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本研究以經電透析處理之鹹鴨蛋蛋白液或未電透析處理之鹹鴨蛋蛋白液為原料，添加0.5%(w/w)的蛋白質分解酵素(Papain W-40、Peptidase R、Proleather FG、Protease A、Protease N或 Prozyme 6)，置於45℃反應槽中進行水解0至24小時，探討酵素種類與水解時間對鹹鴨蛋蛋白液水解物的蛋白質分子分布與產物之抗氧化能力的影響。由可溶性蛋白質含量、胜太含量、胺基態氮含量、蛋白質電泳、膠體層析及高效能液相層析(C4與C18管柱)的分析結果顯示，電透析處理組之Prozyme 6水解物有較高之胜太產率。水解產物分子量分佈以5,000 Da以下為主。進一步探討各水解物對亞麻油酸自氧化作用之抑制能力，結果顯示未電透析處理組經Protease N水解24小時、Prozyme 6水解12小時及Protease A水解12小時之水解物的IC50值分別為1.14、1.20及1.37 mg/ml，其抗氧化能力比電透析處理組經相同酵素與水解時間為佳。將水解物以膜過濾劃分並凍乾後，配製成濃度為5 mg/ml時，電透析處理組之Protease N水解物的分子量1 kDa以下區分物為最具抗氧化能力(p＜0.05)，其抑制率為76.97%。分析其胺基酸組成，其中以脯胺酸(Proline)及鹼性胺基酸群含量較多於未電透析處理組。另以Protease A及Protease N水解物之抗氧性較強的膜區分物再利用Superdex peptide column進行劃分後，可得到7個主要劃分物，其中F3分子量介於1,100-2,800 Da之間，F4分子量介於450-1,100 Da之間，F5分子量介於180-450 Da之間，F6分子量則介於70-180 Da之間。在0.1-2 mg/ml濃度時，Protease A及Protease N水解物之膜區分物具有較佳抑制亞麻油酸自氧化能力之分子量範圍，分別是在1,100-2,800 Da及450-1,100 Da之間。

In this study, the salted duck''s egg white was treated or untreated by electrodialysis desalination as materials which were hydrolyzed with the addition of 0.5% (w/w) proteases (Papain W-40、Peptidase R、Proleather FG、Protease A、Protease N or Prozyme 6) and then were hydrolyzed for 0 to 24 hours at 45℃ in a reactor. The effect of proteases and hydrolysis time on protein molecules'' pattern and the antioxidative activity of salted duck''s egg white hydrolysates were investigated. Analysis of soluble protein content, peptide content, N-amino nitrogen content, SDS-PAGE, gel filtration chromatography and HPLC (C4 column and C18 column), the results suggested that the highest value in peptide yield was obtained when salted duck''s egg white was treated by electrodialysis desalination and then was hydrolyzed by Prozyme 6. The molecular weight distributions of hydrolysates were all below 5,000 Da by gel filtration chromatography.
Further, we examined that all hydrolysates inhibited linoleic acid autoxidation. Results showed that the salted duck''s egg white hydrolysates which were untreated by electrodialysis desalination with Protease N for 24 hours, Prozyme 6 for 12 hours, and Protease A for 12 hours had a higher ability of linoleic acid autoxidation than that treated by electrodialysis desalination. The IC50 values of hydrolysates were 1.14, 1.20 and 1.37 mg/ml, respectively. The hydrolysates were further screened by different proe size membranes, and then were freezed. When the solid concentration was 5 mg/ml, the Protease N hydrolysates of pore size membrane fraction (molecular weight below 1 kDa) was untreated by electrodialysis desalination had a stronger antioxidative activity (p＜0.05), and the inhibition effect was 76.97%. However, this membrane fraction had higher contents of Proline and basic amino acids than those were untreated by electrodialysis desalination.
In addition, the pore size membrane fractions which had a higher antioxidative activity from Protease A and Proteas N were subjected to a Superdex peptide column gel filtration chromatography, and seven major fractions were obtained. Among of the fractions, the molecular weight of F3 was 1,100-2,800 Da, the molecular weight of F4 was 450-1,100 Da, the molecular weight of F5 was 180-450 Da and the molecular weight of F6 was 70-180 Da. The inhibition of linoleic acid autoxidation for all gel filtration fractions of the Protease A and Protease N hydrolysates from pore size membrane fractions were indicated that peptides with the molecular weight of 1,400-2,800 Da and 450-1,100 Da had a higher ability of the inhibition of linoleic acid autoxidation than others.

