臺灣博碩士論文加值系統

竹蟶(Solen strictus)內臟中已經被純化出二種不同澱粉酶，分別命名為Amy I, Amy II。澱粉酶之純化係利用含有5mM氯化鈣的10mM Tris-HCl (pH7.2)緩衝溶液抽取後，再經硫酸銨分劃、DEAE-Sepharose fast flow 和Sephacryl S-200等一系列管柱層析，純化倍率分為82.8倍和26.9倍，回收率則分別為11.7﹪及 7.1﹪，經Native-PAGE電泳分析，證實Amy I已經完全純化，Amy II則部分純化。分子量分別是69 kDa及 116 kDa。再經SDS-PAGE電泳分析，可知Amy I為單體(monomer)，分子量為66.2kDa。而Amy II則應有二個次單元。
Amy I和Amy II之最適溫度為皆為50oC；最適pH兩者都在pH6.0附近；而溫度安定性方面兩者都在50 oC以下安定性較佳。鈉、鈣、鋇、鋰等離子可將澱粉酶Amy I、Amy II活性提高，而鋅、銅、汞等金屬離子可幾乎將此兩種澱粉酶之活性抑制。EDTA會抑制此兩種澱粉酶的活性。
此外，這兩種澱粉酶可以水解直鏈澱粉(amylose)、支鏈澱粉(amylopectin)、肝醣(glycogen)，顯示具有水解α-1,4糖苷鍵能力。而對直鏈澱粉、支鏈澱粉及肝醣之水解產物進行薄層層析法探討反應生成物，發現Amy I與Amy II應為γ-amylase。

Amylases (Amy I and Amy II) have been purified from viscera of the Solen strictus. Both of the two amylases were extracted with 10mM Tris-HCl buffer (pH7.2) containing 5mM CaCl2 and further fractionated by ammonium sulfate, and then chromatographied with DEAE-sepharose fast flow and sephacryl S-200 columns. By these steps, the purifications of the two enzymes increased to 82.8 and 26.9 folds and the recovery of the two enzymes activity were 11.7% and 7.1%, respectively. The Amy I was purified to electrophoretical homogeneity, while Amy II was partial purified. The molecular weights of Amy I and Amy II were 69kDa and 116kDa, respectively.
The optimal temperature of both enzymes were 50 oC. The optimal pH of Amy I and II were the same pH6.0. In temperature stability, Amy I and II were stable below 50oC. The two amylases were activated by Na+、Mg2+、Ca2+、Ba2+、Li+, but completely inhibited by Zn2+、Cu2+、Hg2+ ions. EDTA was the most efficient than others to inhibit the two amylases.
Both Amy I and II could hydrolyze amylose, amylopectin and glycogen, and show the two amylases could hydrolyze α-1,4 glycosidic bond. From the results of TLC, Amy I and Amy II could be γ-amylase.

目錄
頁數
謝誌……………………………………………………………………….i
中文摘要 ii
英文摘要 iii
目錄……………………………………………………………………...iv
表目錄………………………………………………………………….viii
圖目錄…………………………………………………………………...ix
壹、實驗目的 1
貳、文獻整裡 3
一、竹蟶簡介 3
二、澱粉酶 3
三、α-澱粉酶 16
2.各種離子對α-澱粉酶之影響 18
3.物理化學性質 19
4.作用方式 20
5.構造 22
6.特殊的α-澱粉酶 23
7.異構酶 24
四、β-澱粉酶 25
1.分子量 25
2.一般性質 25
3.物理化學性質 26
4.作用方式 26
五、γ-澱粉酶 28
1.分子量 28
2.組成份 29
3.物理化學性質 30
六、去支鏈酵素(debranching enzyme) 30
1.Pullulanases (pullulan 6-glucanohydrolase, EC 3.2.1.41) 31
2.異澱粉分解酵素(glycogen 6-glucanohydrolase, EC 3.2.1.11) 32
七、澱粉酶在工業上的應用 33
1.烘焙業 34
2.糖漿製造 34
3.紡織、造紙業 35
4.清潔劑應用 36
參、實驗材料與方法 39
一、澱粉酶之純化 39
1.實驗材料: 39
2.儀器 39
3.緩衝溶液 39
4.藥品 40
5.澱粉酶的活性測定方法 40
6.蛋白質定量 40
7.純化方法 41
8電泳分析. 41
9.蛋白質分子量的測定 42
二、澱粉酶的生化特性試驗 42
1.最適溫度 42
2.溫度安定性 42
3.最適酸鹼度 42
4.酸鹼度安定性 43
5.基質特異性 43
6.反應生成物探討 43
7.金屬離子的影響 43
8.抑制劑的影響 44
肆、結果與討論 45
一、澱粉酶之純化 45
1.硫酸銨分劃 45
2.DEAE-Sepharose fast flow陰離子交換層析法 45
3. Sephacryl S-200膠體過濾層析法 46
4.電泳分析鑑定純度 47
5.次單元鑑定及分子量估算 47
二、澱粉酶的生化特性分析 47
1.最適溫度 47
2.溫度安定性 48
3.最適酸鹼度 49
4.酸鹼度安定性 50
5.基質特異性 50
6.反應生成物之探討 51
7.金屬離子對竹蟶內臟澱粉酶的影響 51
8.抑制劑對竹蟶內臟澱粉酶的影響 52
伍、結論及其應用 54
陸、參考文獻 55








表目錄

表一、硫酸銨分劃表……………………………………………………74
表二、竹蟶內臟澱粉酶之純化表………………………………………75
表三、竹蟶內臟澱粉酶之基質特異性…………………………………76
表四、各種金屬離子對竹蟶內臟澱粉酶之影響………………………77
表五、各種抑制劑對竹蟶內臟澱粉酶之影響…………………………78













圖目錄

圖一、竹蟶澱粉酶DEAE -Sepharose管柱層析圖……………………79
圖二、竹蟶澱粉酶(Amy I)第二次DEAE -Sepharose管柱層析圖……80
圖三、竹蟶澱粉酶(Amy II)第二次DEAE -Sepharose管柱層析圖… 81
圖四、竹蟶澱粉酶(Amy I)Sephacryl S-200膠體過濾層析圖…………82
圖五、竹蟶澱粉酶(Amy II)Sephacryl S-200膠體過濾層析圖……… 83
圖六、12.5% Native-PAGE電泳圖…………………………………….84
圖七、12.5% Native-PAGE電泳分子量估圖………………………… 85
圖八、12.5% SDS-PAGE電泳圖……………………………………… 86
圖九、12.5% SDS-PAGE電泳分子量估算圖………………………… 87
圖十、溫度對竹蟶內臟澱粉酶活性的影響……………………………88
圖十一、竹蟶內臟澱粉酶的溫度安定性………………………………89
圖十二、pH對竹蟶內臟澱粉酶的影響……………………………… 90圖十三、竹蟶內臟澱粉酶的pH安定性……………………………… 91
圖十四、竹蟶內臟澱粉酶水解直鏈澱粉反應生成物之薄層分析……92
圖十五、竹蟶內臟澱粉酶水解支鏈澱粉反應生成物之薄層分析……93
圖十六、竹蟶內臟澱粉酶水解肝醣反應生成物之薄層分析…………94

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