探討不同蛋白酶對米蛋白水解物抗氧化及抗高血壓活性的影響

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陳琳(Lin Chen) 查詢紙本館藏

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化學工程與材料工程學系

論文名稱

探討不同蛋白酶對米蛋白水解物抗氧化及抗高血壓活性的影響
(Effects of different proteases on antioxidant and antihypertensive activities of rice protein hydrolysate)

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摘要(中)

米為台灣人最大宗的主食之一，在稻米的加工製造過程中會把稻米中的澱粉提取出來用於後續的釀酒或發酵作業上，而去除澱粉的米渣就成了其加工產業中最主要的農業廢棄物。米渣通常會乾燥後當作動物飼料來處理，米渣中含有豐富的營養物質，但其工業附加價值低。因此本研究利用米渣中含有豐富蛋白質的特性，利用不同的酵素在最適反應環境下水解米蛋白，並尋找米蛋白水解液對抗氧化及抗高血壓能力的最適化水解條件。
本實驗利用米蛋白酶會溶於鹼性液體的特性將米蛋白從米渣中初步純化，並探討不同pH沈澱物對米蛋白水解物的影響，發現pH=5時析出的蛋白質，經過Alcalase水解後有最大的蛋白質利用率及胜肽濃度。接著利用三種酵素(Alcalase、Flavourzyme、Trypsin)以單一酵素和兩階段酵素進行水解並探討其DPPH自由基清除率和鐵離子螯合率等抗氧化活性。實驗發現Alcalase水解產物有較大的抗氧化活性，且在水解2小時後達到最大值，而Flavourzyme水解產物之抗氧化活性僅次於Alcalase水解產物，故第二階段利用Alcalase和Flavourzyme混合水解的方式探討是否能提升抗氧化活性。實驗結果發現在Alcalase水解2小時後再加入Flavourzyme水解6小時有最大的自由基移除率及鐵離子螯合率，分別為68.9 %及68.9 %。接著將水解液分成> 10 kDa、10-3 kDa及< 3 kDa三種不同的分子量區間進行抗氧化實驗，發現10-3 kDa的分子量區間有最好的抗氧化效果。利用上述水解條件得到的米蛋白水解液進行抗高血壓的測定，可以發現單一酵素水解中，Alcalase水解產物比Flavourzyme水解產物有較好的ACE抑制活性，且兩階段酵素水解並不能得到較好的結果，推測是加入第二種酵素後會使胜肽的結構產生改變，導致ACE抑制活性下降。但若將水解液分成不同大小的分子量區間進行測試，可以發先小分子量有較好的ACE抑制效果。

摘要(英)

Rice is a principal food source for Taiwanese. In the processing and manufacturing process of rice, the starch in rice is extracted for subsequent brewing or fermentation, and the starch removed residue is the most in the processing industry which is the main agricultural waste. Rice dreg is usually dried and treated as animal feed. The rice dreg is rich in nutrients, but its industrial added value is low. Therefore, this study utilizes the characteristics of protein rich in rice dreg, uses different enzymes to hydrolyze rice protein in the optimum reaction environment, and searches for optimal hydrolysis conditions for rice protein hydrolysate against oxidation and antihypertensive ability.
In this experiment, rice protein was initially purified from rice dreg by using the characteristics of rice protease dissolved in alkaline liquid, and the effects of different pH precipitates on rice protein hydrolysate were investigated. It was found that the protein precipitated at pH=5 had the maximum protein utilization and peptide concentration after Alcalase hydrolysis. Then, three enzymes (Alcalase, Flavourzyme, Trypsin) were used to hydrolyze with a single enzyme and two-stage enzymes to investigate the antioxidant activities such as DPPH free radical scavenging rate and iron ion chelation rate. It was found that Alcalase hydrolysate has a large antioxidant activity and reaches a maximum after 2 hours of hydrolysis. The antioxidant activity of Flavourzyme hydrolysate is second only to Alcalase hydrolysate. Therefore, the second stage uses Alcalase and Flavourzyme to study whether it can enhance antioxidant activity.
The experimental results showed that the maximum of free radical removal rate and iron ion chelation rate were obtained after the hydrolysis of Alcalase for 2 hours and the addition of Flavourzyme for 6 hours. The free radical removal rate and the iron ion chelation rate were 68.9 % and 68.9 %, respectively. The hydrolysis solution was then divided into three different molecular weight ranges of > 10 kDa、10-3 kDa and < 3 kDa for antioxidant experiments. It was found that the molecular weight range of 10-3 kDa had the best antioxidant effect.
The determination of antihypertensive using the rice protein hydrolyzate obtained by the above hydrolysis conditions can found that Alcalase has good ACE inhibitory activity than Flavourzyme, and the mixing of the two enzymes does not give the good results. It is speculated that the addition of the second enzyme will result in a change in the structure of the peptide, resulting in a decrease in ACE inhibitory activity. However, if the hydrolysate is divided into molecular weight ranges of different sizes for testing, a small molecular weight can be obtained with a good ACE inhibition effect.

