: | M93320019
畢業學年度: | 94
語文別: | 中文
關鍵字: | 洋菜酶 agarase
| 純化 purification
| 高效能液相層析法 HPLC
全文點閱次數: | 12

全文影像連結:

論文全文(pdf)

論文頁數: | 108
摘要: | Aeromonas salmonicida MAEF108 為一株具有分解洋菜能力的海洋細菌。將此菌於 MMB-MAEF108 培養液中振盪培養 (20oC、240 rpm) 24 hr，收集離心去除菌體後之培養液，進行洋菜酶的分離與純化。首先，培養液經濃縮透析後之比活性為 2225.10 AU/mg，純化倍數為 2.32倍，回收率為 24.66%；再以 DE-52 離子交換樹脂層析，可分離出三個具分解洋菜能力的蛋白質波峰劃分區域，個別收集後命名為 MAEF108-agarase Ι、ΙΙ、及 ΙΙΙ，其比活性分別為 855.35 AU/mg、174.47 AU/mg、及 1069.46 AU/mg，純化倍數分別為 0.89 倍、0.18 倍、及 1.11 倍，回收率分別為 4.97%、0.27%、及13.32%。MAEF108-agarase Ι 在經第二次 DE-52 離子交換樹脂層析及 Bio-Gel P-100 膠體過濾層析其純化後之比活性為 233.49 AU/mg、純化倍數為 0.24 倍、以及回收率為 0.40%。
| MAEF108-agarase Ι 的最適作用 pH 值為 6.0 或 7.5-8.0，最適作用溫度為 45oC，但是於40oC 下反應 60 min 活性減少 50%。MAEF108-agarase ΙΙ 的最適作用 pH 值為 5.0 或 7.5，最適作用溫度為 45oC，於 50oC 下反應 20 min 後活性幾乎喪失，於其他溫度下反應 60 min 後活性減少 50% 以上。MAEF108-agarase ΙΙΙ 的最適作用 pH 值為 6.0 或 7.5，最適作用溫度為 45oC，於其他各溫度反應 60 min 活性均下降至 60% 以下。MAEF108-agarase Ι、ΙΙ、及 ΙΙΙ 以 high-melting-point agarose 為基質時所表現之基質特異性活性最佳 (分別可產相當於 3.76、2.17、9.46 mg D-galactose)。且此三種洋菜酶皆不能分解 □ι-carrageenan 和 □κ-carrageenan。利用 MAEF108-agarases、MAEF108-agarase Ι、ΙΙ、或 ΙΙΙ 水解中性洋菜，經 HPLC 分析水解產物發現水解產物可能是分子量小於半乳糖之單醣或介於半乳糖與乳糖間之醣類。利用 MAEF108-agarase Ι、ΙΙ、或 ΙΙΙ 水解新洋菜六糖 (neoagarohexaose)，經 HPLC 分析產物發現水解產物可能是分子量小於半乳糖之單醣或介於半乳糖與乳糖間之醣類。
|
| Aeromonas salmonicida MAEF108 is a marine bacterium, which has the ability to degrade agar.  Strain MAEF 108 was grown at 20oC for 24 hr in MMB-MAEF108 broth with shaking speed of 240 rpm.  Collected crude enzymes after removing the cells then to proceed separation and purification of the agarases.  First, after concentrated and dialysed the specific activity, purification fold, and yield of the resulted solutions were 2225.10 AU/mg, 2.32 fold, and 24.66%, respectively.  Chromatographed with DE-52 gel achieved the separation of three agarases in the concentrated and dialysised broth, they are named MAEF108-agarase Ι, ΙΙ, and ΙΙΙ, by their agarase activities in each group of eluted fractions.  The following properties of these Ι, ΙΙ, and ΙΙΙ agarases were: specific activity, 855.35, 174.47, and 1069.46 AU/mg; purification fold, 0.89, 0.18, and 1.11 fold; and yield, 4.97%, 0.27%, and 13.32%, respectively.  MAEF108-agarase Ι was purified further by second DE-52 and then Bio-Gel P-100 chromatographs.  The final purified MAEF108-agarase Ι showed its specific activity, purification fold, and yield were 233.49 AU/mg, 0.24 fold, and 0.40%, respectively.