目錄.............................................I
表目錄......................................... VII
圖目錄........................................ VIII
中文摘要........................................ XI
英文摘要...................................... XIII
第一章　前言.................................... 1
第二章　文獻回顧................................ 4
一、蛋白的理化質................................ 4
（一）卵白蛋白.................................. 4
（二）伴白蛋白.................................. 7
（三）卵類黏蛋白................................ 7
（四）卵球蛋白.................................. 7
（五）卵黏蛋白.................................. 8
（六）溶菌每.................................... 8
二、鹹鴨蛋...................................... 9
（一）鹹鴨蛋（鹽漬殼蛋）之製法.................. 9
1. 紅土塗佈法................................... 9
2. 浸漬法....................................... 9
（二）鹽漬中蛋白與蛋黃的變化................... 10
（三）鹹鴨蛋蛋白液之應用....................... 10
三、電透析分離技術............................. 12
（一）原理..................................... 12
（二）薄膜的特性............................... 12
（三）應用..................................... 14
四、蛋白質分解酵素的特性....................... 14
（一）絲胺酸型蛋白質分解酵素................... 15
1. 胰凝乳蛋白每與胰蛋白每...................... 15
2. 麴菌屬之蛋白每.............................. 16
（二）硫醇型蛋白質分解酵素..................... 16
1. 木瓜蛋白分解每.............................. 17
2. 鳳梨蛋白分解每.............................. 17
（三）金屬型蛋白質分解酵素..................... 18
（四）酸性蛋白質分解酵素....................... 18
五、油脂氧化與抗氧化劑......................... 18
（一）脂質氧化作用............................. 18
1. 自氧化作用.................................. 18
2. 光氧化作用.................................. 19
3. 熱氧化作用.................................. 19
4. 酵素性氧化作用.............................. 20
（二）脂質氧化對生理健康之影響................. 20
（三）防止食品氧化的方法與途徑................. 21
（四）抗氧化物質的作用機制..................... 22
1. 自由基終止劑................................ 22
2. 還原劑和氧的清除劑.......................... 23
3. 金屬螯合劑.................................. 23
4. 單重態氧抑制劑.............................. 23
六、蛋白質水解程度之影響因子................... 24
（一）水解方式................................. 24
（二）酵素的種類、來源與水解位置............... 24
（三）酵素與受質比例........................... 25
（四）溫度..................................... 25
（五）pH值..................................... 26
（六）食鹽濃度與抑制劑......................... 26
七、蛋白質水解物之應用......................... 27
（一）蛋白質水解物的抗氧化性................... 27
1. 動物性來源之蛋白質或胜太的抗氧化性.......... 27
（1）肌太之抗氧化性............................ 27
（2）卵白蛋白及其水解物之抗氧化性.............. 28
（3）牛乳蛋白及其水解物之抗氧化性.............. 29
（4）魚、蝦蛋白及其水解物之抗氧化性............ 29
2. 植物性來源之蛋白質或胜太的抗氧化性.......... 30
（1）大豆蛋白及其水解物之抗氧化性.............. 30
（2）蠶豆蛋白之抗氧化性........................ 31
3. 其它........................................ 32
（1）明膠之抗氧化性............................ 32
（2）鮪魚蒸煮液蛋白質水解物之抗氧化性.......... 32
（二）蛋白質水解物的其他功能性................. 32
