臺灣博碩士論文加值系統

摘要

本研究探討以吳郭魚內臟粗酵素液水解蛋白粉 (EAP)、濃縮乳清蛋白 (WPC)、分離大豆蛋白 (SPI) 及吳郭魚肉乾物 (TMP) 等水解物之抗氧化活性。蛋白質基質添加粗酵素液後 pH 調整至 4.0、7.0 及 9.0，於 50℃ 水解12 小時之水解液製成乾物，測定 α,α-diphenyl-β-picrylhydrazyl (DPPH) 自由基清除率、還原力、亞麻油酸過氧化抑制率、亞鐵離子螯合率及超氧陰離子自由基清除率等。整體上，以 WPC 於 pH 7.0 及 SPI 於 pH 4.0 兩者水解物的抗氧化活性較高，但還原力以TMP 於 pH 4.0 的水解物高於其他水解物。其次針對 WPC 於 pH 7.0 與 SPI 於 pH 4.0 進行溫度 (40 及 50℃) 和水解時間 (0~24 小時) 的影響，結果顯示均以 40℃、12 小時水解為較佳的條件。
依據上述結果，WPC 於 pH 7.0 及 SPI 於 pH 4.0 在 40℃ 水解 12 小時之水解液製成乾物，以及水解物再經 80% 乙醇沉澱處理之低分子量區分 (LMW) 同樣製成乾物，比較不同濃度下的抗氧化活性。WPC 組於還原力、亞鐵離子螯合能力、DPPH 自由基及超氧陰離子清除能力等活性高於 WPC-LMW 組，但抑制亞麻油酸過氧化能力則以後者較高。SPI 組於抑制亞麻油酸過氧化能力、亞鐵離子螯合能力、DPPH 自由基及超氧陰離子清除能力等活性高於 SPI-LMW 組，但還原力則以後者較高。四種乾物作比較時，SPI 組之亞麻油酸過氧化抑制率 (IC50 為 0.055 mg/mL)、亞鐵離子螯合率 (IC50 為 18.68 mg/mL) 及超氧陰離子自由基清除率 (IC50 為 0.10 mg/mL) 有最高的活性，而 WPC 組則以還原力 (IC50 為 2.12 mg/mL) 及 DPPH 清除率 (IC50 為 0.89 mg/mL)最高。以 HPLC 法測定 DPPH 自由基清除率之 IC50 值較之分光法降低 36.4~58.9%。
另測定 WPC 於 pH 7.0 及 SPI 於 pH 4.0 在 40℃ 水解 0~24 小時之水解物對血管升壓素轉換酶 (angiotensin I-converting enzyme, ACE) 之抑制能力，結果顯示抑制率隨水解時間的延長而上升，水解 24 小時之水解物的 IC50 值 (0.71~0.96 mg/mL) 的抑制效果低於其低分子量區分乾物 (0.24~0.35 mg/mL )。

Abstract

This study investigated the antioxidative activity in the hydrolysates of egg albumin protein (EAP), whey protein concentrate (WPC), soy protein isolate (SPI) and Tilapia muscle protein (TMP) by using the crude extract of tilapia viscera as the enzyme source. Protein substrates were hydrolyzed at 50℃ for 12 hours at different pH values (4.0, 7.0 and 9.0).The lyophilized hydrolysates were then measure for the scavenging effect on α,α-diphenyl-β-picrylhydrazyl (DPPH) radical, reducing power, inhibition on linoleic acid peroxidation, Fe2+-chelating effect, and scavenging effect on superoxide anion radical. On the whole, the WPC (at pH 7.0) and SPI (at pH 4.0) hydrolysates exhibited higher antioxidative activities, but the TMP (at pH 4.0) hydrolysate had the highest reducing power than other hydrolysates. The WPC (at pH 7.0) and SPI (at pH 9.0) were chosen to evaluate the effect by hydrolsis temperature (40℃ and 50℃) and time (0~24 hours). The results showed that the hydrolysis carried out at 40℃ for 12 hours was a better condition.
Accordingly, the lyophilized hydrolysates of WPC (at pH 7.0) and SPI (at pH 4.0), which were hydrolyzed at 40℃ for 12 hours, together with their low-molecule-weight fractions (LMW), which were treated with 80% ethanol to precipitate proteins were prepared and measured for antioxidative activity at different concentrations. The reducing power, Fe2+-chelating effect, and DPPH radical and superoxide anion scavenging effects in the WPC hydrolysate were higher than that in WPC-LMW. On the contrary, the inhibition on linoleic acid peroxidation were stronger in the latter. The SPI hydrolysate had higher inhibition on linoleic acid peroxidation, Fe2+-chelating effect, and DPPH radical and superoxide anion scavenging effects, but SPI-LMW was higher in reducing power. Among the four lyophilized powders , SPI hydrolysate was the highest in the inhibition on linoleic acic peroxidation (IC50 = 0.055 mg/mL), Fe2+-chelating effect (IC50 = 18.68 mg/mL), and scavenging effect on superoxide anion radical (IC50 = 0.10 mg/mL). On the contrary, the WPC hydrolysate was the highest in reducing power (IC50 = 2.12 mg/mL) and scavenging effect on DPPH radical (IC50 = 0.89 mg/mL). Regarding the measurement on scavenging DPPH radical, here was found that the IC50 values determined by HPLC method decreased by 36.4~58.9% as compared with that by photometric method.
The inhibitory activity against angiotensin I-converting enzyme (ACE) by the lyophilized hydrolysates of WPC (at pH 7.0) and SPI (at pH 4.0) after hydrolyzing at 40℃ for 0~24 hours. The data showed that the inhibitory activity on ACE increased with hydrolysis time. The 24-hour hydrolysates (IC50 = 0.71~0.96 mg/mL) exhibited lower ACE inhibitory activity than their low-molecule-weight fractions (IC50 = 0.24~0.35 mg/mL ).

