臺灣博碩士論文加值系統

原料豆渣 (Okara) 先以70℃，20分鐘預熱促進水解後，經脫脂 (Hexane)、加鹼分解 (2N NaOH) 等電點沉澱 (Isoelectric point precipitation) 製備成大豆豆渣分離蛋白 (Okara protein isolate, OPI)，並經酵素水解製備大豆豆渣水解物 (Okara protein hydrolysates, OPIH)。酵素水解分成兩種方式，單一酵素水解採用一種酵素進行，使用酵素包括Alcalase, Protamex, Flavourzyme及Papain；兩階段水解 (Two-stage hydrolysis) 採用Protamex及Flavourzyme。在兩階段水解時，第一階段水解條件為：Protamex, 5 % 豆渣溶液、酵素濃度E/S=1 %、50℃、pH 7.0及120分鐘，第二階段水解條件：Flavourzyme, 酵素濃度E/S=0.5%、50℃、pH 7.0及60分鐘，於180分鐘之總水解時間可以得到水解度 (Degree of hydrolysis) 22.3% 之水解液，以二階段雙酵素可得到苦味低及水解度較高之產品。
兩階段水解大豆豆渣水解液經不同分子量限值 (Molecular weight cut- off , MWCO) 之三種超濾膜 (1kDa、3kDa及10kDa) 連續操作，可得不同區分物 (Fractions)，區分物可分成濾液 (Permeates, Per) 及保留液 (Retentate, Ret)，各區分物分別測試氫氧自由基 (Hydroxyl free radicals) 及ABTS‧＋自由基 (ABTS‧＋ free radicals) 之清除能力 (Scavenging activity)。結果顯示，水解物 (OPIH) 在濃度10 mg/mL時可顯著清除ABTS‧＋及氫氧自由基 49 %以上，超濾後小分子量之濾液如Per 3 (3 kDa> MW > 1kDa) 及Per4 (MW < 1kDa) 為例，在濃度10 mg/mL時對自由基清除率可達85 %，此效果與BHA及Ascobic acid 用量為1.0 mg/mL時之自由基清除率相近。
本研究也探討豆渣分離蛋白及其水解區分物對血管收縮素轉化酶 (Angiotensin-I converting enzyme, ACE) 的抑制能力。豆渣分離蛋白未水解前抑制能力 IC50值為39.1mg/mL，經二階段水解後其IC50值降為0.56 mg/mL，小分子量區分物Per 4之抑制能力 IC50值更降低到0.09 mg/mL，抑制能力約為抗高血壓學名藥Enalapril IC50之25 % 用量之效力。水解物之胺基酸組成分析顯示，經酵素水解後疏水性胺基酸 (HydrOPIHobic amino acid) 佔全體之40.08%，且含高量脯胺酸 (Pro) 及白胺酸 (Leu)，這些胺基酸組成與抗氧化及抑制ACE有關。
豆渣兩階段水解液及其區分物加入3T3-L1分化成熟脂肪細胞中，以測試其是否具有增強促進成熟脂肪細胞脂肪分解 (Lipolysis) 之能力。以400ppm之水解液及100 ppm之小分子量水解區分物 (Per 4) 皆可降低脂肪聚集 (Relative lipid accumulation, RLA) 達37%，並使丙三醇 (Glycerol) 之釋放量提高108.3 %。從 Oil Red O細胞染色中明顯觀察到Per 4 (MW<1000Da) 濾液區分物具有使脂肪油滴分解之現象。
由二階段水解及超濾膜所製成之豆渣水解液及區分物其中之小分子量Per 4具有抑制ACE及促進脂肪分解之功效，而小於3 kDa之區分物（Per 3及Per 4）也具有良好的抗氧化功效。

Okara was heated (70℃, 20 min), defatted with hexane, alkaline-treated (2N NaOH) and precipitated at isoelectric point to obtain okara protein isolate (OPI). OPI was further hydrolyzed with proteases either by single enzyme (including Alcalasem, Protamex, Flavourzyme and Papain) or by two-stage hydrolysis consisting of Protamex and Flavourzyme. In the first stage of the two-stage hydrolysis, Protamex was used with the hydrolysis conditions of 5% substrate concentration, E/S=1%, 50℃, pH 7.0 and 120 min; and the hydrolytic product was denoted as P120. In the second stage, Flavourzyme was used with the hydrolysis conditions of E/S=0.5%, 50℃, pH 7.0 and 60 min; and the hydrolytic product was denoted as P120+F60. The results showed that two-stage hydrolysis could achieve the degree of hydrolysis (DH) of OPI to 22.3% with less bitter taste.
P120+F60 was consecutively separated into four fractions (denoted as Ret 1 , Per 2, Per 3and Per 4) by ultrafiltration membranes with molecular-weight cut-off (MWCO) of 10kDa, 3kDa and 1kDa.The four fractions as well as OPI, P120 and P120+F60 were tested for their hydroxyl and ABTS free radical scavenging activities. The scavenging activities for both free radicals were more than 49% when the concentration of P120+F60 was 10 mg/mL. However, the scavenging activities for both free radicals were 85% when Per 3 and Per 4 were used at the level of 10 mg/mL, which was comparable to BHA and ascorbic acid at the level of 1.0 mg/mL.
The inhibitory activities of angiotensin-I converting enzyme (ACE) of the above okara protein products were also tested. The IC50 values for OPI, P120+F60 and Per 4 were 39.1, 0.56 and 0.09 mg/mL, respectively. The inhibitory activity of Per 4 was about one fourth of the antihypertension drug Enalapril. The amino acid composition analysis revealed that the content of hydrOPIHobic amino acid was 40.08%, and the high level of prolein and leucine might partly explain the antioxidant and anti-AGE activities.
The ability of OPI and hydrolysate fractions for catalyzing lipolysis in differentiated 3T3-L1 adipocytes was tested. Relative lipid accumulation (RLA) was decreased by 37% and the glycerol release was increased by 108.3% when P120+F60 at the level of 400 ppm and Per 4 at the level of 100 ppm were used. Disintegration of fat drops was observed when adipocytes were stained with Oil-Red O.

第一章目錄 i
表目錄 v
圖目錄 vi
中文摘要 10
英文摘要 (Abstract) 12
壹、前言 14
貳、文獻整理 16
一、原料豆渣介紹 16
二、脫脂大豆豆粕 17
三、生物活性肽來源 18
四、生物活性肽之生理功能 20
(一) 延緩血壓 (Blood pressure) 上升 20
(1) 高血壓與血管收縮素轉化酶
(Angiotensin converting enzyme, ACE) 20
(2) 抑制ACE之原理及胜肽結構特性 24
(3) 蛋白水解物對血壓的影響 24
(4) 大豆蛋白水解物與血壓之關係 28
(二) 抗氧化作用 (Antioxidation) 28
(1) 自由基 (Free radicals) 及抗氧化作用 28
(2) 天然抗氧化物質 31
(3) 抗氧化胜肽之結構特性 32
(4) 大豆及豆渣之抗氧化之作用 32
(三) 抗肥胖 (Anti-obecity) 與體重控制 (Weight control) 35
(1) 脂肪組織 (Adipose tissue) 35
(2) 3T3-L1前脂肪細胞株 (3T3-L1 Preadipocytes) 36
(3) 脂肪細胞研究模式 36
(4) 脂肪細胞分化 (Cell differentiation) 過程 37
(5) 大豆蛋白水解物抑制脂肪聚集 (Inhibit lipid accumulation)
及促進脂肪分解 (Lipolysis) 功能 39
五、大豆胜肽的製備方法 42
(一) 酵素水解法 42
(1) 絲胺基酸型蛋白質分解酵素 (Serine proteases) 43
(2) 硫醇型蛋白質分解酵素 (Thiol proteases) 43
(3) 金屬型蛋白質分解酵素 (Metalloproteases) 43
(4) 酸性型蛋白質分解酵素 (Acid protease) 43
(二) 微生物發酵法 45
六、大豆胜肽之分離 (Separation)、純化 (Purification) 與
鑑定 (Identification) 45
七、超過濾技術 (Ultrafiltration) 46
八、酵素水解物之特性 47