| The optimum pH for MAEF108-agarase Ι was found to be 6.0 or 7.5-8.0.  The optimum temperature for MAEF108-agarase Ι was 45oC, but approximately 50% of the enzyme activity was inactivated in 60 minutes under 40oC.  The optimum pH for MAEF108-agarase ΙΙ was found to be 5.0 or 7.5.  The optimum temperature for MAEF108-agarase ΙΙ was 45oC, but almost inactivated in 20 minutes under 50oC and more than 50% of the enzyme activity was inactivated after exposure to the rest tested temperature.  The optimum pH for MAEF108-agarase ΙΙΙ was found to be 6.0 or 7.5.  The optimum temperature for MAEF108-agarase ΙΙΙ was 45oC, but more than 60% of the enzyme activity was inactivated while stand 60 minutes under the rest tested temperature.  The best substrate specificity activities of MAEF108-agarase Ι, ΙΙ, and ΙΙΙ toward high-melting-point agarose were produced equivalent 3.76, 2.17, and 9.46 mg D-galactose, respectively.  MAEF108-agarase Ι, ΙΙ, and ΙΙΙ did not have the capability to degrade □ι-carrageenan and □κ-carrageenan.  Hydrolytic products of agarose digested by MAEF108-agarases, MAEF108-agarase Ι, ΙΙ, or ΙΙΙ were analyzed by HPLC, and the results showed that they could be monosaccharides, which molecular weight were smaller than galactose, and disaccharides, which molecular weight were between galactose and lactose.  Hydrolytic products of neoagarohexaose digested by MAEF108-agarase Ι, ΙΙ, or ΙΙΙ were analyzed by HPLC.  The products examined could be monosaccharides, which molecular weight were smaller than galactose, and disaccharides, which molecular weight were between galactose and lactose.
|
論文目次: | 目錄  -i-
| 圖目錄  -v-
| 表目錄  -vii-
| 附錄  -viii-
| 中文摘要  -ix-
| Abstract  -xi-
| 壹、前言  -1-
| 貳、文獻整理  -3-
| 一、Agarose 的構造與特性  -3-
| 二、洋菜酶生產菌株及其分離來源  -4-
| 三、洋菜酶對洋菜水解的作用機制  -4-
| 四、洋菜酶分解海藻寡多醣之產物  -5-
| 五、洋菜酶之生化特性  -5-
| 5.1 溫度和 pH 值  -5-
| 5.2 分子量  -6-
| 5.3 金屬離子  -7-
| 六、海藻寡醣組成成分之鑑定  -8-
| 6.1 薄層層析法 (thin-layer chromatography, LLC)  -8-
| 6.2高效能液相層析法 (high-performance liquid chromatography, HPLC)  -8-
| 6.3 核磁共振光譜法 (nuclear magnetic resonance, NMR)  -9-
| 七、洋菜酶的應用  -10-
| 7.1 細胞的分離  -10-
| 7.2 DNA分離  -11-
| 7.3 藻類原生質體的製作  -12-
| 7.4 海藻多醣的生產與降低黏度  -12-
| 7.5 藻類組成的分析  -13-
| 7.6 融合瘤細胞分離  -14-
| 参、實驗設計  -15-
| 肆、實驗材料與方法  -16-
| 一、實驗材料  -16-
| 1.1 實驗菌株  -16-
| 1.1.1 菌株之保存  -16-
| 1.1.2 菌株之活化  -16-
| 1.2 試驗藥品  -17-
| 1.2.1 藥品  -17-
| 1.2.2 電泳標準品  -18-
| 1.2.3 膠體過濾標準品  -18-
| 1.3 儀器設備  -18-
| 二、實驗方法  -20-
| 2.1 洋菜酶之生產及濃縮  -20-
| 2.1.1 洋菜酶之生產  -20-
| 2.1.2 洋菜酶之濃縮  -20-
| 2.2 洋菜酶的活性測定  -21-
| 2.2.1 測定方法  -21-
| 2.2.2 活性單位定義  -22-
| 2.3 蛋白質的定量  -22-
| 2.4 洋菜酶之分離純化  -22-
| 2.4.1 DE-52 離子交換樹脂層析  -22-