目 錄
頁次
中文摘要……………………………………………………………I
英文摘要……………………………………………………………III
目錄…………………………………………………………………V
表目錄………………………………………………………………VIII
圖目錄………………………………………………………………IX
壹、研究背景與目的………………………………………………1
貳、文獻整理………………………………………………………3
一、吳郭魚之簡介……………………………………………….3
(一)生態習性.………………………………………………….3
(二)養殖現況……………………………………………………3
(三)加工利用……………………………………………………4
二、蛋白質水解條件…………………………………………….4
(一)化學水解……………………………………………………4
(二)酵素水解……………………………………………………4
1. 酵素種類…………………………………………………5
2. pH 值與溫度………………………………………….…6
3. 酵素濃度…………………………………………………6
4. 抑制劑和食鹽濃度………………………………………7
三、水產食品的酵素…………………………………………….7
四、蛋白質水解物的特性與應用……………………………….8
(一)水產蛋白質來源……………………………………………10
(二)其他動物蛋白質來源………………………………………12
(三)植物蛋白質來源……………………………………………13
五、氧化作用與自由基………………………………………….14
六、抗氧化劑…………………………………………………….16
(一)抗氧化劑的來源……………………………………………16
(二)抗氧化劑作用原理及種類…………………………………17
1.自由基終止.……………………………………………17
2.還原劑或氧清除劑…………….………………………18
3.金屬螯合劑………………………………….…………18
4.單重氧的抑制劑……………………………………….18
參、材料與方法……………………………………………………20
一、材料………………………………………………………….20
1.實驗材料……………………………………………….20
2.化學藥品………………………………………….……20
3.使用儀器…………………………………….…………21
二、實驗項目與方法…………………………………………….21
(一)粗酵素液製備………………………………………………21
(二)粗酵素水解對蛋白抽出物抗氧化活性之影響……………21
1.pH 值的影響……….……………………….…………21
2.水解溫度和時間的影響……………….………………22
3.水解物及低分子量區分乾物不同濃度之抗氧化活性.22
(三)離子交換樹脂管柱分離…………………………….…….23
(四)蛋白水解物之抑制 ACE 活性………………………….…24
1.水解時間之影響……………………………………….24
2.水解物及低分子量乾物於不同濃度之抑制 ACE 活性24
三、化學分析方法……………………………………………….24
(一)抗氧化活性測定……………………………………………24
1.清除 DPPH 自由基能力測定….………………………24
2.還原力測定………………………………….…………25
3.抑制血紅蛋白催化亞麻油酸過氧化之能力……….…25
4.亞鐵離子離子螯合能力.………………………………26
5.捕捉超氧陰離子能力測定……………………….……26
(二)可溶性蛋白質含量測定……………………………………26
(三)胺基含量測定………………………………………………27
1.OPA 呈色法…………………………………………….27
2.Ninhydrin 呈色法…………………………………….27
(四)水解物對抑制 ACE 活性之測定………………………….27
四、統計分析…………………………………………………….28
肆、結果與討論……………………………………………………29
一、水解條件對抗氧化活性之影響…………………………….29
(一) pH 值之影響………………………………………………29
(二)水解溫度和時間的影響……………………………………34
(三)水解物及低分子量區分乾物不同濃度之抗氧化活性……40
二、離子交換樹脂管柱分離…………………………………….44
三、蛋白水解物之抑制 ACE 活性………………………………47
(一)水解時間之影響……………………………………………47
(二)水解物及低分子量區分乾物於不同濃度之抑制 ACE 活
性……………………………………………………………47
伍、結論……………………………………………………………49
陸、參考文獻………………………………………………………51
柒、表………………………………………………………………70
捌、圖………………………………………………………………85