(一) 高溶解度 (Solubility)、低黏度 (Viscosity) 及加工穩定性 47
(二) 高消化性及低過敏性 47
(三) 苦味物質產生 48
參、實驗架構 49
肆、實驗材料 50
一、材料 50
二、儀器設備 50
三、實驗藥品 51
伍、 實驗方法 53
一、大豆豆渣分離蛋白 (Okara protein isolate) 之製備 53
(一) 去油大豆豆渣粉 (Defaterd okara flours) 之製備 53
(二) 大豆豆渣分離蛋白 (Okara protein isolates, OPI) 之製備 53
二、OPI高水解度蛋白酶之篩選 53
(一) 商業混合酵素水解豆渣之條件探討 53
(二) 二階段水解法 54
(三) OPI水解產物分析 56
(1) 水解度 (Degree of hydrolysis, DH) 56
(2) 總氮及產量 (Yield) 測定 57
(3) 回收率 (Recovery) 的計算 57
(4) 胜肽濃度 (Peptide concentration) 測定 57
三、濾膜的系統操作條件之建立 59
(一) 批式超過濾操作流程 59
(二) 連續式酵素膜反應系統 (Enzyme membrane reactor system) 59
四、水解液之分子量測定及區分 60
五、OPI水解物及其濾膜區分物之生理活性測定 60
(一) 抗氧化活性 (Antioxidative activity) 測定 60
(1) DPPH自由基清除能力測定 60
(2) ABTS‧＋自由基清除能力 61
(3) 氫氧自由基清除能 (Hydroxyl radicalscavanging activity) 62
(二) 水解物及其濾膜區分物中收縮素I轉化酵素 (Angiotensin-
I converting enzyme, ACEI) 抑制活性測定 69
(1) ACEI抑制活性測定方法 69
(2) ACE抑制活性計算 69
(3) IC50值的測定 70
(三) OPI水解物及其區分物之促脂解 (Lipiolysis) 活性 70
(1) 細胞培養 70
(2) Oil red O染色及相對脂肪累積
(Relative lipid accumulation, RLA) 73
(3) 丙三醇 (Glycerol) 釋放量檢測 73
(4) 三酸甘油酯 (Triglyceride) 含量檢測 73
(5) 蛋白質定量 74
六、胺基酸組成 (Amino acid composition) 分析 75
七、計算水解混合物胜肽之F值 (Fischer ratio) 75
八、統計分析 75
陸、結果與討論 76
一、酵素水解豆渣蛋白試驗 76
(一) 一階段酵素水解 76
(二) 二階段酵素水解 76
二、水解條件對豆渣蛋白水解度之影響 77
三、前處理加熱對水解度之影響 79
四、超濾操作及酵素模反應系統 88
五、大豆豆渣分離蛋白水解物抗氧化能力 90
(一) 清除DPPH自由基能力 90
(二) 水解及超濾區分物對ABTS‧＋自由基清除能力之影響 90
(三) 水解及超濾區分物對氫氧自由基 (Hydroxyl radical)
清除能力之影響 91
六、批式酵素膜反應系統水解物分子量分布情形 97
七、連續式酵素模反應系統與批式系統之比較 97
八、大豆豆渣水解產率 (Yield) 102
九、OPIH及超濾區分物對血管收縮轉化酶 (ACE) 抑制能力 105
十、胺基酸分析 109
(一) 水解及超濾區分物胺基酸分析 109
(1) 水解物及區分物中必需胺基酸 109
(2) 水解物及區分物中氨基酸與ACEI之關係 109
(二) 水解及超濾區分物支鏈胺基酸
(Branched chain amino acids, BCAA) 110
(三) 水解物及區分物中氨基酸與抗氧化能力之關係 111
十一、水解條件對相對脂肪堆積量
(Relative lipid accumulation, RLA%) 之影響 113
十二、大豆豆渣水解物對促進脂肪分解 (Lipiolysis) 之影響 116
十三、大豆豆渣蛋白水解液超濾區分物對促進脂肪分解之影響 120
十四、大豆豆渣水解超濾區分物前脂肪細胞油紅染色顯微鏡觀察 120
十五、促進脂肪分解機制探討 122
柒、結論 127
捌、參考文獻 128
第二章目錄

目錄 i
表目錄 v
圖目錄 vi
中文摘要 151
英文摘要 (Abstract) 152
壹、前言 153
貳、文獻整理 154
一、蛋白質的功能特性 (Fumctional properties) 154
(一) 水合性質 (Hydration properties) 154
(二) 沉澱與凝膠 (Gelling) 作用 154
(三) 表面性質 (Surface properties) 154
二、大豆蛋白質的功能特性 (Functional properties) 154
(一) 蛋白質溶解度 (Protein solubility, PS) 154
(二) 表面疏水性 (Surface hydrOPIHbicity, Ho) 155
(三) 乳化能力 (Emulsifying capacity) 與乳化安定性
(Emulsifying stability) 155
(四) 起泡能力 (Foaming capacity) 與起泡安定性
(Foaming stability) 156
(五) 影響泡沫生成與安定性的因子 157
(1) 蛋白質的結構 157
(2) 蛋白質的濃度 157
(3) 溫度 157
(4) pH和離子強度 (Ionic strength, I) 157
三、酵素水解對蛋白質功能特性之影響 157
(一) 蛋白質溶解度與表面疏水性 157
(二) 乳化能力與乳化安定性 158
(三) 起泡能力與起泡安定性 159
四、實驗目的 160
参、實驗材料 161
一、材料 161
二、儀器設備 161
三、實驗藥品 161
肆、實驗方法 163
一、豆渣分離蛋白水解物之胜肽製備 163
(一) 去油大豆豆渣粉 (Defatted okara flour) 之製備 163
(二) 大豆豆渣分離蛋白 (Okara protein isolate, OPI) 之製備 163
(三) 大豆豆渣蛋白水解物 (Okara protein hydrolysate, OPIH)
之製備 163
(1) 單階段水解 163
(2) 二階段水解 163
二、大豆豆渣蛋白水解物之超濾 (Ultrafiltration) 164
三、大豆豆渣水解酵素及超濾區分物對功能性質之影響 164
四、實驗分析方法 164
(一) 蛋白質定量 (Protein assay) 164
(二) 蛋白質溶解度 (Protein solubility, PS%) 164
(三) 表面疏水性 (Surface hydrophobicity) 165
(四) 乳化能力指數 (Emulsifying activity index, EAI) 及乳化
安定指數(Emulsifing stability index, ESI) 166
(五) 起泡能力 (Foamung capcity, FC %) 及泡沫穩定度
(Foaming stability, FS %) 166
五、計算分析 167
伍、結果與討論 168
一、酵素水解及超濾對蛋白質溶解度(Protein solubility) 之影響 168
二、酵素水解及超濾對表面疏水性 (Surface hydrophobicity, Ho)
之影響 171
三、水解及超濾之分子量分布圖 (Molecular weight distribution) 172
四、酵素水解及超濾對乳化性質 (Emulsifying properties) 之影響 132
五、泡沫性質 179
六、功能性質之利用之相關性 183
陸、結論 184
柒、參考文獻 185
第三章目錄

目錄 i
表目錄 v
圖目錄 vi
中文摘要 199
英文摘要 (Abstract) 200
壹、前言 201
貳、文獻整理 202
一、豆渣 (Okara) 之利用 202
二、低脂漢堡肉 (Low fat burger) 與脂肪取代物 (Fat replacer) 203
(一) 蛋白質基礎 (Protein base) 之取代物 203
(1) 乳清 (Whey) 203
(2) 膠原蛋白 (Collagen) 204
(3) 大豆蛋白 (Soy protein) 204
(二) 脂肪 (Fat-base) 為主體之取代物 205
(三) 碳水化合物 (Carbohydrate) 為主體之取代物 205
(1) 纖維 (Fiber) 205
(2) 膠類 (Gums) 206
(3) 多種混合物 206
三、漢堡肉之風味感官品評 206
四、可溶性膳食纖維 (Soluble dietary fiber) 207
五、大豆膳食纖維 (Dietary fibers) 之生理功能與製程技術 208
參、實驗材料 210
一、材料 210
二、儀器設備 210
三、實驗藥品 211
肆、實驗方法 212
一、濕豆渣一般成分分析 212
(一) 水分含量 (Moisturr content) 212
(二) 粗蛋白分析 212
(三) 粗脂肪 (Crude fat) 212
(四) 灰份 (Ash) 212
(五) 膳食纖維 (Fotal dietary fiber) 分析 213
二、濕豆渣前處理 214
三、濕豆渣之酵素水解 217
四、豬肉漢堡肉之製備 217
五、添加濕豆渣豬肉漢堡品質變化 217
(一) 色澤 (Color) 217
(二) 烹煮損耗 (Cook loss) 219
(三) 肉品收縮度 (Dimensional shrinkage) 219
(四) 保水能力 (Water-holding capacity, WHC) 測定 219
(五) 膽固醇 (Cholesterol) 測定 220
(六) 感官品評 220
六、統計分析 220
伍、結果與討論 223
一、濕豆渣原料及豬肉漢堡一般成份分析 223
二、豆渣可溶性膳食纖維之提升 223
(一) 加熱前處理對可溶性膳食纖維之影響 223
(二) 纖維分解酵素處理對可溶性膳食纖維之影響 224
三、添加濕豆渣對豬肉漢堡成份之影響 225
四、添加濕豆渣對豬肉漢堡之影響 232
(一) pH值 232
(二) 烹煮流失 (Cook loss) 232
(三) 色澤 (Color) 232
(四) 膽固醇 (Cholesterol) 235
(五) 感官品評 (Sensory evaluation) 235
陸、結論 238
柒、參考文獻 239

第一章、參考文獻

崔泳菱。2010。以3T3-1前驅脂肪細胞篩選具有降三酸甘油酯作用之大豆胜肽。東海大學食品科學研究所碩士論文
鄒梅君、盧錫祺、趙佳宏、江文德。2010。利用超濾膜區分中性蛋白酶一大豆蛋白水解物中具脂解促進作用的胜肽。台灣農業化學與食品科學 48 (3) : 120-127。
AACC Report 2001. The definition of dietary fiber. American Asociation of Cereal Chemists’
Achour, A., Zhang, W.Z. and Shiying, X. 1998. Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resultjng protein hydrolysates Food Research International 31 (9) : 617-623.