| 2.4.2 Bio-Gel P-100 膠體過濾層析  -23-
| 2.4.3 純化酵素之命名  -23-
| 2.5 洋菜酶之生化性質測試  -23-
| 2.5.1 分子量的鑑定  -23-
| 2.5.2 基質特異性  -25-
| 2.5.3 最適作用 pH 值  -26-
| 2.5.4 pH 值的安定性  -26-
| 2.5.5 最適作用溫度  -26-
| 2.5.6 溫度安定性  -27-
| 2.5.7 金屬離子的影響  -27-
| 2.5.7.1 鈣離子的影響  -27-
| 2.5.7.2 鈉離子的影響  -27-
| 2.5.7.3 其他金屬離子的影響  -27-
| 2.5.8 儲存安定性  -28-
| 2.5.9 活化能的決定  -28-
| 2.6 洋菜酶之分解產物的探討  -29-
| 伍、結果與討論  -30-
| 一、酵素的純化  -30-
| 1. 粗酵素液的製備  -30-
| 2. DE-52 離子交換樹脂層析  -30-
| 3. Bio-Gel P-100 膠體過濾層析  -32-
| 二、洋菜酶的生化特性  -33-
| 1.  分子量  -33-
| 2.  基質特異性  -34-
| 3.  最適作用 pH 值  -36-
| 4.  pH 值的安定性  -37-
| 5.  最適作用溫度  -38-
| 6.  溫度安定性  -39-
| 7.  鈣離子的影響  -40-
| 8.  鈉離子的影響  -41-
| 9.  其他金屬離子的影響  -43-
| 10. 儲存安定性  -44-
| 11. 活化能的決定  -45-
| 三、洋菜酶之分解產物的探討  -45-
| 陸、結論  -47-
| 柒、參考文獻  -49-
| 圖一、A. salmonicida MAEF108 生長曲線與洋菜酶活性圖  -61-
| 圖二、MAEF108-agarases 之 DE-52 管柱層析圖  -62-
| 圖三、MAEF108-agarase Ι 之第二次 DE-52 管柱層析圖  - 63-
| 圖四、MAEF108-agarase Ι 之 Bio-Gel P-100 膠體過濾層析圖  -64-
| 圖五、A. salmonicida MAEF108 菌株所產洋菜酶之 12.5% SDS-PAGE 圖  -65-
| 圖六、MAEF108-agarases 於不同緩衝液中的最適作用 pH值  -66-
| 圖七、MAEF108-agarase Ι 於不同緩衝液中的最適作用 pH 值  -67-
| 圖八、MAEF108-agarase ΙΙ 於不同緩衝液中的最適作用 pH 值  -68-
| 圖九、MAEF108-agarase ΙΙΙ 於不同緩衝液中的最適作用 pH 值  -69-
| 圖十、pH 值對 MAEF108-agarases之安定性  -70-
| 圖十一、pH 值對 MAEF108-agarase Ι 之安定性  -71-
| 圖十二、pH 值對MAEF108-agarase ΙΙ 之安定性  -72-
| 圖十三、pH 值對MAEF108-agarase ΙΙΙ 之安定性  -73-
| 圖十四、MAEF108-agarases 的最適反應溫度  -74-
| 圖十五、MAEF108-agarase Ι 的最適反應溫度  -75-
| 圖十六、MAEF108-agarase ΙΙ 的最適反應溫度  -76-
| 圖十七、MAEF108-agarase ΙΙΙ 的最適反應溫度  -77-
| 圖十八、MAEF108-agarases 之溫度安定性  -78-
| 圖十九、MAEF108-agarase Ι 之溫度安定性  -79-
| 圖二十、MAEF108-agarase ΙΙ 之溫度安定性  -80-
| 圖二十一、MAEF108-agarase ΙΙΙ 之溫度安定性  -81-
| 圖二十二、氯化鈣濃度對各洋菜酶活性之影響  -82-
| 圖二十三、氯化鈉濃度對各洋菜酶活性之影響  -83-
| 圖二十四、MAEF108-agarase Ι 之 Arrhenius polt  -84-
| 圖二十五、MAEF108-agarase ΙΙ 之 Arrhenius polt  -85-
| 圖二十六、MAEF108-agarase ΙΙΙ 之 Arrhenius polt  -86-
| 圖二十七、半乳糖、乳糖、及新洋菜六糖標準品之高效能液相層析圖  -87-
| 圖二十八、經 MAEF108-agarases 分解 1% agarose 之高效能液相層析圖  -88-
| 圖二十九、經 MAEF108-agarase Ι 分解 0.1% agarose 之高效  能液相層析圖  -89-
| 圖三十、經 MAEF108-agarase ΙΙ 分解 0.1% agarose 之高效能液相層析圖  -90-
| 圖三十一、經 MAEF108-agarase ΙΙΙ分解 0.1% agarose 之高效能液相層析圖  -91-
| 圖三十二、經MAEF108-agarase Ι 分解 1% 新洋菜六糖之高效能液相層析圖  -92-
| 圖三十三、經MAEF108-agarase ΙΙ分解 1% 新洋菜六糖之高效能液相層析圖  -93-
| 圖三十四、經MAEF108-agarase ΙΙΙ 分解新洋菜六糖之高效能液相層析圖  -94-
| 表一、MAEF108 洋菜酶之純化表  -95-
| 表二、MAEF108-agarases、MAEF108-agarase Ι、ΙΙ、及 ΙΙΙ 對九種多糖之基質特異性  -96-
| 表三、金屬離子對 MAEF108-agarases 活性之影響  -97-
| 表四、金屬離子對 MAEF108-agarase Ι 活性之影響  -98-
| 表五、金屬離子對 MAEF108-agarase ΙΙ 活性之影響  -99-
| 表六、金屬離子對 MAEF108-agarase ΙΙΙ 活性之影響  -100-
| 表七、MAEF108-agarase Ι 在七天儲存期間不同因子對活性的影響  -101-
| 附錄一、Agarose 的基本構造及洋菜酶作用位置  -102-