關鍵字(中)

★ 米渣蛋白
★ 生理活性胜肽
★ 抗氧化
★ 抗高血壓

關鍵字(英)

★ rice dreg protein
★ bioactive peptides
★ antioxidant
★ antihypertensive

論文目次

摘要 I
Abstract III
致謝 V
總目錄 VI
圖目錄 X
表目錄 XII
第一章緒論 1
1.1 研究動機 1
1.2 研究目的 2
第二章文獻回顧 4
2.1 稻米 4
2.1.1 稻米的基本介紹 4
2.1.2 稻米的營養成分 4
2.2 米蛋白之萃取 7
2.2.1 酵素法萃取 7
2.2.2 鹼性萃取法 7
2.3 蛋白質的水解方式 8
2.3.1化學水解 8
2.3.2酵素水解 8
2.4 影響蛋白質酵素水解之因素 9
2.4.1酵素的種類 9
2.4.2 酵素與受質比 11
2.4.3 pH值與溫度 11
2.5 蛋白質水解胜肽之應用 12
2.5.1蛋白質水解的目的及益處 12
2.5.2 胜肽應用 13
2.6 高血壓 18
2.6.1 高血壓的成因 18
2.6.2 高血壓及其併發症 20
2.6.3 高血壓的防治及治療 21
2.7 腎素-血管收縮素系統(renin-angiotension system, RAS) 23
2.7.1 腎素-血管收縮素系統與血壓調節 23
2.7.2 腎素-血管收縮素系統與高血壓 26
2.8 血管收縮素轉化酶(angiotensin I-converting enzyme, ACE) 26
2.9 血管收縮素轉化酶抑制劑(angiotensin I-converting enzyme inhibitor, ACEI) 28
第三章實驗規劃、材料與方法 31
3.1 實驗規劃 31
3.2 實驗材料 32
3.2.1 實驗用米蛋白 32
3.2.2 蛋白分解酵素 32
3.2.3 實驗藥品 33
3.2.4 實驗儀器與設備 35
3.2.5 數據使用代號定義 37
3.2.6 實驗裝置 37
3.3 實驗方法 39
3.3.1 製備米蛋白水解物 39
3.3.1.1 米蛋白前處理 39
3.3.1.2 米蛋白酵素水解 39
3.3.2 超膜過濾水解物(Ultrafiltration) 39
3.4 分析方法 40
3.4.1 蛋白質濃度測定(BCA) 40
3.4.2 胜肽含量之測定(OPA) 41
3.4.3 抗氧化活性測試 42
3.4.3.1 清除-diaphenyl--picrylhydrazyl (DPPH)自由基能力測定 42
3.4.3.2鐵離子螯合分析 43
3.4.4 血管收縮素轉化酵素抑制物(ACEI)之抑制活性測定 44
3.4.5 蛋白質純化 (FPLC) 46
第四章實驗結果與討論 49
4.1 利用不同pH值沉澱對米蛋白水解之影響 49
4.2 使用單一酵素對米蛋白進行水解之探討 51
4.2.1使用單一酵素水解對蛋白質濃度及胜肽濃度之影響 51
4.2.2 使用單一酵素水解對抗氧化活性之影響 54
4.2.2.1 單一酵素水解物之清除DPPH自由基能力 54
4.2.2.2 單一酵素水解物之鐵離子螯合率 55
4.3 使用兩種酵素對米蛋白進行水解之探討 56
4.3.1使用兩階段水解對蛋白質濃度及胜肽濃度之影響 57
4.3.2使用兩階段水解對抗氧化活性之影響 58
4.4 經膜過濾分離後之水解液對抗氧化活性之探討 60
4.5 米蛋白水解液對ACE抑制之探討 63
4.5.1 不同酵素隨時間水解米蛋白之ACE抑制之影響 63
4.5.2 不同分子量大小之水解液對ACE抑制之影響 65
4.6經FPLC純化後之米蛋白水解液對抗氧化及ACE抑制活性之影響 66
第五章結論 69
第六章參考文獻 71
附錄一、英文代號及其中文意義 84