Adler-Nissan. J. 1979. Determination of degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. Journal of Agricultural and Food Chemistry 27: 1256-1262.
Adler-Nissen, J. 1986. Enzymic hydrolysis of food protein. New York; Elsevier Supplied Science Publishers, pp. 110-169.
Aoyama, T., Frukui, K., Takamatsu, K. Hashimo. Y. and Yamamoto, T. 2000. Soy protein isolate and its hydrolysates reduce body fat of dietary obese rats and genetically obese mice (yellow KK). Nutrition 16:349-354.
Barmes, S., Kirk, M. and Coward, L. 1994. Isoflavone and their conjugates in soy food: Extraction conditions and analysis by HPLC-mass spectrometry. Journal of Agricultural and Food Chemistry 42: 2466-2474.
Becker, G.C. 1993. Preserving food and health: antioxidants make functional, nutritious preservations. Food Processing 12: 54-56.
Benavente-Gaecia, O., Castillo, J., Marin, F.R. and Rio, A.D. 1997. Uses and properties of citrus flavonoids. Journal of Agricultural and Food Chemistry 45: 4505-4515.
Blois, M.S. 1958. Antioxidant determination by the use of a stable free radical Nature 181: 1199-1200.
Bucolo, G. and David, H. 1973. Quantitative determination of serum triglycerides by the use of enzyme. Clinical Chemistry 19: 476-482.
Chen, H.M., Muramoto, K. and Yamauchi, F. 1995. Structural analysis of antioxidative peptides from soybean beta-conglycinin. Journal of Agricultural and Food Chemistry 43: 574-578.
Chen, H.M., Muramoto. K., Yamauchi, F. and Nokihara. K. 1996. Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein. Journal of Agricultural and Food Chemistry 44: 2619-2623.
Chen, H.M., Muramoto, K., Yamauchi, F. and Nokihara, Fuliruoto, K. and Nokihara. K. 1998. Antioxidative properties of histidine-containing peptide designed from peptide frogments found in the digests of soybean protein. Journal of Agricultuyal and Food Chemistry 46:49-53.
Chiang, W.D., Chin, C.J. and Chu, Y.W. 1999. Functional properties of soy protein hydrolysates produced from a continuous membrane reactor system. Food Chemistry. 65: 189-194.
Chiang, W.D., Tsou, M.J., Tsai, Z.Y. and Tsai, T.C. 2006. Angiotensin I-converting enzyme inhibitor derived from soy protein hydrolysates and produced by using membrane reactor. Food Chemistry 98: 725-732.
Chobanian, A.V., Bakris, G.L., Black, H.R. 2003. Seventh Report of the Joint National Committee on Prevention, Detection, Evaluation, and Treatment of High Blood Pressure.Hypertension 42 (6): 1206–1652.
Chung, S.K., Osawa, T. and Kawakishi, S. 1997. Hydroxyl radical scavenging effects of spices and scavengrs from brown mustard. Bioscience,Biochemical and Biotechnology 61: 118-123.
Church, F.C., Swaisgood, H.E., Porter, D.H. and Catignani, G.L. 1983. SpectrOPIHotometric assay using O-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. Journal of Dairy Science 66:1219-1227.
Cowherd, R.M., Lyle, R. and McGeHee, R, E. 1999. Molecular regulation of adipocyte differentiation. Semilar Cell Developement and Biology 10: 3-10.
Darlington, G., Ross, S.E. and MaDomald, B. 1998. The role of C/EBP gene in adipocyte differentiation. Biology Chemistry 273 (46): 3057-3060.
Deeslie W.D. and Cheryan, M. 1992. Fractionation of soy protein hydrolysates using ultrafiltration membrane. Journal of Food Science 57 (3): 411-413.
Deleo, F., Panarese, S., Gallerani, R. and Ceci, L.R. 2009. Angiotensim converting enzyme (ACE) inhibitory peptidel: production and implementation of functional food. Current Pharmaceutical Design 15 (31): 3622~3643.
Erdmann, K., Cheung, B.W.Y. and Schroder, H. 2008. The possible roles of food-derived bioactive peptides in reducing the risk of cardioxascular disease. Journal of Nutrition Biochemical and Molecular Medicine 19: 643-654.
Field, A.E., Coakley, E.H., Must, A., Spadano, J.L., Laird, N., Dietz, W.H., Rimm, E.and Colditz, G. A. 2001. Impact of overweight on the risk of developing common chronic diseases. during a 10-year period. Pharmaceutical and Medicinal 161:1581-1586.
Fujita, H., Yoshilawa, M., and Lkpnm, A. 1999. Prodrug-type ACE-inhibitory peptide derived from fish protein. ImmunologicalPharmacology 44. 123-127.
Gibbs, B.F., Zougman, A., Masse, R. and Mulligan, C. 2004. Production and characterization of bioactive peptides from soy hydrolysates and soy-fermented food. Food Research International 37: 123-131.
Gobbetti, M., Stepaniak, L., De Angelis, M., Corsetti, A., and Cagno, R. 2002. Latent bioactive peptides in milk proteins: proteolytic activation and significance in dairy processing. Critical Reviewin Food Science and Nutrition 42 (3): 223-239.
Goosen, M.F.A., Sablani, S.S., Al-Himal, H., Al-Belushi, R. and Jackson, P. 2004. Fouling of reverse osmosis and ultrafiltration membranes: Critical Review Sepration Science and Technology 9 (10): 2261-2298
Green, H. and Kehinde, O. 1974. Subline 3T3 cells that accumulate lipid. Cell 113-116.
Green, A., Rumberger, J. Stuart, C.A. and Ruhoff, M.S. 2004. Stimulation of lipolysis by tumor necrosis factors in 3T3-L1 adipocytes is glucose dependent. Diabetes 53: 74-81.
Green, H. and Kehinde, O. 1975. An established preadipose cell line and its differention in culture factors affecting the adipose conversion. Cell 5:19-27.
Gregoire, F.M. Smas, C.M. and Sul, H.S. 1998. Understanding adipocyte differentiation. Physiology Review 78: 783-809.
Guadix, A., Camacho, F. and Guadix, E.M. 2006. Production of whey protein hydrolysates with reduced antigencity in a stable membrane reactor. Journal of Food Engineering 72: 398-405.
Hartmann, R. and Meisel, H. 2007. Food-derived peptides with biological activity: from research to food applications. Current Opinion in Biotechnology 18: 163-169.
Harmon, A.W. and Harp, J.B. 2001. Differential effects of flavonoids on 3T3-L1 adipogenesis and lipolysis. Americian Journalof Cell Physiology C807-C814.
Haslaniza. H., Markal M.Y., Wan, A.W.M. and Marot. S. 2010. The effect of enzyme concentration temperature and incubation tine on nitrogen counter and degree of protein precipitate from cockle meat wash water. International. Food Research Journal 17: 147-152.
Hata, Y., Yamamoto, M., Ohni, M., Nakajima, K., Nakamura, Y. and Takano, T. 1996. A placebo-controlled study of the effect of sour milk on blood pressure in hypertensive subjects. American Journal of Clinical Nutrition 64: 767-771.
He, J., Jiang, H., Tansey, J.T., Pu, S. and Xu, G. 2006. Calyculin and okadaic acid promote perilipin phosphorylation and increase lipolysis in primary rat adipocyte. Biochemica et BiOPIHysica ACTA 1761: 247-225.
Heranandez-Ledesma, B., Davalos, A., Bartolome, B. and Amigo, L. 2005. Preparation of antioxidant enzymatic hydrolysates from alpha-lacto albumin and beta-lactoglobulin. Identification of active peptides by HPLC-MS/MS. Journal of Agricultural and Food Chemistry 53: 588-593.
Hong, Y.S., Lee, K.Y. and Lee, C.H. 2011. Molecular weight distribution of weakly acid-treated wheat gluten. Food Science and Technology Research (2): L26-L30.
Hong, F. Ming, L. Yi, S. Zhanxia, L. Yangquan, W. and Chi, L. 2008. The antihypertensive effect of peptides: A novel alternative to drug? Peptides. 29: 1062-1071.
