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詳目顯示區塊

第 9 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: | 石蓴 (Ulva fasciata) 脂氧合酶純化及固定化後之生化特性
| Purification and Biochemical Properties of Membrane-Bound Lipoxygenase from Sea Algae (Ulva fasciata) and Its Immobilization.
研究生: | 李武峰 Wu-Feng Li
指導教授: | 孫寶年 Bonnie Sun 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: | M93320002
畢業學年度: | 94
語文別: | 中文
關鍵字: | 海藻 sea algae
| 脂氧合酶 lipoxygenase
| 蛋白質純化 protein purification
| 固定化 immobilization
| 膜結合蛋白 membrane-bound protein
| 石蓴 Ulva
全文點閱次數: | 15

全文影像連結:

論文全文(pdf)

論文頁數: | 78
摘要: | 中文摘要
| 石蓴脂氧合酶 ( LOX ) 作用於雞油及魚油後，可改善其氣味（Hu et al., 2000 and Ma et al., 2004），但游離態LOX易受環境因子影響而失活，酵素易失活，且不易回收重複使用。
| 石蓴粗酵素液經固定化，LOX的反應性差（劉，2005），本研究為純化石蓴（U.  fasciata）LOX並固定化，探討其安定性及比較其生化特性與游離態LOX之差異。
| 萃取石蓴LOX時，添加介面活性劑 0.05％ Triton X-100萃取之比活性由0.046提高至0.484 μmole min-1 mg-1，增加10.52倍，但萃取率未隨Triton 的濃度增加而升高。
| 石蓴粗酵素液以MW 100 KDa膜過濾法純化回收率為78.9％，以35-55％硫酸銨沈澱法為73.7％；純化倍數分別為1.77、3.37倍。經35-55％硫酸銨沈澱之LOX，添加0.2 mM CaCl2於4 ℃含磷酸緩衝液中透析，可保留原本之活性，未添加CaCl2 時，則透析後完全失活，於透析液內再添加蛋白酶抑制劑1 mM PMSF及還原劑1 mM Glutathione，透析後4℃儲存4天，活性可維持原來之50％ ，未添加任何保護劑，則1天後完全失活。
| 經由35-55 ％硫酸銨分劃之沉澱物再經陰離子交換樹酯Macroprep Q純化後，有活性之部分，回收率為52 ％、純化倍數10倍，於Native-PAGE電泳分析後，以硝酸銀染色為一條蛋白帶。此純化之石蓴LOX最適溫度為35 ℃，最適pH 為7.5，以亞麻油酸（C18：2）當基質之km為117.64 μM，Vmax為12.82 μmole hydroperoxy fatty acid/min-mg protein，以花生四稀酸（C20:4）之km為 31.25 μM，Vmax為 23.25 μmole hydroperoxy fatty acid/min-mg protein，石蓴脂氧合酶對對不同脂肪酸的基質反應速度依序為C18:4＞C20:4＞C18:2較酯化C18:4高。
| 以褐藻膠包埋部分純化之脂氧合酶，進行固定化。固定化酵素( 0.89 μmole /g beads )於25 ℃、100 rpm震盪，與1 μmole亞麻油酸作用，反應達平衡需110分鐘。固定化脂氧合酶重複使用6次時，酵素活性為原來之66％。固定化酵素放置於4 ℃，至14天可維持原來活性，儲藏至一個月，酵素活性仍保持約原來的51％。
| 游離態與固定化LOX分別作用於花生四烯酸( C20:4 )，產物有15-HETE及11-HETE，活性比例分別為1: 7及1: 6，以11- HETE為主。以亞麻油酸（C18:2）為基質，產物為9-HpODE，約為13- HpODE 之6.63倍，因此固定化並不影響其催化基質之特異性。未來需探討固定化酵素對各種不同游離脂肪酸產生之氣味並進而以氣相-質譜得知化學結構。
|
| Abstract
| The flavor modification of chicken and fish oil treated with LOX from Ulva（Hu et al., 2000 and Ma et al., 2004）. Because free-form LOX easily affected by environmental factor, LOX activity and stability were lost easily and not be reused.
| When immobilized the extracts of U. fasciata, the LOX activity were very low. The objective of this study was purified LOX from U. fasciata then to investigate the stability of immobilized LOX, Further the compare and characteristics the biochemical properties from free and immobilized LOX was studied.
| The recovery of partial purified LOX activities from crude algal LOX extract were 78.9%, 73.7% and purified about 1.77, 3.37-folds by MW10000 membrane and 35-55% saturation of ammonium sulfate fractionation, respectively. The partial purified LOX added 0.2mM CaCl2 during dialysis was retained activity but it was not detected without Ca2+. Adding protease inhibitor PMSF (1mM) and hydroperoxy reducing reagent glutathione (1mM) to partial purified LOX retains 50% of relative activity at 4 days during storage at 4℃.The whole LOX activity was lost within 1 day in the absence of any protector.