1. 調味利用.................................... 32
2. 營養利用.................................... 33
3. 促進鈣磷吸收................................ 34
4. 類鴉片作用.................................. 34
5. 調整免疫作用................................ 35
6. 防止血栓形成................................ 35
7. 抗高血壓性.................................. 36
8. 促進雙歧桿菌生長............................ 37
9. 抗菌活性.................................... 37
10. 苦味性..................................... 38
第三章　材料與方法............................. 39
一、實驗流程................................... 39
二、實驗材料................................... 39
1. 鴨蛋........................................ 39
2. 鹹鴨蛋白液.................................. 39
3. 電透析脫鹽之鹹鴨蛋蛋白液.................... 39
4. 蛋白質分解酵素.............................. 39
5. 化學藥品.................................... 40
三、實驗方法................................... 44
1. 鹹鴨蛋蛋白液酵素水解........................ 44
2. 可溶性蛋白質含量的測定...................... 44
3. 胺基態氮含量的測定...........................44
4. 胜太含量的測定.............................. 45
5. SDS不連續聚丙烯醯胺膠體電泳................. 45
6. 膠體過濾層析................................ 46
7. 高效能液相層析.............................. 46
（1）C4管柱HPLC分析條件........................ 47
（2）C18管柱HPLC分析條件....................... 47
8. 鹹鴨蛋蛋白水解物於亞麻油酸乳化系統之抗氧化活性. 48
（1）0.02 M之亞麻油酸乳化物之製備.............. 48
（2）抗氧化活性之測定法........................ 48
9. IC50值的測定............................... 48
10. 水解物之膜過濾劃分與收集................... 49
11. 劃分收集物對亞麻油酸自氧化抑制能力之測定... 49
12. 表面硫氫基含量之測定....................... 49
13. 胺基酸組成與含量之測定..................... 50
14. 膜區分物之管柱析出物劃分與收集............. 50
15. 膜區分物之各劃分收集物抑制亞麻油酸自氧化能力的測定. 50
16. 統計分析................................... 51
第四章　結果與討論............................. 52
一、電透析脫鹽處理對鹹鴨蛋蛋白液酵素水解物之化學性質的影響. 52
（一）可溶性蛋白質含量......................... 52
（二）胜太含量................................. 54
（三）胺基態氮含量............................. 56
（四）SDS-PAGE電泳圖譜......................... 58
（五）水解物分子量分布圖譜..................... 61
（六）水解物之C4逆相管柱HPLC圖譜............... 66
（七）水解物之C18逆相管柱HPLC圖譜.............. 69
二、電透析脫鹽處理之鹹鴨蛋蛋白液酵素水解物對亞麻油酸自氧化作用 的抑制能力..................................... 73
（一）水解物之胜太濃度與抑制能力的關係......... 73
（二）水解物之IC 50值.......................... 82
三、電透析鹹鴨蛋蛋白液之Protease A、Protease N及Prozyme 6水解物經膜區分物對其抗氧化性的影響................... 86
（一）各膜區分物之產率......................... 86
（二）各膜區分物之胜太含量..................... 88
（三）各膜區分物之表面硫氫基含量............... 90
（四）各膜區分物抑制亞麻油酸自氧化的能力....... 90
（五）各膜區分之胺基酸組成及化學性質區分....... 95
（六）抗氧化活性強之膜區分物進一步再探討其分子量與抑制亞麻油酸自氧化作用的關係................................ 105
第五章　結論.................................. 109
第六章　參考文獻.............................. 110
【表目錄】
表一、雞蛋卵白中主要蛋白質之物理性質............ 5
表二、雞蛋蛋白中主要蛋白質之化學性質............ 6
表三、酵素種類與水解時間對電透析處理之鹹鴨蛋蛋白液水解物抑制亞麻油酸自氧化能力之IC50值的影響................... 83
表四、酵素種類與水解時間對電透析處理之鹹鴨蛋蛋白液水解物抑制亞麻油酸自氧化能力之IC50值的影響................... 84