| 附錄二、Agarases 的生產微生物、種類及分離來源  -103-
| 附錄三、微生物所產洋菜酶分解洋菜之產物  -105-
| 附錄四、洋菜酶的生化特性  -107-
|
參考文獻: | 吳紹祺。1999。海洋細菌所產 agarases 生產條件與海藻多醣經 agarase 分解所得寡醣類組成之探討。國立臺灣海洋大學食品科學系碩士學位論文，基隆。
| 吳紹祺。2005。海藻多醣洋菜酶水解物及其發酵產物之生理活性研究。國立臺灣海洋大學食品科學系博士學位論文，基隆。
| 梁鳳鈺。1999。Pseudomonas vesicularis MA103 菌株所產洋菜酶的純化與性質。國立臺灣海洋大學食品科學系碩士學位論文，基隆。
| 郭孟欣。2002。海藻糖生成酶的生產與特性探討。國立臺灣海洋大學食品科學系碩士學位論文，基隆。
| 郭熙志、劉耀光、羅達。2004。以可轉化人工染色體 (TAC) 載體為基礎的百脈根基因組文庫的構建及篩選。植物生理與分子生物學學報。30: 234-238。
| 德永隆久、日高秀昌。1991。寒天オリグ糖の生產と利用。バイオサイエンスとインダストリ。49: 28-32。
| Allouch, J., M. Jam, W. Helbert, T. Barbeyron, B. Kloareg, B. Henrissat, and M. Czjzek.  2003.  The three-dimensional structures of two β-agarases.  J. Biol. Chem.  278: 47171-47180.
| Allouch, J., W. Helbert, B. Henrissat, and M. Czjzek.  2004.  Parallel substrate binding sites in a β-agarase suggest a novel mode of action on double-helical agarose.  Structure  12: 623-632.
| Aoki, T., T. Araki, and M. Kitamikado.  1990a.  Purification and characterization of β-agarase from Vibrio sp. AP-2.  Nippon Suisan Gakkaishi  56: 825-830.
| Aoki, T., T. Araki, and M. Kitamikado.  1990b.  Purification and characterization of a novel□ β-agarase from Vibrio sp. AP-2.  Eur. J. Biochem.  187: 464-465.
| Araki, C., and K. Arai.  1954.  Studies on agar-digesting bacteria. The isolation of agar-digesting bacteria and enzymatic activities.  Memoirs. Science and Technology/Faculty of Industrial Arts, Kyoto Technical University  3B: 7-23.
| Araki, T., Z. Lu, and T. Morishita.  1998a.  Optimization of parameters for isolation of protoplasts from Gracilaria verrucosa (Rhodophyta).  J. Mar. Biotechnol.  6: 193-197.
| Araki, T., M. Hayakawa, Z. Lu, S. Karita, and T. Morishita.  1998b.  Purification and characterization of agarases from a marine bacterium, Vibrio sp. PO-303.  J. Mar. Biotechnol.  6: 260-265.
| Belas, R., D. Barlent, and M. Silverman.  1988.  Cloning and gene replacement mutagensis of a Pseudomonas atlantica agarase gene.  Appl. Environ. Microbiol.  54: 30-37.
| Bradford, M. M.  1976.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.  Biochemistry  72: 248-254.
| Call, L. M., C. S. Moore, G. Stetten, and J. D. Gearhart.  2000.  A Cre-lox recombinationsystem for the targeted integration of circular yeast artificial chromosomes into embryonic stem ceels.  Hum. Mol. Genet.  9: 1745-1751.
| Carlsson, J., and M. Malmqvist.  1977.  Effects of bacterial agarase on agarose gel in cell culture.  In Vitro  13: 417-422.
| Chen, L. C.-M., J. S. Craigie, and Z. K. Xie.  1994.  Protoplast production from Porphyra linearis using a simplified agarase procedure capable of commercial application.  J. Appl. Phycol.  6: 35-39.