Jaworski, K., Sarkadi-Naggy, E., Duncan, R.E., Ahmadian, M. and Sue, H.S. 2006. Rrgulation of triglycevied metabolismⅣ. Hormonal regulation of lipolysis in adipose tissue. Gastrointestinal Journal of Physiology 293: G1-G4.
Jequier, E., and Tappy, L. 1999. Regulation of body weight in humans.Physiology Review 79: 451-480.
Jimenez-Escrig, A., Alaiz, M., Viogul, J. and Ruperez, P. 2010. Health-promoting activities of ultrafiltraed okara protein hydrolysates released by in of active peptide from soy bean eipoxygenase. Europe Food Ressearch and Technology 230: 655-663.
Kalyanaraman. B. 2004. Redox-active metal, reactive oxdical biology and apoptosis (Review). Free Radical Biology and Medicine 37 (5): 582-593.
Kao, F.J., Chou, M.J., Kao, H.C., and Chiang, W.D. 2011. Optimization of enzymatic hydrolysis condition for producing soy protein hydrolysates with maximum lipolysis-stimulating activity. Journal Food and Drug Analysis 19 (2): 197-201.
Kapel, R., Chabeau, A., Lesage, J., Riviere, G., Ravallecple, R. Lecouturier, D., Wartelle, M., Guillochon, D. and Dhulster, P. 2006. Production in continuous enzymatic membrane reactor of antihypertensive hydrolysate from an industrial white protein concerntrate exhibiting ACE inhibitory and opioid activities. Food Chemistry 98: 120-126.
Karaki, H., Doi, K., Sugano, S., Uchiwa, H., Murakmi, U. and Takemmoto, S. 1990. Antihypertensive effect of tryptic hydrolysates of milk casein in spontaneously hypertensin rat. Comparative Biochemistry and Physiology 96: 367-371.
Kawasaki, T., Seki, E., Osajima, K., Yoshicl, M., Asada, K., Matswi, T. and Osajima, Y. 2000. Antihypertensive effect of valyl-tyrosine, a short chain peptide derived from sardine muscle hydrolyzate, on mild hypertensive subjects. Journalof Human Hypertension 14: 519-523.
Kim, S.E., Kim, H.H., Kim, J.Y., Kang, Y.I., Woo, H.J. and Lee, H.J. 2000. Anticancer activity of hydrOPIHobic peptides from soy proteins. BioFactors 12 (14):151-155.
Kim, S. Je, J.E. and Kim, S.K. 2007. Purification and characterization of antioxidative peptides from bovine skin. Journal of Biochemical and Molecular Medicine. 34: 279-224.
Kim, H.K., Della-Fera, M.A. and Baile, C.A. 2006. Docosahexaenoic acid inhibits adipocyte differentiation and induces apoptosis in 3T3-1 pereadipocytes. Journal of Nutrition
Kitts, D.D. and Weller, K. 2003. Bioactive proteins and peptides from food sources, Applications of bioprocesses used in isolation and recovery. Current Pharmaceutical Design 9: 1309-1323.
Kodera, T. and Nio, N. 2006. Identification of angiotensin I-converting enzyme inhibitory peptides from protein hydrolysates by a soybean protease and the antihypertensive effects of hydrolysates in spontaneously hypertensive model rats. Journal of Food Science 71: C164-C173.
Korhonen, H., Pihlanto Leppälä, A. Rantamäki, P and Tupasela, T. 1998. Impact of processing on bioactive proteins and peptides. Trends in Food Science and Technology 9:307-319.
Korhonen, H. and Pihlanto, A. 2003. Food derived bioactive peptides;opportunities for designing future foods. Current Pharmaceutical Design 9 (16):1297-1308.
Korhonen, H. and Pihlanto, A. 2006. Bioactive peptides: production and functionality. International Dairy Journal 16: 945-960.
Kuan Y.H. and Liong, M.T. 2008. Chemical and physicochemical characterization of agrowaste fibrous materials and residue. Journal of Agricultural and Food Chemistry 56: 9252-9257.
Kuba, M., Tana, C., Tawata, S. and Yasuda, M. 2005. Production of angiotensin I converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase. Biochemical and Molecular Medicine 40: 2191-2196.
Langin, D. 2006. Adipose tissue lipolysis as a metabolic pathway to define pharmacological strategies against obesity and the metabolic syndrome. Pharmaceutical Research 53: 482-491.
Lahl, W.J. and Braun, S.D. 1994. Enzymatic production of protein hydrolysates for food use. Food Technology 48 (10): 68-71.
Leaflet, A.S. 2004. Okara: A possible high protein feedstuff for organic pig diets. Iowa State University Animal Industry Report.
Lee, S. J., Franks, P. D. and Spangenburg, E. E. 2001. Glycogen a diglycogen phosphorylase associated with sarcoplasmic retieulum: effects of fatiguing activity. Journal of Applied Physiology 91 (4): 1638-1644.
Leo, D., Panarese, S., Gallerani, R. and Ceci, R. 2009. Angiotensin converting enzyme (ACE) inhibitory peptide production and implementation of functional food. Current Pharaceutical Design 15 (31): 622-3643.
Li, C., Matsui T., Matsumoto K., Yamasaki, R. and Kawasaki, T. 2002. Latent production of angiotensin I-converting enzyme inhibitors from buckwheat protein. Journalof Peptide Science 8 (6): 267-274.
Lovati, M.R., Manzoni, C., Corsini, A., Granata, A., Frattini, R., Fumagalli, R. and Sirtori, C.R. 1992. Low-density lipoprotein receptor activity is modulated by soybean globulins in cell culture. Journal of Nutrition 122: 1971-1978.
Ma, C.Y., Lin, W.S., Kwok, K.C. and Kwok, F. 1997. Isolation and characterization of proteins from soymilk residue (Okara). Food Research International 29: 799-805.
Mahmoud, M.I. 1994. Physicochemical and functional properties of hydrolysates in nutritional products. Food Technology 48: 89-95.
Maruyama, S., Nakagomi, K., Tomizuka, N. and Suzuki, H. 1985. Angiotensin I-converting enzyme inhibitor derived from enzymatic hydrolysates of the ileum of rats. Agricultural and Biology Chemistry 49 (5): 1405-1409.
Mateos-Aparicio, I., Mateos-Peinado, C. and Ruperez, P. 2010. High hydrostatic pressure improves the tunctionality of dietary fiber in okara by-product from soybean. Innovative Food Science and Emerging Technology 11:445-450.
Making, S., Nakashima, H., Minami, K., Moriyama, R. and Takao, S. 1988. Bile acid-binding protein from soybean seed: isolation, partial characterization and insulin-stimulating activity. Agricultural Biological Chemistry 52: 803-809.
Matsumoto, K., Watanabe, Y. and Yokoyama, S. 2001. Okara, soybean residue, prevents obesity in a diet-induced murine obesity model. Bioscience, Biotechnology, Biochemical and Molecular Medicine 71 (3): 720-727.
Menduis, E., Rajapack, N and Kim, S.K. 2005. Antioxidant properties of a radical-scavenging peptide purified from enzymaticueey prepaeed fish sikn glatin hyolloeysater. Journal of Agricultural and Food Chemistry 53:581-587.
Minguell, J.J., Erices, A.and Coget, P. 2005. Mesenchymal stem cell Experimental Biology and Medicine 226 (6): 507-520.
Moriyama, T. Kishimoto, K. Nagai, K. Urade, R. Ogawa, T. and Utsumi, S. 2004. Soybean beta-conglycinin diet suppresses serum triglyceride levels in normal and genetically obese mice by induction of beta-oxidation, downregulation of fatty acid synthase, and inhibition of triglyceride absorption. Bioscience Biotechnology Biochemical and Molecular Medicine 68: 352-359.
Morimoto, C., Tsujita, T. and okuda, H. 1997. Norepinephrine-induced lipolysis in rat cells from visceral and subcutaneous sites. Journal of Lipid Research 38: 132-138.
Murray, B.A. and FitzGerald, R.J. 2010. Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemical and Molecular Medicineistry, bioactivity and production. Current Pharmaceutical Design13 (8): 773-791.
Murase, H., Nagao, A. and Terao, A. 1993. Antioxidant and emulsifying activity of N-(long-chain-acyl) Histidine and N (long-chain-acye) carnosine. Journal of Agriculture and Food Chemistry 41: 1601-1604.
Mullally, M.M., Meisei, H. and Fitzgerald, R.J. 1990. Synthetic peptides corresponding to beta-Lactalumin and β-eactoglobulin sequence with angiotensin I-converting enzyme inhibitory activity. Biology Chemistry 377: 259-260.