表五、電透析鹹鴨蛋蛋白液以Protease A, Protease N或Prozyme 6水解之膜區分物的產率............................... 87
表六、電透析鹹鴨蛋蛋白液以Protease A, Protease N或Prozyme 6水解之膜區分物的胜太含量........................... 89
表七、電透析鹹鴨蛋蛋白液以Protease A, Protease N或Prozyme 6水解之膜區分物的表面硫氫基含量..................... 91
表八、電透析鹹鴨蛋蛋白液以Protease A, Protease N或Prozyme 6水解之膜區分物抑制亞麻油酸自氧化的能力............. 92
表九、電透析鹹鴨蛋蛋白液以Protease A, Protease N或Prozyme 6水解之膜區分物抑制亞麻油酸自氧化的能力............. 93
表十、電透析鹹鴨蛋蛋白液以Protease A水解之膜區分物的胺基酸組成............................................. 96
表十一、電透析鹹鴨蛋蛋白液以Protease N水解之膜區分物的胺基酸組成............................................. 97
表十二、電透析鹹鴨蛋蛋白液水以Prozyme 6水解之膜區分物的胺基酸組成............................................. 98
【圖目錄】
圖一、電透析裝置圖............................. 13
圖二、鹹鴨蛋蛋白液以不同酵素水解處理之實驗與分析流程. 41
圖三、鹹鴨蛋蛋白水解物抗氧化性之實驗與分析流程. 42
圖四、鹹鴨蛋蛋白水解物之膜區物經膠體過濾層析劃分後，抗氧化性之實驗與分析流程................................... 43
圖五、酵素種類與水解時間對電透析處理之鹹鴨蛋蛋白液水解物可溶性蛋白質含量的影響................................. 53
圖六、酵素種類與水解時間對電透析處理之鹹鴨蛋蛋白液水解物胜太含量的影響......................................... 55
圖七、酵素種類與水解時間對電透析鹹鴨蛋蛋白液水解物胺基態氮含量的影響........................................... 57
圖八、電透析處理之鹹鴨蛋蛋白液以Papain W-40、PeptidaseR或Proleather FG水解不同時間之SDS聚丙醯胺膠體電泳圖譜. 59
圖九、電透析處理之鹹鴨蛋蛋白液以Protease A、ProteaseN或Prozyme6水解不同時間之SDS聚丙醯胺膠體電泳圖譜.......... 60
圖十、膠體過濾層析分析各標準蛋白質分子量與滯留時間之半對數圖..62
圖十一、電透析處理之鹹鴨蛋蛋白液以Papain W-40、Peptidase R或Proleather FG水解不同時間的胜太管柱HPLC圖譜.... 63
圖十二、電透析處理之鹹鴨蛋蛋白液以Protease A、Protease N或Prozyme 6水解不同時間的胜太管柱HPLC圖譜........ 64
圖十三、電透析鹹鴨蛋蛋白液以Papain W-40、Peptidase R或Proleather FG水解不同時間之C4逆相管柱HPLC圖譜.. 67
圖十四、電透析鹹鴨蛋蛋白液以Protease A、Protease N或Prozyme 6水解不同時間之C4逆相管柱HPLC圖譜................. 68
圖十五、電透析鹹鴨蛋蛋白液以Papain W-40、Peptidase R或Proleather FG水解不同時間之C18逆相管柱HPLC圖譜
圖十六、電透析鹹鴨蛋蛋白液以Protease A、Protease N或Prozyme 6水解不同時間之C18逆相管柱HPLC圖譜................ 71
圖十七、鹹鴨蛋蛋白液以Papain W-40水解之產物胜太濃度與抑制亞麻油酸自氧化能力之關係............................. 74
圖十八、鹹鴨蛋蛋白液以Peptidase R水解之產物胜太濃度與抑制亞麻油酸自氧化能力之關係............................. 75
圖十九、鹹鴨蛋蛋白液以Proleather FG水解之產物胜太濃度與抑制亞麻油酸自氧化能力之關係........................... 77
圖二十、鹹鴨蛋蛋白液以Protease A水解之產物胜太濃度與抑制亞麻油酸自氧化能力之關係............................... 78
圖二十一、鹹鴨蛋蛋白液以Protease N水解之產物胜太濃度與抑制亞麻油酸自氧化能力之關係............................. 80
圖二十二、鹹鴨蛋蛋白液以Prozyme 6水解之產物胜太濃度與抑制亞麻油酸自氧化能力之關係............................. 81
圖二十三、電透析鹹鴨蛋蛋白液之Protease A酵素水解24小時水解物之膜區分物中胺基酸性質的比較...................... 102
圖二十四、電透析鹹鴨蛋蛋白液之Protease N酵素水解18小時水解物之膜區分物中胺基酸性質的比較...................... 103
圖二十五、電透析鹹鴨蛋蛋白液之Prozyme 6酵素水解18小時水解物之膜區分物中胺基酸性質的比較...................... 104
圖二十六、電透析鹹鴨蛋蛋白液之Protease A 24小時水解物的分子量1-3 kDa膜區分物經膠體過濾層析劃分收集後，其劃分物抑制亞麻油酸自氧化的能力...................................... 107
圖二十七、電透析鹹鴨蛋蛋白液之Protease N 18小時水解物的分子量1 kDa以下膜區分物經膠體過濾層析劃分收集後，其劃分物抑制亞麻油酸自氧化的能力.................................... 108

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