表 目 錄
頁次
表一、蛋白質水解物之清除 DPPH 自由基能力…………………70
表二、蛋白質水解物之還原力……………………………………71
表三、蛋白水質解物之抑制亞麻油酸過氧化能力………………72
表四、蛋白質水解物之亞鐵離子螯合能力………………………73
表五、蛋白質水解物之清除超氧陰離子自由基能力……………74
表六、蛋白質水解物之可溶性蛋白質及胺基含量………………75
表七、不同水解時間及溫度之蛋白質水解物中的可溶性蛋白質及胺
基含量………………………………………………………76
表八、濃縮乳清蛋白和分離大豆蛋白水解物與其低分子量區分之抗
氧化活性 (IC50 值)………………………………………77
表九、濃縮乳清蛋白和分離大豆蛋白水解物與其低分子量區分之可
溶性蛋白質及胺基含量……………………………………78
表十、濃縮乳清蛋白與分離大豆蛋白水解物之中性、正電荷及負電
荷區分之清除 DPPH 自由基能力…………………………79
表十一、濃縮乳清蛋白與分離大豆蛋白水解物之中性、正電荷及負
電荷區分之還原力………………………………………80
表十二、濃縮乳清蛋白與分離大豆蛋白水解物之中性、正電荷及負
電荷區分之抑制亞麻油酸過氧化能力…………………81
表十三、濃縮乳清蛋白與分離大豆蛋白水解物之中性、正電荷及負
電荷區分之亞鐵離子螯合能力…………………………82
表十四、濃縮乳清蛋白與分離大豆蛋白水解物之中性、正電荷及負
電荷區分之清除超氧陰離子自由基能力………………83
表十五、濃縮乳清蛋白與分離大豆蛋白水解物之中性、正電荷及負
電荷區分之胺基含量……………………………………84

圖 目 錄
頁次
圖一、水解溫度和時間對蛋白水解物清除 DPPH 自由基能力之影
響……………………………………………………………85
圖二、水解溫度和時間對蛋白水解物還原力之影響……………86
圖三、水解溫度和時間對蛋白水解物抑制亞麻油酸過氧化之影響
………………………………………………………………87
圖四、水解溫度和時間對蛋白水解物螯合亞鐵離子效果之影響88
圖五、水解溫度和時間對蛋白水解物清除超氧陰離子自由基之影
響……………………………………………………………89
圖六、水解時間 (40℃) 對蛋白水解物抑制 ACE 活性之影響.90
圖七、濃縮乳清蛋白和分離大豆蛋白水解物在不同濃度之抑制ACE
活性…………………………………………………………91
圖八、濃縮乳清蛋白和分離大豆蛋白水解物之低分子量區分乾物
在不同濃度之抑制 ACE 活性…………………………….92
圖九、蛋白質基質於不同pH 值之水解物所含可溶性蛋白質與胺基
含量與抗氧化活性之相關性………………………………93
圖十、濃縮乳清蛋白和分離大豆蛋白於不同水解時間之水解物所
含可溶性蛋白質與胺基含量與抗氧化活性之相關性……94
圖十一、濃縮乳清蛋白和分離大豆蛋白於不同水解時間 (40℃) 之
水解物所含可溶性蛋白質與胺基含量與抗氧化活性之相關
性…………………………………………………………95
圖十二、濃縮乳清蛋白和分離大豆蛋白於不同水解時間 (50℃) 之
水解物所含可溶性蛋白質與胺基含量與抗氧化活性之相關
性…………………………………………………………96
圖十三、濃縮乳清蛋白和分離大豆蛋白之水解物及其低分子量區分
物在不同濃度之抑制亞麻油酸過氧化能力……………97
圖十四、分別以分光法和 HPLC 法測定濃縮乳清蛋白與分離大豆蛋
白之水解物及其低分子量區分物在不同濃度之 DPPH 自由
基清除能力………………………………………………98
圖十五、濃縮乳清蛋白和分離大豆蛋白之水解物及其低分子量區分
物在不同濃度之還原力…………………………………99
圖十六、濃縮乳清蛋白和分離大豆蛋白之水解物在不同濃度之亞鐵
離子螯合能力……………………………………………100
圖十七、濃縮乳清蛋白和分離大豆蛋白之水解物及其低分子量區分
物在不同濃度之清除超氧陰離子自由基能力…………101

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