Nagata, Y. Ishiwaki, N. and Sugano, M. 1982. Studieson the mechanism of antihypercholesterolemic action of soy protein and soy proteintype amino acid mixtures in relation to the casein counterparts in rats. Journal of Nutrition 112: 1614-1625.
Napolitano, A. Lanzuise, S. Ranieri, R. and Fogliamo, V. 2006. Treatment of cereal products with a tailord preparation of Teichoserma enzymes increase the amount of soluble dietary fiber. Journal of Agricultural andFood Chemistry 254 (20): 7863-7869.
Nakamura, Y.,Yamanoto, N., Sakai, K., Okubo, A., Yamazaki, S. and Takano, T. 1995. Purification and characterization of anti angiotensin I-converting enzyme inhibitors from sour milk. Journal Dairy Science 78: 777-783.
Nishi, T., Hara, H., Asano, K. and Tomita, F. 2003. The soybean beta-conglycinin beta 51-63 fragment suppresses appetite by stimulating cholecystokinin release in rats. Journal of Nutrition 133 (8): 2537-2542.
Ntamb, J.M.and Kim,.Y.C. 2000. Adipocytes differentiation and gene expression. Journal of Nutrition 130:3122s-3126s.
Official Methods of Analysis. 1994. 15th Ed. AOAC, Arlington, VA, sec, 993.
Ono, H. 2001. Methods for producing fermented food from soymilk refuse. United States Patent, US 6254901 B1, Juyl. 3.
O’Toole, D.K. 1999 Characteristics and use of okara, the soybean residue from soy milk production. Journal of Agricultural and Food Chemistry 47:363-371.
Park, V.V., Koo, M.S., Kasymova, T.D. and Kwon, D.Y. 2005. Isolation and identification of peptides from soy 11S-globulin with hypocholesterolemic activity. Chemistry of Natural Compounds 41: 710-714.
Park, Y., Storksin, J.M., Liu, W., Albright, K.J., Cook, M.E. and Pariza, M.W. 2004. Structure-activity relationship of conjugated linoleic acid and its cognates in inhibiting heparin releasable lipoprotein lipase and glycerol release from fully differentiated 3T3-L1 adipocytes. Journal of Nutrition Biochemical and Molecular Medicine 15 (9): 561-568.
Panasiuk, R., Amarowicz, R., Kostyra, H. and Sijtama, L. 1998. Determination of α-amino acid nitrogen in pea protein hydrolysates: a comparison of three analytical methods. Food Chemistry 62: 363-367.
Paulaskis, J.D. and Sul, H.S. 1989. Hormonal regulation of mouse fatty acid synthase gene transcription in liver. Journal of Biology and Cell Development 264 (1): 574-577.
Pellegrini, R.R., Proteggente, A., Pannata, A., Yang, M. and Rice-Evans, C. 1999. Antioxidant activity applying an improvement ABTS‧＋ radical cation decolorization assay. Method Enzymol 299:589
Penta-Ramos, E.A.and XiongP.l. 2002. Antioxidant activity of soy protein hydrolysates in a liposomal system. Journal of Food Science 67 (8): 2952-2956.
Pihlanto-Leppala, A. 2001. Bioactive peptiaes derived from bovine whey protein: opoid and ACE-inhibitory peptides. Trend in Food Science and Technology 11: 347-356.
Prestamo G., Ruperez, P., Espinosa-Martos, I., Villanueva, M. J. and Lasuncion, M. A. 2007. The effect of okara on rat growth, fecal fermentation and serum lipid. Europe FoodResearch and Technology 225:925-928.
Prosky, L., Asp, N.G., Furda, I. Schweitzer, T.F. and Harland, B.F. 1985. Determination of total dietary fiber in foods and food products: Collaborative study. Journal of the Association of Official Analytical Chemist 68: 677-679.
Prosky L.,Asp, N.G., Schweitzer, T.F. Davies, J.W. and Furda, I. 1992. Determination of insoluble dietary fiber and soluble dietary fiber in food and food products: Collaborative study. Journal of the Association of Official Analytical Chemist 75: 360-367.
Puechkamut, Y. and Panyathitipong, W. 2012. Cheracteristics of protein from fresh and dried residues of soy milk production. Kasetsart Journal Natural Science 46: 804-811.
Purcell, A.W., Aguilaz, M. I. and Hearn, M. T. M. 1995. Conformational effects in reversed-phase high performance liquid chromatography of polypeptides resolution of insulin variants. Journal of Chromatography 717: 61-70.
Redondo-Cuenca, A. J, Villanueva-Sua’rez, M. and Mateos-Aparicio, I. 2008. Soybean seeds and its by-product okara as sources of dietary fiber. Measurement by AOAC and Englyst methods. Food Chemistry 108: 1099-1105.
Reid, J., Novak, D.J. and Lewandosid, D.J. 2006. Grain Product with increased soluble fiber contend and associate methods US patent Apptication No. 20060275536.
Rho, S.J., Lee, J.S., Chung, Y.I., Kim, Y.W. and Lee, H.G. 2009. Purification and indentify of and ACE inhibitory Reptide from fermented cation soybean extract. Process Biochemistry 44: 490-493.
Riad, M., Mogos, M., Thangathurai, D. and Lumb, P. D. 2002. Steroids. Current Opinion in Critical Review 8: 281-284.
Rossetto, B.J. 1987. Side effect of Captopril and Enalapeil. West Journal Medicine 146 (1): 102-103.
Saito, K., Jin, D.H., Ogawa, T., Muramoto, K. Hatakeyama, E., Yasuhara, T. and Nokihara, K. 2003. Antioxidative properties of tripeptide libraries prepared by the combinatorial chemistry. Journal of Agricultural and Food Chemistry 51 (12): 3668-3674
Shah, B.C. and Hayashi, K. 2001. Debitterihg of protein hydrolyzates Biotechnology Advances 19:355-370.
Shallo H.E., Rao, A., Ericson, A.P. and Thomas, R.L. 2001. Preparation of soy protein concentrate by ultrafiltration. Journal of Food Science 66 (2): 242-46.
Sheih, I.C., Wang, H.C., Chang, C.L., Lai, Y.C., Liang, C.W., Chiang,W.D.and Chu, Y.H. 2004. Screening of high isoflavone aglycones producing organism and serum lipid lowering effect of ethanol-extracted fermented soybean hypocotyls. Taiwanese Journal Agricultural Chemistry and Food Science 42 (1):69-74.
Shepherd, P.R., Gnudi, L., Tozzo, E.Y., Leach, F. and Kahn, B.B. 1993. Adipose cell hyperplasia and enhanced glucose disposal in transgenic mice over expressing GLUT4 selectively in adipose tissue. Journal Biology and Cell Development 286:243-246.
Shi, H.S., Hudson, L.G. and Liu, K.J. 2004. Oxidative stress and apoptosis in metal ion-induced carcinogenesis. Free radical Biology and Medicine 37 (5): 582-593.
Shin, Z.I., Park, S.A., Ching, D.K., Ahn, C.W., Nam, H.S., Kim, K.S. and Lee, H.J. 2001. His-His-Leu, and angiotensin-I converting enzyme inhibitory peptide derived from Korean soybean paste, exert antihypertensive activity in vivo. Journal Agricultural and Food Chemistry 49 (6): 3004-3009.
Siemensma, A. D., Weijer, W. J. and Bak, H.J. 1993. The important of peptide lengths in hyposllenic infant formula. Trends in Food Science and Technology 4:16-21.
Singhanin, R. R., Sukumaran, R. K. and Randey, A. 2007. Improved cellulase production by Trichoderma reesei RUT C30 under SSF though process optimization. Applied Biochemical and Molecular Medicine 142 (1): 60-70.
Soomro, A.A. Pevrajani, B.R., Ghori, P.A. Lohana, H. and Qureshi, G.A. 2008. Role of branched chain amino acid in the management of hepatic encephalopathy.World Journal of Medical Science 3 (2): 60-64.
Su, G., Ren, J., Tang, B., Cui, C. and Zhao, M. 2001. Comparison of hydrolysis characteristics on defatted peanut meal proteins between a protease extract from Aspergillus oryzae and commercial protease. Food Chemistry 126: 1306-1311.
Suruga, K., Akiyamy, Y., Kadokura, K., Sekino, Y., Kawagoe, M., Komatsu, Y., and Sugiyamy, T. 2007. Synergistic effect on reactive oxygen scavenging activity of fermented okara and banana by XYZ system. Food Science and Technology Research 13 (2): 139-144.
Takenaka, A. Annaka, H. Kimura, Y. Aoki, H. and Igarashi, K. 2003. Reduction of paraquat induced oxidative stress in rats by dietary soy peptide. Bioscience, Biochemical and Biotechnology 67 (2): 278-283.
Takenaka, Y., Utsumi, S. and Yoshikawa, M. 2000. Introduction of enterostatin (VPDPR) and a related sequence into soybean proglycinin A1aB1b subunit by site-directed mutagenesis. Bioscience, Biochemical and Biotechnology 64: 2731-2733.