參考文獻

[1] 行政院農委會農糧署. https://www.afa.gov.tw/cht/index.php?code=list&ids=299
[2] 黃怡仁, 宋鴻宜, "水稻機能性成分之研究成果," 農業生技產業季刊, no. 39, pp. 35-37, 2014.
[3] X. Li, H. Xiong, K. Yang, D. Peng, H. Peng, and Q. Zhao, "Optimization of the biological processing of rice dregs into nutritional peptides with the aid of trypsin," (in eng), J Food Sci Technol, vol. 49, no. 5, pp. 537-46, Oct 2012.
[4] B. O. Juliano, Rice in human nutrition (no. 26). Int. Rice Res. Inst., 1993.
[5] R. M. Helm and A. W. Burks, "Hypoallergenicity of rice protein," Cereal Foods World, vol. 41, no. 11, pp. 839-843, 1996.
[6] J. Zhang, H. Zhang, L. Wang, X. Guo, X. Wang, and H. Yao, "Antioxidant activities of the rice endosperm protein hydrolysate: identification of the active peptide," European Food Research and Technology, vol. 229, no. 4, pp. 709-719, 2009.
[7] G.-H. Li, M.-R. Qu, J.-Z. Wan, and J.-M. You, "Antihypertensive effect of rice protein hydrolysate with in vitro angiotensin I-converting enzyme inhibitory activity in spontaneously hypertensive rats," Asia Pacific Journal of Clinical Nutrition, vol. 16, no. S1, pp. 275-280, 2007.
[8] H. Zhang, G. E. Bartley, C. R. Mitchell, H. Zhang, and W. Yokoyama, "Lower weight gain and hepatic lipid content in hamsters fed high fat diets supplemented with white rice protein, brown rice protein, soy protein, and their hydrolysates," Journal of agricultural and food chemistry, vol. 59, no. 20, pp. 10927-10933, 2011.
[9] A. Kannan, N. Hettiarachchy, M. G. Johnson, and R. Nannapaneni, "Human colon and liver cancer cell proliferation inhibition by peptide hydrolysates derived from heat-stabilized defatted rice bran," Journal of agricultural and food chemistry, vol. 56, no. 24, pp. 11643-11647, 2008.
[10] L. Amagliani, J. O′Regan, A. L. Kelly, and J. A. O′Mahony, "The composition, extraction, functionality and applications of rice proteins: A review," Trends in food science & technology, vol. 64, pp. 1-12, 2017.
[11] H. Belitz, W. Grosch, and P. Schieberle, "Food Chemistry 4th Revised and Extended Edition. 315-327," ed: Springer-Verlag, Berlin, Heidelberg, 2009.
[12] J. Hamada, "Characterization of protein fractions of rice bran to devise effective methods of protein solubilization," Cereal Chemistry, vol. 74, no. 5, pp. 662-668, 1997.
[13] S. Agboola, D. Ng, and D. Mills, "Characterisation and functional properties of Australian rice protein isolates," Journal of cereal science, vol. 41, no. 3, pp. 283-290, 2005.
[14] F. F. Shih and K. W. Daigle, "Preparation and characterization of rice protein isolates," Journal of the American Oil Chemists′ Society, vol. 77, no. 8, pp. 885-889, 2000.
[15] W. J. Lahl, "Enzymatic production of protein hydrolysates for food use," Food Sci., vol. 48, pp. 68-71, 1994.
[16] W. Qi and Z. He, "Enzymatic hydrolysis of protein: mechanism and kinetic model," Frontiers of Chemistry in China, vol. 1, no. 3, pp. 308-314, 2006.
[17] R. D. Phillips and L. Beuchat, "Enzyme modification of proteins," Protein functionality in foods, vol. 13, no. 3, pp. 275-298, 1981.
[18] M. I. Mahmoud, W. T. MALONE, and C. T. Cordle, "Enzymatic hydrolysis of casein: effect of degree of hydrolysis on antigenicity and physical properties," Journal of Food Science, vol. 57, no. 5, pp. 1223-1229, 1992.
[19] T. Godfrey and S. West, Industrial enzymology. London: Macmillan, 1996.