| Chen, Y.-C., and Y.-M. Chiang.  1994.  Development of protoplasts from Grateloupia sparsa and G. filicina (Halymeniaceae, Phodophyta).  Botanica Marina  37: 361-366.
| Corzo, A., J. J. Vegara, and M. C. Garcia-Jimenez.  1995.  Isolation and flow cytometric characterization of protoplasts from marine macroalgae.  J. Phycol.  31: 1018-1026.
| Couto, L. B., E. A. Spangler, and E. M. Rubin.  1989.  A method for the preparative isolation and concentration of intact yeast artificial chromosomes.  Nucl. Acids Res.  17: 8010.
| Day, D. F., and W. Yaphe.  1975.  Enzymatic hydrolysis of agar: Purification and characterization of neoagarobiose hydrolase and p-nitrophenyl α-galactoside hydrolase.  Can. J. Microbiol.  21: 1512-1518.
| Duckworth, M., and J. R. Turvey.  1969.  The specificity of an agarase from a Cytophaga species.  Biochem. J.  113: 693-696.
| Ensor L. A., Stosz S. K., and R. M. Weiner.  1999.  Expression of multiple complex polysaccharide-degrading enzyme systems by marine bacterium strain 2-40.  J. Ind. Microbiol. Biotechnol.  23: 123-126.
| Enzyme Nomenclature Database.  2006.  Agarase. http://us.expasy.org/cgi-bin/nicezyme.pl?3.2.1.81. (July 12, 2006, U.S.A.)
| Fukasawa, S., and H. Kobayashi.  1987.  Properties of agarase from a luminous bacterium, Vibrio harveyi.  Agric. Biol. Chem.  51: 269-270.
| Gnirke, A., C. Huxley, K. Peterson, and M. V. Olson.  1993.  Microinjection of intact 200-to-500-kb fragments of YAC DNA into mammalian cells.  Genomics  15: 659-667.
| Gray, F., J. S. Kenney, and J. F. Dunne.  l995.  Secretion capture and report web: Use of affinity derivatized agarose microdroplets for the selection of hybridoma cells.  J. Immunol. Methods  182: 155-163.
| Groleau, D., and W. Yaphe.  1977.  Enzyme hydrolysis of agar: Purification and characterization of□ β-neoagarotetraose hydrolase from Pseudomonas atlantica.  Can. J. Microbiol.  23: 672-679.
| Ha, J. C., G. T. Kim, S. K. Kim, T. K. Oh, J. H. Yu, and I. S. Kong.  1997.  β-Agarase from Pseudomonas sp. W7: Purification of the recombinant enzyme from Escherichia coli and the effects of salt on its activity.  Appl. Biochem. Biotechnol. 26: 1-6.
| Hassairi, I., R. B. Amar, M. Nonus, and B. B. Gupta.  2001.  Production and separation of α-agarase from Alteromonas agarlyticus strain GJ1B.  Bioresour. Technol.  79: 47-51.
| Hodgson, D. A., and K. F. Chater.  1981.  A chromosomal locus controlling extracellular agarase production by Streptomyces coelicolor A3(2), and its inactivation by chromosomal integration of plasmid SCP1.  J. Gen. Microbiol.  124: 339-348.
| Hosoda, A., M. Sakai, and S. Kanazawa.  2003.  Isolation and characterization of agar-degrading Paenibacillus spp. associated with the rhizosphere of Spinach.  Biosci. Biotechnol. Biochem.  67: 1048-1055.
| Imai, T., and M. V. Olson.  1990.  Second-generation approach to the construction of yeast artificial-choromosome libraries.  Genomics  8: 297-303.
| Ishimatsu, K.  1953.  Studies on the agar-liquefying bacteria (IV). Influence of temperature on the activity of agarase.  J. Ferment. Technol.  31: 53-56.
| Ivanova, E. P., E. A. Kiprianova, V. V. Mikhailov, G. F. Levanova, A. D. Garagulya, N. M. Gorshkova, M. V. Vysotskii, D. V. Nicolau, N. Yumoto, T. Taguchi, and S. Yoshikawa.  1998.  Phenotypic diversity of Pseudoalteromonas citrea from different marine habitats and emendation of the description.  Int. J. Syst. Bacteriol.  48: 247-256.
| Ivanova, E. P., T. Sawabe, N. M. Gorshkova, V. I. Svetashev, V. V. Mikhailov, D. V. Nicolau, and R. Christen.  2001.  Shewanella japonica sp. nov.  Int. J. Syst. Evol. Microbiol.  51: 1027-1033.
| Kamiunten, H.  l995.  Involvement of a plasmid in the expression of virulence in Pseudomonas syryngae pv. eriobotryae.  Nippon Shokubutsu Byori Gakkaiho  61: 376-380.