Tsou, M.J., Kao, F.J., Tseng, C.k. and Chiang, W.D. 2010. Enhancing the anti-adipogenic activity of soy protein by limitedhydrolysis with Flavourzyme and ultrafiltration. Food Chemistry 122:243-248.
Tsou, M.J., Kao, F.J., Lu, H.C., Kao, H.C. and Chiang, W.D. 2013. Purification and identification of lipolysis-stimulating peptide derived from enzymatic hydrolysis of soy protein. Food Chemistry 138 (2-3): 1454-1461.
Tubaro, F, Ghiselli, A., Maiorino, M. and Ursine, F. 1998. Analysis of plasma antioxidant capacity hy competition kinetics. Free Radical, Biology and Medicine 24 (7-8): 1228-1234.
Tucker G.A. and Woods L.F.J. 1995. Enzymes in Food processing, pp.12-17. Blackie Academic and Professional, and imprint of Chapman and Hall, Wester Cleddens Road, Bishobriggs, Glasgow G642NZ.
Turhan, S., Temiz, H and Sagir, I. 2009. Characteristics of beef patties using okara powder. Journal of Muscle Foods 20 (1): 89-100.
Vaithanomsat, P. and Punyasawon C. 2008. Process optimization for the production of Philosamia ricini (eri silk) papae hydrolysate. Kasetsart Journal National Science 42: 341-352.
Van der riet, W. B., Cilliers, J. J. and Datel, J. M. 1989. Food chemistryical investigation of tofu and its byproduct okara. Food Chemistry 34: 193-202.
Villanueva, M.J., Yokoyama, W.H., Hong, Y.J., Barttley, G.E., and Ruperez, P. 2011. Effect of high-fat diets supplemented with okara soybean by-product on lipid profiles of plasma, liver and feaces in Syrian hamsters. Food Chemistry 124 (1): 72-79.
Waliszewski, K.N., Pardio, V. and Carreon, E. 2002. Physicochemical and sensory properties of corn tortillas made from Nixtamalited corn flour fortified with spent soymilk residue (Okara). Journal of Food Science. 67 (8): 3194-3197.
Wang, A. and De Mejia 2005. A new frontier in soy bioactive peptides may prevent age-related chronic diseases. Comprehensive Reviews in Food Science and Food Safety 4:63-78.
WHO/FAO/UNU 2007. Protein and amino acid reguirements in human nutrition report of a joint WHO/FAO/UNU expert consulation Geneva, 2002. Technical Reports Series 935, WHO, Geneva, Switzerland.
World Health Organization 2003. Diet, nutrition and thr prevention of chronic disease, In Report of a Joint WHO Expert Consultation WHO Technical Report Series Vol 916.
Wu, J. and Ding, X. 2001. Hypotensive and physiological effect of angiotensin converting enzyme inhibitory peptides derived from soy protein on spontaneously hypertensive rats. Journal of Agricultural and Food Chemistry 49 (1): 501-506.
Wu, J.P. and Ding, X.T. 2002. Characterization of inhibition and stability of soy protein derived angiotensin I converting enzyme inhibitory peptide. Food Research International 35: 367-375.
Wu, J., Aeluko, R.E. and Nakai, S. 2006. Structural reguirements of angiotensin I-converting enzyme inhibitory peptide:quantitative structure-activity relationship study of di and tripeptide. Journal of Agricultural and Food Chemistry 54: 732-738.
Yamamoto, N., Ejiri, M. and Mizuno, S. 2003. Biogenic peptides and their potential use. Current Pharmaceutical Design 9 (16):1345-1355.
Yan, H., Kermouni, A., Abdel-Harfez, M.and Lau, D.C. 2003.Role of cyclooxygenases COX-1and COX-2 in modulating adipogenesis in 3T3-L1 cell. Journal Lipid Research 44: 424-429.
Yang, Y., Marczak, E.D., Usui, H., Kawamura, Y. and Yoshikawa, M. 2004. Properties of spinach leaf protein digest hypertensive. Journal of Agricultural and Food Chemistry 52 (8): 223-225.
Yang, S., Yunden, J. Sonoda, S., Doyama, N., Lipkowski, A.W., Kawamura, Y. and Yoshikawa, M. 2001. Rubiscolin, a selective opioid peptide derived from plant Rubisco. Federation of European Biochemical Societies509 (2): 213-217.
Yangilar, F. 2013. The application of dietary fibre in food industry: structural textures, effects on health and definition, obtaining and analysis of dietary fibre: A review. Journal of Food Nutrition Research 1 (3):13-23.
Yokomizo, A. Takenaka, Y. and Takenaka, T. 2002. Antioxidative activity of peptide prepared from okara protein. Food Technology 8 (4):357-359.
Yoshikawa, M. Takahashi, M. and Yang, S. 2003. Delta opioid peptides derived from plant proteins. Current Pharmaceutical Design 9 (16):1325-1330.
Yu, L., Perret, J. Parker, T. and Allen, K.G.D. 2003. Enzymatic modification to improve the water-absorbing and gelling properties of psyllium. Food Chemistry 82:243-248.
Yu, Z.R. Hung, C.C. Weng, Y.M. S, C.L. and Wang, B.J. 2007. Physiochemical, antioxidant and whitening properties of extract from root cories of mulberry as affected by membrane process. Food Science and Technology 10: 900-907.
Zhu, Y.P., Fan, J.F., Cheng, Y.Q. and Li, L.T. 2008. Improvement of the antioxidant activity of Chinese traditional fermented okara (Meitauza) using Bacillus subtillis B2. Food Control 19: 654-661.
Zhu, K.X., Zhou, H.M. and Qian, H.F. 2006. Antioxidan and free radical scavenging activities of wheat protein hydrolysates (WGPH) prepared with alcalase. Process Biochemical and Molecular Medicine 41: 1296-1302.
Zhao, X.H., Wang, J.K. and Li, T.J. 2011. In vitro ACE-inhibitory and antioxidant activies of the casein hydrolysates subjected to peastein ceaction with addition of three extrinsic. Biotechnology 10 (5): 408-411.
第二章、參考文獻

Adler-Nissen, J. 1986. Methods in food protein hydrolysates. In enzymatic hydrolysis of food protein. (pp. 110–131), New York: Elsevier.
Alzadeh-Pasdar, N. and Li-Chen, E.C.Y. 2000. Comparison of protein surface hydrOPIHobicity measure at various pH values using three different fluorent probes. Journal of Agricultural and Food Chemistry 48 (2) : 328-334.
Anon, C.M. and Ortiz, S.M. 2000. Analysis of products, mechanisms of reaction, and some functional properties of soy protein hydrolysates. Journal of the American Oil Chemists' Society77:1293-1301.
AOCS 1989. Official methods and recommended practices of the American Oil Chemists' Society (4th Ed.). Champaign, IL: AOCS.
Barać, M.B., Stanojević, S.P., Jovanović, S.T. and Pešić M.B. 2004. Soy protein modification-a review.APTEFF, 35, 1-280
Barać, M. Cabrilo, S. Pesić, M. and Janković. M. 2012. Functional properties of protein hydrolysates from ped seed (Pisum Safivum, L). Food Science and Technology Techinol 47:1457-1467.
Bernardi, L.S., Pilosof, A.M.R. and Bartholomai, G.B. 1991. Enzymatic modification of soy protein concentrates by fungal and bacterial proteases. Journal of the American Oil Chemists’ Society 68:102–105.
Carp, D.J., Bartholomat, G.B. and Pilosof, A.M.R. 2001. Effect of denaturation on soy protein-xanthan interaction: comparison of a chipping-rheological and a bubbling method Colloids and Surfaces B: Biointerfaces 21 (1-3) : 163-171.
Chabanon, G., Chevalot, I. Framboisier, X. and Mar, I. 2007. Hydrolysis of rapeseed protein isolates: Kinetics, characterization and functional properties of hydrolysates. Process Biochemical and Molecular Medicine. 42 (10) :1419-1428.
Chiang, W.P., Chin, C.J. and Chu, Y.W. 1999. Functional properties of soy protein hydrolysates produced from a continuous membrane reactor system. Food Chemistry 65: 189-194.
Cho, M.J., Unblesbay, N., Hsie, F.H and Clark, A.D. 2004. HydrOPIHobicity of bitter peptides foom soy protein hydrolysates. Journal of Agricultural and Food Chemistry 52:5895-5901.
Chobert, J, Briand,M.L., Gueguen,J., Opineau,P., Larre,J., C. and Haertle, T. 1996. Recent advances in enzymatic modifications of food proteins for improving their functional properties. Nahrung 40:177-182
Chobert, J.M., Bertrand-Harb, C. and Nicolas, M.G. 1998. Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin. Journal of Agricultural and Food Chemistry 36 (5): 883-892.