[20] J. Adler‐Nissen, "Limited enzymic degradation of proteins: A new approach in the industrial application of hydrolases," Journal of Chemical Technology and Biotechnology, vol. 32, no. 1, pp. 138-156, 1982.
[21] Q. Zhao et al., "Enzymatic hydrolysis of rice dreg protein: effects of enzyme type on the functional properties and antioxidant activities of recovered proteins," Food chemistry, vol. 134, no. 3, pp. 1360-1367, 2012.
[22] A. Clemente, J. Vioque, R. Sanchez-Vioque, J. Pedroche, and F. Millán, "Production of extensive chickpea (Cicer arietinum L.) protein hydrolysates with reduced antigenic activity," Journal of Agricultural and Food Chemistry, vol. 47, no. 9, pp. 3776-3781, 1999.
[23] J. Adler-Nissen, "Some fundamental aspects of food protein hydrolysis," Enzymic hydrolysis of food proteins, pp. 9-24, 1986.
[24] N. Sripathy, D. Sen, N. L. Lahiry, A. Sreenivasan, and V. Subrahmanyan, "Fish hydrolysates. II. Standardisation of digestion conditions for preparation of hydrolysates rich in peptones and proteoses," Food Technology, vol. 16, no. 5, pp. 141-142, 1962.
[25] P. M. Nielsen, "Enzyme Technology for Production of Protein-Based Flavours," Novo Nordisk A/S, 1995.
[26] Y. Zhang, K. MURAMOTO, and F. YAMAUCHI, "Hydrolysis of soybean proteins by a vortex flow filtration membrane reactor with Aspergillus oryzae proteases," Journal of food science, vol. 61, no. 5, pp. 928-931, 1996.
[27] S. Frokjaer, "Use of hydrolysates for protein supplementation," Food technology (USA), 1994.
[28] G. K. Grimble and D. B. Silk, "Peptides in human nutrition," Nutrition research reviews, vol. 2, no. 1, pp. 87-108, 1989.
[29] 陳怡宏, "生物活性胜肽及其合成 " 食品工業月刊, 1999.
[30] H. Meisel, "Multifunctional peptides encrypted in milk proteins," Biofactors, vol. 21, no. 1‐4, pp. 55-61, 2004.
[31] E. Maestri, M. Marmiroli, and N. Marmiroli, "Bioactive peptides in plant-derived foodstuffs," Journal of proteomics, vol. 147, pp. 140-155, 2016.
[32] K. Chan, E. De Cker, and W. Means, "Extraction and activity of carnosine, a naturally occurring antioxidant in beef muscle," Journal of Food Science, vol. 58, no. 1, pp. 1-4, 1993.
[33] 中華民國防高血壓協會網站. http://hypertension.org.tw/know.php
[34] 林新進. (2009). 淺談高血壓.
[35] 蔡岡廷. (2009). 高血壓的預防與治療.
[36] R. N. Re, "Obesity-related hypertension," The Ochsner Journal, vol. 9, no. 3, pp. 133-136, 2009.
[37] S. L. Bacon, A. Sherwood, A. Hinderliter, and J. A. Blumenthal, "Effects of exercise, diet and weight loss on high blood pressure," Sports Medicine, vol. 34, no. 5, pp. 307-316, 2004.
[38] T. J. Moore, P. R. Conlin, J. Ard, L. P. Svetkey, and D. C. R. Group, "DASH (Dietary Approaches to Stop Hypertension) diet is effective treatment for stage 1 isolated systolic hypertension," Hypertension, vol. 38, no. 2, pp. 155-158, 2001.
[39] A. Atkinson and J. Robertson, "Captopril in the treatment of clinical hypertension and cardiac failure," The Lancet, vol. 314, no. 8147, pp. 836-839, 1979.
[40] M. R. Weir, "Effects of renin-angiotensin system inhibition end-organ protection: can we do better?," Clinical therapeutics, vol. 29, no. 9, pp. 1803-1824, 2007.
[41] B. J. Bhuyan and G. Mugesh, "Angiotensin converting enzyme inhibitors in the treatment of hypertension," Current Science, vol. 101, no. 7, pp. 881-887, 2011.
[42] A. Pihlanto-Leppälä, "Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides," Trends in food science & technology, vol. 11, no. 9-10, pp. 347-356, 2000.