| Kang, N. Y., Y. L. Choi, Y. S. Cho, B. K. Kim, B. S. Jeon, J. Y. Cha, C. H. Kim, and Y. C. Lee.  2003.  Cloning, expression and characterization of a β-agarase gene from a marine bacterium, Pseudomonas sp. SK.38.  Biotechnol. Lett.  25: 1165-1170.
| Kim, B. J., H. J. Kim, S. D. Ha, S. H. Hwang, D. S. Byun, T. H. Lee, and J. Y. Kong.  1999.  Purification and characterization of β-agarase from marine bacterium Bacillus cereus ASK202.  Biotechnol. Lett.  21: 1011-1105.
| Kirimura, K., N. Masuda, Y. Iwasaki, H. Nakagawa, R. Kobayashi, and S. Usami.  1999.  Purification and characterization of a novel β-agarase from an alkalophilic bacterium, Alteromonas sp. E-1.  J. Biosci. Bioeng.  87: 436-441.
| Kobayashi, R., M. Takimasa, T. Suzuki, K. Kirimura, and S. Usami.  1997.  Neoagarobiose as a novel moisturizer with whitening effect.  Biosci. Biotechnol. Biochem.  61: 162-163.
| Kong, J. Y.  2001.  Production and functional properties of agarooligosaccharides.  Proceedings of Symposium on Scientific Study and Industrialization of Health Food, Health Food Society of Taiwan, Taipei.  pp. 60-81.
| Leon, O., L. Quintana, G. Peruzzo, and J. C. Slebe.  1992.  Purification and properties of an extracellular agarase from Alteromonas sp. strain C-1.  Appl. Microbiol. Biotechnol.  58: 4060-4063.
| Li., X., X. Dong, C. Zhao, Z. Chen, and F. Chen.  2003.  Isolation and some properties of cellulose-degrading Vibrio sp. LX-3 with agar-liquefying ability from soil.  World J. Microbiol. Biotechnol.  19: 375-379.
| Liu, Y.-G., H. Liu, L. Chen, W. Qiu, Q. Zhang, H. Wu, C. Yang, J. Su, Z. Wang, D. Tain, and M. Mei.  2002.  Development of new transformation-competent artificial chromosome vectors and rice genomic libraries for efficient gene cloning.  Gene  282: 247-255.
| Malmqvist, M.  1978.  Purification and characterization of two different agarose-degrading enzymes.  Biochem. Biophys. Acta  537: 31-43.
| Maule, J. C., D. J. Porteous, and A. J. Brookes.  1994.  An improved method for recovering intact pulsed field gel purified DNA, of at least 1.6 megabases.  Nucleic Acids Res.  22: 3245-3246.
| Mollet, J. C., M. C. Verdus, and H. Morvan.  l995.  Improved protoplast yield and cell wall regeneration in Gracilaria verrucosa (Huds.) Papenfuss (Gracilariles, Rhodophyta).  J. Exp. Bot.  46: 239-247.
| Morrice, J. M., M. W. McLean, W. F. Long, and F. B. Williamson.  1983a.  Porphyran primary structure: An investigation using β-agarase I from Pseudomonas atlantica and C-NMR spectroscopy.  Eur. J. Biochem.  133: 673-684.
| Morrice, L. M., M. W. McLean, F. B. Williamson, and W. F. Long.  1983b.  β-Agarases I and II from Pseudomonas atlantica. Purifications and some properties.  Eur. J. Biochem.  135: 553-558.
| Morrice, L. M., M. W. McLean, W. F. Long, and F. B. Williamson.  1983c.  β-Agarases I and II from Pseudomonas atlantica.  Eur. J. Biochem.  137: 149-154.
| Naganuma, T., D. A. Coury, M. Poline-Fuller, A. Gibor, and K. Horikoshi.  1993.  Characterization of agarolytic Microscilla isolates and their extracellular agarases.  Syst. Appl. Microbiol. 16: 183-190.
| Nikolaeva, E. V., A. I. Usov, and A. H. Tambiev.  1999.  Study on the marine agarolytic bacterium-infusorium association.  Mar. Biol.  135: 407-410.
| Osoegawa, K., P. Y. Woon, B. Zhao, E. Frengen, M. Tateno, J. J. Catanese, and P. J. de Jong.  1998.  An improved approach for construction of bacterial artificial chromosome libraries.  Genomics  52: 1-8.
| Osumi, Y., M. Kawai, H. Amano, and H. Noda.  1997.  Isolation and indentification of a porphyran-decomposing bacterium.  Nippon Suisan Gakkaishi  63: 709-714.