Clemente, A., Viogue, J., Sanchez-Viogue, R. and Millam, F. 1999. Protein guality of chickpea protein hydrolysates. Food Chemistry 67 (3) : 209-274.
Darwicz, M., Dziuba, J. and Caessens, P.W.J.R. 2000. Effect of enzymatic hydrolysis on emulsifying and foaming properties of milk proteins-a review. Polish Journal of Food and Nutrition Sciences 9 (1): 3-8.
De La Barca, A.M.C., Ruiz-Salazar, R.A. and Jara-Marini, M.E. 2000 Enzymatic hydrolysis and synthesis of soy protein to improve its amino acid composition and functional properties. Food Chemistry and Toxicology 65:246-253.
Dickinson, E. 2003. Interfacial, emulsifying and foaming properties of milk proteins. In: Advanced Dairy Chemistry; Fox, P.F., and McSweeney, P., Eds; Kluwer Academic/Plenum Publishers: Dordrecht, The Netherlands, Vol. l, Proteins, Parts A and B: 1229-1260.
Dickinson, E. and Mcclements, D.J. 1996. Molecular basis of protein functionality. In: Aduance in Food Colloids p 27-80 Blackie Academic and Professional, UK.
Fischer, M., Gruppen, H., Piersma, S.E., Kofod, L.V. Schols, H.A. and Voragen, A.G.J. 2002. Aggregation of peptides during hydrolysis as a cause of reduced enzymatic extractability of soybean meal proteins. Food Chemistry 20 (3) :1164-1172.
Govindaraju, K., and Srinivas, H. 2006. Studies on the effects of enzymatic hydrolysis on functional and physico-chemical properties of arachin.Food Science and Techonlogy. 39 (1): 54-62.
Guan, X,m Yao, H., Chem, Z. X., and Zhamg, M.D. 2007. Some functional properties of oatbran protein concentrate modied by trypsin. Food Chemistry 101 (1) : 163-170.
Haskard, C.A. and Li-Chan, E.C.Y. 1998. HydrOPIHobicity of bovine serum albumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANS-) fluorescent probes. Journal of Agricultural and Food Chemistry 46 (7) : 2671-2677.
HettiarachchyE, N.S. and Kalapathy, U. 1998. Functional properties of proteins. In: Whitaker, J.P (Ed.): Functional properties of proteins and lipids. ACS Symp. Ser. No. 708. American Chemistry Society, Washington, D.C. p.p. 80-87.
Hrckova, M., Rusnakova, M. and Zemanovic, J. 2002. Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulties of resulting protein hydrolysates. Czech Journal of Food Science 20 (1): 7-14.
Jideani, L.A. 2001 Functional properties of soybean food ingredient in food system Food Chemistry 31: 345-366.
Jimenez-Escrig, A., Alaiz, M., Viogul, J. and Ruperez, P. 2010. Health-promoting activities of ultrafiltered okara protein hydrolysates released by in of active peptide from soybean expoxygenase. Europe Food Research and Technology 230: 655-663.
Jung, S., Murphy, P.A. and Johnson, L.A. 2005. physicochemical and functional properties of soy protein substrates modified by low levels of protease hydrolysis. Journal of Food Science 70 (2) : C180-C187.
Karayannidou, A., Makvi. E., Laptevo, N, and Articov, G. 2007. Limited proteolysis as door for the improvent of the functionality of sunflower protein isolates by seed or by-product solvent cake. Food Chemistry 104 (4) : 1728-1733.
Kato, A. and Nakai. S. 1980. HydrOPIHobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochemical and Molecular Medicine 624:13-20.
Kim, S.Y., Park, P.S.W. and Rhee, K.C. 1990. Functional properties of proteolytic enzyme modified soy protein. Journal of Agricultural and Food Chemistry 38 (3) : 651-656.
Kinsella, J.E. 1979. Functional properties of soy proteins Journal of the American Oil Chemists’ Society 56 (3): 242-258.
Klompong, V., Benjakul, S., Kantachote, D., and Shahidi, F. 2007. Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by degree of hydrolysis and enzyme type. Food Chemstry 102: 1317-1327.
Korhonen, H. and Pihlanto, A. 2003. Food derived bioactive peptides: Opportunities for designing future foods. Current Pharmaceutical Design 9 (16) :1297-1308.
Lamsal, B.P., Reitmeier, C., Murphy, P.A. and Johnson, L.A. 2006. Enzymatic hydrolysis of extruded-expelled soy flour and resulting functional properties. Journal of the American Oil Chemists' Society 83 (8) : 731-737.
Liu, J., Jiang, L.-Z., Zhang, J.-L and Li, Y. 2009. Optimization of Protamex catalyzed hydrolysis of alcohol-leached soy protein concentrates using response surface methodology (In Chinese). Journal of Food Science 30: 13 163-169
Ma, C.-Y., Lui, W.-S., Kwok, K.C. and Kwok, F. 1997. Isolate and characterization of protein from soy milk residue (Okara). Food Research International 29 (8): 799-805.
Mahmoud, M. I. 1994. Physicochemical and functional properties of hydrolysates in nutritional products. Food Technology 48: 89-95.
Molina, D.E. and Wanger, J.R. 2002. Hydrolysates of native and modified soy protein isolates: Structures characteristics, solubility and foaming properties Food Research International 35 (6) : 511-518.
Molina, S., Carrera, C., Rodriguez Nino, M.R., C. and Rodriguez Patino, J.M. 2003. Structural characterization and surface activity of spread adsorbed soy globulin films at equilibrium. Colloids and Surfaces B: Biointerfaces 32 (1): 57-67.
Nakai, S. and Li-Chan, E.C.Y. 1989. Effects of heating on protein functionality. In: Philips RD, and Finley JW, editors. Protein quality and the effects of processing. New York: Mercel Dekker. pp. 125-144.
Nielsen, P.M. 1994. Enzyme technology for production of protein based flavours. Food Ingredients Europe Conference.
Ogunwolu, S.O., Henshawb, F.O., Mock, H., Santros, A., and Awonorin, S.O. 2009. Functional properties of protein concentrates and isolates produced from cashew (Anacardiu moccidentale L.) nut. Food Chemistry 115: 852–858.
Panyam, D. and Kilara, A. 1996. Enhancing the functionality of food proteins by enzymatic modification. Trend Food Science and Technology 7 (4): 120-125
Peak N.A. and Johnson, L.A. 2007. Effect of extradion temperature and preservation method on functionality of soy protein Journal of the American Oil Chemists’ Society 84: 259-268.
Pearce, K.N. and Kinsella, J.C. 1978. Emulsifying properties of protein Evaluation of a turbidimetric technigue. Journal of Agircultural and Food Chemistry 26:716-723.
Peng, I.C., Quass, D.W., Daytin, W.R. and Allen, C.E. 1984. The physicochemical and functional properties of soybean 11S Globulin: A Review. Cereal Chemistry 61 (6) : 480-490.
Petruccelli, S.and Anon, M.C. 1994. Relationship between the method of abstention and structural and functional properties of soy protein isolates. 2. Surface properties. Journal of Agricultural and Food Chemistry 42:2170-2176.
Petruccelli, S., and Anon, M.C. 1995. Soy protein isolate components and their interactions. Journal of Agricultural and Food Chemistry 43:1762-1767
Pizones, V., Carrera, C. and Rodriguez J.M. 2007. Formulation engineering can improve the interfacial and foaming properties of soy globulins.Journal of Agricultural and Food Chemistry 55 (15) : 6339-6348.
Puppo, M.C. Speroni, F., Chapleau, N., De Lamballerie, M., Anon, M.C. and Anton, M. 2005. Effect of high-pressure treatment on emulsifying properties of soybean proteins. Food Hydrocolloids 19 (2) : 289-296.
Qi, M., Hettiarachchy, N.S. and Kalapathy, U. 1997. Solubility and emulsifying Properties of soy protein isolates modified by pancreatin. Journal of Food Science 62 (6) : 1110-1115.
Radha,C., Parigi, R.K. and Vishweshwaraiah, P. 2008. Enzymatic modification as a tool to improve the functional properties of heat-processed soy flour. Journal of the Science of Food and Agriculture88:336–343
Rodelguez, J.M., Rodrlguez , M.R. and Carrera, C. 2008. Implications of interfacial characteristics of food emulsifiers in foam formulations. Advance Colloid and Interface Science 140 (2): 95-113.
Rodriguez P.J.M., Rodriguez N.M.R. and Carrera, C. 2007. Physicochemical properties of surfactant and protein films. Current Opinion Colloid and Interface Science 12:187-195.
Shimizu, M., Saito, M. and Yamauchi, K. 1986 HydrOPIHobicity and emulsifying activity of milk proteins.Agricultural Biology Chemistry 50:791–792.