| The lipoxygenase was purified 10-folds from U. fastata using 35-55% saturation of ammonium sulfate fractionation, followed Macroprep Q ion exchange. The recovery of total recovery was 52%. The Michaelis constant ( Km ) of LOX was 117.64、31.25 μM, and maximal velocity ( Vmax ) was 23.25、12.82 μmole hydroperoxy fatty acid/min-mg protein using linoleic acid (C18:2) and arachidonic acid (C20:4) as substrate, respectively. Algal LOX showed the highest activity towards C18:4 followed by C20:4, C18:2 and C18:4-methyled.
|
| The partial purified LOX was entrapped using Ca2+-alginate. The immobilized LOX need 110 minutes to reach maximal activity ( A234nm/mg protein ) on shaking rate 100 rpm at 25℃using linoleic acid ( 1μM ) as substrate. When used repeatedly for 6 times, the immobilized LOX was decreased 66% activity. The residual activity of immobilized algal LOX was 51% after a month storage at 4℃.
| The hydroxy product of arachidonic acid reacted with free and immobilized algal LOX were 15- and 11- hydroxyeicosatetraenoic acid at reactive ratio of 1:7 and 1:6.When linoleic acid was incubated with the LOX, 9-hydroperoxy octadecadienoic acid was found to be main product, and total activity was about 6.63-folds to 13-LOX. Therefore the immobilization of LOX did not affect it’s catalyst specific substrate.
| To study of the flavor produced by immobilized LOX reacts with different free fatty acid and to identification using GC-MS in the future.
|
論文目次: | 中文摘要    i
| 英文摘要    iii
| 壹、前言    1
| 貳、文獻回顧    3
| 一、脂氧合酶來源及分佈    3
| (1) 動物    3
| (2) 陸生植物    4
| (3) 水產植物    4
| 二、脂氧合酶反應機制    4
| 三、藻類脂氧合酶之特性與其應用    5
| 1.藻類脂氧合酶之生化特性    5
| (1) 來源    5
| (2) 活化及抑制    6
| (3) 最適溫度和pH    7
| (4) 安定性    7
| (5) 基質特異性    8
| (6) 異構酶種類    8
| 2. 脂氧合酶之應用-揮發性成分之影響    9
| 四、脂氧合酶不穩定之因素    10
| 1. 動物與植物結構差異    10
| 2. 活性部位鐵離子還原    11
| 3. 產物之回饋抑制    11
| 4. 胺基酸之結構組成氧化    12
| 五、固定化脂氧合酶方法與生化性質    12
| 1. LOX固定化方法    12
| 2. 固定化 LOX 之生化特性    14
| 參、材料與方法    17
| 一、材料    17
| 二、方法    18
| 1. 粗酵素液之製備    18
| 2. 脂氧合酶活性之測定    18
| (1) 吸光度法-LOOH產物測定    18
| (2) 基質特異性分析    19
| (3) 蛋白質定量-染劑結合法    20
| 3. 脂氧合酶純化步驟及異構酶鑑定    20
| (1) 膜過濾純化    20
| (2) 硫銨分劃    21
| (3) Q 陰離子交換管柱層析    21
| (4) Native PAGE電泳    22
| (5) 脂氧合酶異構酶之鑑定    22
| 4. 石蓴脂氧合酶生化特性之測定    23
| (1) 最適作用溫度    23
| (2) 最適作用pH    24
| (3)  Km及Vmax    24
| (4) 基質特異性    24
| (5) 儲存安定性    25
| 5. 固定化海藻脂氧合酶之製備及活性測定    25
| (1) 固定化 LOX 的製備    25
| (2) 固定化 LOX 活性之測定    25
| 6. 固定化 LOX 特性之測定    26
| (1) 操作穩定性 ( Operational stability )    26
| (2) 儲存安定性    26
| 肆、結果與討論    27
| 一、 石蓴脂氧合酶萃取與種類鑑定    27
| 1. 石蓴酵素之萃取    27
| 2. 基質特異性    29
| 3. 以GC/MS鑑定之氫過氧化物    34
| 二、石蓴脂氧合酶之儲存安定性及純化    36
| 1. 硫酸銨沈澱與膜過濾部分純化方法之比較    36
| 2. Ca2+ 對脂氧合酶安定性之影響    39
| 3. 保護劑對脂氧合酶儲存安定性之影響    40
| 4. Q 陰離子交換管柱層析    44
| 5. 以Native-PAGE鑑定LOX之純度    48
| 三、石蓴脂氧合酶之固定化    49
| 四、游離態與固定化石蓴脂氧合酶之特性    51
| 1. 異構酶種類    51
| 2. 石蓴脂氧合酶之特性    55
| (1) 最適作用溫度    55
| (2) 最適作用 pH 值    57
| (3)  Km、Vmax    59
| (4) 基質特異性    62
| 3. 儲存安定性    64
| 4. 重複使用性    66
| 伍、結論    68
| 陸、參考文獻    70
|
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2009 年 11 月 22 日 23:19