| Osumi, Y., M. Kawai, H. Amano, and H. Noda.  1998.  Effect of oligosaccharides from prophyran on in vitro digestions, utilizations by various intestinal bacteria, and levels of serum lipids in mice.  Nippon Suisan Gakkaishi  64: 98-104.
| Potier, M.-C., W. L. Kuo, A. Dutriaux, J. Gray, and M. Goedert.  1992.  Construcion and characterization of a yeast artificial chromosome library containing 1.5 equivalents of human chromosome 2l.  Genomics  14: 481-483.
| Potin, P., C. Richard, C. Rochas, and B. Kloareg.  1993.  Purification and characterization of the□ α-agarase from Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B.  Eur. J. Biochem.  214: 599-607.
| Rochas, C., P. Potin, and B. Kloareg.  1994.  NMR spectroscopic investigation of agarase oligomers produced by an □-agarase.  Carbohydr. Res.  253: 69-77.
| Ryu S. K., Cho S. J., Park S. R., Lim W. J., Hong S. Y., Bae D. W., Park Y. W., Kim B. K., Kim H., and H. D. Yam.  2001. Cloning of the cel9A gene and characterization of its gene product from marine bacterium Pseudomonas sp. SK38.  Appl. Microbiol. Biotechnol.  57: 138-145.
| Schroeder, D. C., M. A. Jaffer, and V. C. Coyne.  2003.  Investigation of the role of a β(1-4) agarase produced by Pseudoalteromonas gracilis B9 in eliciting disease symptoms in the red alga Gracilaria gracilis.  Microbiology  149: 2919-2929.
| She, K.  2003.  So you want to work with giants: The BAC vector.  Bio. Tech. J.  1: 69-74.
| Shibasaki, Y., J. C. Maule, R. S. Devon, E. M. Slorach, J. R. Gosden, D. J. Porteous, and A. J. Brookes.  1995.  Catch-linker+PCR labeling: A simple method to generate fluorescence in situ hybridization probes from yeast artificial chromosomes.  PCR Methods Appl.  4: 209-211.
| Shieh, W. Y., and W. D. Jean.  1998.  Alterococcus agarolyticus, gen. nov., sp. nov., a halophilic thermophilic bacterium capable of agar degradation.  Can. J. Microbiol.  44: 637-645.
| Shizuya, H., and H. Kouros-Mehr.  2001.  The development and applications of the bacterial artificial chromosome cloning system.  Keio J. Med.  50: 26-30.
| Shome, B. R., R. Shome, S. P. S. Ahlawat, and N. D. Verma.  2000.  Agar depolymerizing (agarolytic) bacteria isolated from mangrove soil samples of Andaman.  Curr. Sci.  79: 696-697.
| Singh, T.  1992.  Agar and Agar Production.  INFOFISH, Kuala Lumpur  pp. 1-25.
| Singh, R., P. A. Lessard, T. S. Guan, J. M. Panandam, A. Sinskey, and S.-C. Cheah.  2003.  Preliminary attempts at the construction of large insert DNA libraries for oil palm.  J. Oil Palm. Res.  15: 12-20.
| Solursh, M.  l991.  Formation of cartilage tissue in vitro.  J. Cell. Biochem. 45: 258-260.
| Stanier, R. Y.  1942.  Agar decomposing strains of the Actinomyces coelicolor species group.  J. Bacteriol. 44: 555-570.
| Stedman, T. L.  1982.  Stedman’s Medical Dictionary.  24th ed.  Williams and Awaikins, London.  p. 30.
| Sugano, Y., I. Terada, M. Arita, M. Noma, and T. Matsumoto.  1993a.  Purification and characterization of a new agarase from marine bacterium, Vibrio sp. strain JT0107.  Appl. Environ. Microbiol.  59: 1549-1554.
| Sugano, Y., T. Matsumoto, H. Kodama, and M. Noma.  1993b.  Cloning and sequencing of agaA, a unique agarase 0107 gene from a marine bacterium, Vibrio sp. strain JT0107.  Appl. Environ. Microbiol.  59: 3750-3756.
| Sugano, Y., H. Kodama, I. Terada, Y. Yamazaki, and M. Noma.  1994.  Purification and characterization of a novel enzyme, α-neoagarooligosaccharide hydrolase (α-NAOS hydrolase), from a marine bacterium, Vibrio sp. strain JT0107.  J. Bacteriol.  176: 6812-6818.
| Suzuki, H., Y. Sawai, T. Suzuki, and K. Kawai.  2002.  Purification and characterization of an extracellular α-neoagarooligosaccharide hydrolase from Bacillus sp. MK03.  J. Biosci. Bioeng.  93: 456-463.