Simpson, R.J., Neuberger, M.R. and Liu, T.Y. 1976. Complete amino acid analysis of proteins from a single hydrolysate. Journal Biology Cell Development 251:1936-1940.
Tang C.-He., and Ma C.-Y. 2009. Heat-induced modifications in the functional and structural properties. Food Chemistry 115: 859–866
Tsumura, K., Kugimiya, W. and Inouye, K. 2005. Emulsifying properties of a peptide from peptic hydrolysates of soy glycinin. Food Science and Technology Research11: 46-51.
Turner, J.R. 1969. Midified soy protein and preparation thereof. US Patent 2,489,208.
Utsumi, S., Matsumura, Y. and Mori, T. 1997. Structure-function relationships of soy proteins. In: Food Proteins and their Applications; Damodaran, S., Paraf, A., Eds.; Dekker; New York, pp. 257-291.
Vioque, J., Sanchez-Vioque, R., Clemente, A., Pedroche, J. and Millan, F. 2000. Partially hydrolyzed rapeseed protein isolates with improved functional properties. Journal of the American Oil Chemists’ Society 77 (4) : 1-4.
Voutsinas, L.P., Nakai,S. and Harwalkar,V.R. 1983. Relationship between protein hydrophobicity and thermal functional properties of food proteins Canadian Institute of Food Science and Technology Journal16:185–190.
Wang, H. L. and Cavin, J.F. 1989. Yield and amino acid composition of fraction obtained during tofu production. Cereal Chemistry 60; 359-361.
Wagner, J.R., Sorgentini, D.A. and Anon, M.C. 2000. Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory-prepared soy protein isolates. Journal of Agricultural and Food Chemistry 48 (8) : 3159-3165.
Were, L., Hettiarachchy, N.S. and Kalapathy, U. 1997. Modified soy proteins with improved foaming and water hydration properties. Journal of Food Science 62 (4) : 821-824.
Wu, W., Hettiarachchy N.S., and Qi, M. 1998. Hydrophobicity, solubility and emulsifying properties of soy protein peptides prepared by papain and ultrafiltration. Journal of the American Oil Chemists’ Society 75:845–50.
Zhang, Y., Zhao, W., Hua Zhang W., Zhang W. and Zhang, Y. 2013. Preparation and functional properties of proteinfrom heat-denatu soybean meal assisted bys team flash-explosion with dilutred acid Journal of Engineering 19: 56-64.
第三章、參考文獻

李風。2007。酶解提取大豆膳食纖維的研究。四川食品與發酵，437-439。
姜竹茂、陳新美、繆靜。2001。微豆渣中制取可溶性膳食纖維的研究。中國食品學報，16 (3) : 52-55。
Anderson, E.T., and Berry, B.W. 2000. Sensory, shear, and properties of lower-fat beef patties made with inner pea fiber. Journal of Food Science 65 (5) : 805-810.
AOAC 1990.Official methods of analysis (15th ed). Arlington, VA: Assoction of official Analyical Chemists.
Bilek, A.E. and Turhan, S. 2009. Enhancement of the nutritional status of beef patties by adding flaxseed flour. Meat Science 82: 472-477.
Brewer, M.S. 2012. Reducing the fat content in ground beed without sacrificing guality: A review. Meat Science 91:385-395.
EI-Shemy2011. Soybean and health. Rijeka:In Tezh, p.p. 422-436.
Food and Nutrition Board, Institute of Medicine of the National.2001. Dietary reference intakes for energy, carbohydrate, fiber,fat fatty acids, cholesterol, protein and amino acids. Washingtion. D.C., National Academies Press. pp. 265-334.
Genta, H.D.,Genta,M.L.,Alvarez, N.V. and Santana,M.S. 2002. Production and acceptance of a soy candy. Journal of Food Engineering 53:199-202.
Grizotto, R.K. and De Aguirre, J.M. 2011 Study of the flash drying of the residue from soymilk processing-okara. Food Science and Technology 31: 645-653.
Gujral, H.S., Kaur, A.N., Singh, N. and Sodhi,N.S. 2002. Effect of liquid whole egg, fat and textured soy protein on the textural and cooking properties of raw and baked patties from goat meat. Journal of Food Engineering 53:377-385.
Jimenez-colmenero, F., Carballo, J. and Cofrades, S. 2001. Healthier meat and meat products: Their role as functional foods. Meat Science 59: 5-13.
Kasai, N. Murata, A.,Inui, H.,Sakamoto,T. and Kahn,R.I. 2004. Enzymatic high digestion of soybean milk residue (Okara). Journal of Agricultural and Food Chemistry 52: 5709-5716
Kassem, M.A.G.and Emara, M.M.T. 2010. Quality and acceptability of value-added beef burger. World Journal of Dairy Food Science 5 (1) : 14-20.
King,J.W.,Johnson, J.H.,Orton, W.L.,Mackeith, F.K.,O'conner, P.L. J.N. and Carr, T.R. 2009. Fat and cholesterol content of beef patties as affected by supercritical CO2 extraction. Journal of Food Science58:950-958
Mansour, E.H. and Khalil, A.H. 1997. Characteristics of low-fat beef burger as influenced by various types of wheat fibers. Food Research International30: 199-205.
Matsuo, M. 1989. Morphological and physicochemical properties and composition of “okara” ermented with Rhizopus oligosporus. Journal of the Japanese Society of Nutrition and Food Science 42:173-178 (In Japanese).
McMindes, M.K. 1991. Applications of isolated soy protein in low-fat meat products. Food Technology 45: 61-64.
Mottram, D.S. 1998. The chemistry of meat flavor In:Shahidi,F. (Ed.), Flavour of meat, meat products, and seafoods (pp. 5-26). London: Blackie Academic and Professional.
Naveena, B.M., Muthukumar, M., Babji, A.R.S.Y., and Murthy, T.R.K. 2006. Quality characteristics and storage stability of chicken patties formulated with finger millet flour (Eleusine coracana). Journal of Muscle Foods 17: 92-104.
O’Toole, D.K., 1999. Characteristics and use of okara. the soybean residue from soy milk production –A review. Journal of Agricultural and Food Chemistry 47: 363–371.
Pinero, M.P., Parra, K., Hueta-Leidenz, N., De Moreno, L.A., Ferrer, M. and Araujo, S., 2008. Effect of oat’s soluble fibre (Beta-glucan) as fat replacer on physical, chemical, microbiological and sensory properties of low-fat beef patties. Meat Science 80 (3) : 675-680.
Prosky, L. N.-G., Asp, T.F., Schweizer, J.W., De Vries, J.V., and Furda, I. 1988. Determination of insoluble, soluble and total dietary fiber in foods and food products: Interlaboratory study. Journal of the American OilChemists’ Society 71: 1017-1023.
Rinaldi, V.E.A., Ng, P.K.V. and Bennink M.R. 2000. Effects of extrusion on dietary fiber and isoflavone contents of wheat extrudates enriched with wet okara. Cereal Chemistry 77: 237-240
Saricaoglu, F.T. and Turham, S. 2013 Chemical Composition, colour and textural properties of akcaabat meatball, A traditional twrkish meat product. GIDA, 38:1-10.
Serdaroglu, M. 2006. Improving low fat meatball characteristics by adding whey powder. Meat Science72: 155-163.
Tabarestani, H.S. and Tehani, M.M. 2012. Optimization of low fat hamburger formulation using of soy flour,split pea flour starch as parts of fat replacer system. Journal Food Processing and Preservation (5) 1-7.
Turhan, S. H.,Temiz, and Sagir I. 2007. Utilization of wet okara in low-fat beef patties. Journal Muscle Foods 18: 226-235.
Turhan, S., Temiz, H. and Sagir, I. 2009. Characteristic of beef patties using okara powder. Jounral Muscle Foods 20: 89-100.
Troutt, E.S.,Hunt, M.C.,Johnson,D.E. Claus,J.R. Kastner, C.L. and Kropf, D.H. 1992. Characteristics of low-fat ground beef containing texture modifying ingredients. Journal of Food Science 57: 19-24.
Van der riet, Cilliers, J.J.L., Wing, J. J. and Datel, J. M. 1989. Food Chemistryical investigation of tofu and its byproduct okara. Food Chemistry 34 (3) : 193-202.
Waliszewski, K.N., Pardio, V. and Carreon, E. 2002. physicochemical and sensory properties of corn tortillas made from nixtamalized corn flour fortified with spent soymilk residue (Okara). Journal of Food Science 67: 3194-3197.
Youssef, M.K.and Barbut, S. 2011. Fat reduction in comminuted meat products-effects of beef fat, regular and pre-emulsified canola oil. Meat Science 87 (4) : 356-360.
Zhu, L., Robbins, K.L., Cadwallaer, K.R. and Brewer, M.S. 2001. Effects of soy protein isolate on headspace aroma componenrs of cooked ground beef, IFT Annual Meeting. New Orleans, L.A. Abstract. 88A-18.