| Suzuki, H., Y. Sawai, T. Suzuki, and K. Kawai.  2003.  Purification and characterization of an extracellular β-agarase from Bacillus sp. MK03.  J. Biosci. Bioeng.  95: 328-334.
| Swartz, M., and N. Gordon.  1959.  Agarase from an agar-digesting bacterium.  J. Bacteriol.  77: 403-409.
| Turvey, R., and J. Christison.  1967.  The enzymic degradation of porphyran.  Biochem. J.  105: 317-321.
| van der Meulen, H. J., and W. Harder.  1975.  Production and characterization of the agarase of Cytophaga flevensis.  Antonie van Leeuwenhoek  41: 431-447.
| van der Meulen, H. J., and W. Harder.  1976.  Characterization of the neoagarotetra-ase and neoagarobiase of Cytophaga flevensis.  Antonie van Leeuwenhoek  42: 81-94.
| Vera, J., R. Alvarez, E. Murano, J. C. Slebe, and O. Leon.  1998.  Identification of a marine agarolytic Pseudoalteromonas isolate and characterization of its extracellular agarase.  Appl. Environ. Microbiol.  64: 4378-4383.
| Volinia, S., R. P. Piva, A. Bozza, S. Stefani, D. Gandini, and L. del Senno.  1992.  Simplified construction and characterization of yeast artificial chromosome libraries.  Biochem. Int. 27: 45-53.
| Whitehead, L. A., S. K. Stosz, and R. M. Weiner.  2001.  Characterization of the agarase system of a multiple carbohydrate degrading marine bacterium.  Cytobios  106: 99-117.
| Wu, R.-Y., and M.-H. Chen.  1995.  Indentification of the Streptomyces strain KS3-5.  Bot. Bull. Acad. Sin. 36: 201-205.
| Wu, S. C., and C. L. Pan.  2004.  Preparation of algal-oligosaccharide mixtures by bacterial agarase and their antioxidative properties.  Fish. Sci.  70: 1164-1173.
| Wu, S. C., T. N. Wen,. and C. L. Pan.  2005.  Algal-oligosaccharide-lysates prepared by two bacterial agarases stepwise hydrolyzed and their anti-oxidative properties.  Fish. Sci.  71: 1149-1159.
| Yamaura, I., T. Matsumoto, M. Funatsu, H. Shigeiri, and T. Shibata.  1991.  Purification and properties of agarase from Pseudomonas sp. PT-5.  Agric. Biol. Chem.  55: 2531-2536.
| Yaphe, W.  1957.  The use of agarase from P. altantica in the identification of agar in marine algae (Rhodophyceae).  Can. J. Microbiol.  3: 987-993.
| Yoshizawa, Y., A. Ametani, J. Tsunehiro, K. Nomura, M. Itoh, F. Fukui, and S. Kaminogawa.  1995.  Macrophage stimulation activity of the polysaccharide fraction of a marine alga (Porphyra yezoensis): Structure-function relationships and improved solubility.  Biosci. Biotechnol. Biochem.  59: 1933-1937.
| Yoshizawa, Y., J. Tsunehiro, K. Nomura, M. Itoh, F. Fukui, A. Ametani, and S. Kaminogawa.  l996 . In vivo macrophage-stimulation activity of the enzyme-degraded water-soluble polysaccharide fraction from a marine alga (Gracilaria verrucosa).  Biosci. Biotechnol. Biochem.  60: 1667-1671.
| Young, K.S., S. S. Battacharjee, and W. Yaphe.  1978.  Enzymic cleavage of the α-linkages in agarose, to yield agaro-oligosaccharides.  Carbohydr. Res.  66: 207-212.
| Zhong, Z., A. Toukdarian, D. Helinski, V. Knauf, S. Sykes, J. E. Wilkinson, C. O’Bryne, T. Shea, and G. DeLoughery.  2001.  Sequence analysis of a 101-kilobase plasmid required for agar degradation by a Microscilla isolate.  Appl. Environ. Microbiol.  67: 5771-5779.
|

|

預覽及輸出檢索結果

記錄

欄位

| 本頁 1 筆
| 記錄 20 至 32
| 選擇之記錄

| 標題
| 全部欄位
| selected fields new window
| APA Style
| Chicago Style
| MLA Style
| CNS-13611 Style
| EndNote Style

e-mail 地址 | : |
e-mail 標題 | : |

| | |

系統規劃：海洋大學圖書館
系統製作：飛資得資訊有限公司

2010 年 3 月 8 日 23:00