[43] M. R. Weir and V. J. Dzau, "The renin-angiotensin-aldosterone system: a specific target for hypertension management," American journal of hypertension, vol. 12, no. S9, pp. 205S-213S, 1999.
[44] R. Natesh, S. L. Schwager, E. D. Sturrock, and K. R. Acharya, "Crystal structure of the human angiotensin-converting enzyme–lisinopril complex," Nature, vol. 421, no. 6922, p. 551, 2003.
[45] P. R. Studdy, R. Lapworth, and R. Bird, "Angiotensin-converting enzyme and its clinical significance--a review," Journal of clinical pathology, vol. 36, no. 8, pp. 938-947, 1983.
[46] D. Cushman and H. Cheung, "Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung," Biochemical pharmacology, vol. 20, no. 7, pp. 1637-1648, 1971.
[47] M. A. Ondetti, B. Rubin, and D. W. Cushman, "Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents," Science, vol. 196, no. 4288, pp. 441-444, 1977.
[48] D. W. Cushman, H. Cheung, E. Sabo, and M. Ondetti, "Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids," Biochemistry, vol. 16, no. 25, pp. 5484-5491, 1977.
[49] A. Michaud, T. A. Williams, M.-T. Chauvet, and P. Corvol, "Substrate Dependence of Angiotensin I-Converting Enzyme Inhibition: Captopril Displays a Partial Selectivity for Inhibition ofN-Acetyl-Seryl-Aspartyl-Lysyl-Proline Hydrolysis Compared with That of Angiotensin I·," Molecular pharmacology, vol. 51, no. 6, pp. 1070-1076, 1997.
[50] L. Niskanen, T. Hedner, L. Hansson, J. Lanke, and A. Niklason, "ACE inhibitor as one of several possible first-line agents is reasonable for diabetic patients with hypertension," Diabetes care, vol. 25, no. 8, pp. 1488-1489, 2002.
[51] C. U. o. U. S. Inc., "Using ACE Inhibitors to treat: High Blood Pressure and Heart Disease(Comparing Effectiveness, Safety, and Price)," pp. p.2-19, 2011.
[52] P. F. Semple, "Putative mechanisms of cough after treatment with angiotensin converting enzyme inhibitors," Journal of hypertension. Supplement: official journal of the International Society of Hypertension, vol. 13, no. 3, pp. S17-21, 1995.
[53] J. D. Irvin and J. M. Viau, "Safety profiles of the angiotensin converting enzyme inhibitors captopril and enalapril," The American journal of medicine, vol. 81, no. 4, pp. 46-50, 1986.
[54] B. Hernández-Ledesma, M. del Mar Contreras, and I. Recio, "Antihypertensive peptides: production, bioavailability and incorporation into foods," Advances in colloid and interface science, vol. 165, no. 1, pp. 23-35, 2011.
[55] H. G. Kristinsson and B. A. Rasco, "Fish protein hydrolysates: production, biochemical, and functional properties," Critical reviews in food science and nutrition, vol. 40, no. 1, pp. 43-81, 2000.
[56] H. Geisenhoff, "Bitterness of soy protein hydrolysates according to molecular weight of peptides," 2009.
[57] 張靜如, "白殭菌纖溶酶之分離純化與特性研究," 碩士, 生物技術研究所, 朝陽科技大學, 台中市, 2006.
[58] C. M. Stoscheck, "[6] Quantitation of protein," in Methods in enzymology, vol. 182: Elsevier, 1990, pp. 50-68.
[59] T. Zor and Z. Selinger, "Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies", Analytical biochemistry, vol. 236, no. 2, pp. 302-308, 1996.
[60] 台大園藝系加工組第一研究室. 蛋白質濃度分析 (BCA 法).
[61] F. C. Church, H. E. Swaisgood, D. H. Porter, and G. L. Catignani, "Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins1," Journal of Dairy Science, vol. 66, no. 6, pp. 1219-1227, 1983.
[62] H. Frister, H. Meisel, and E. Schlimme, "OPA method modified by use of N, N-dimethyl-2-mercaptoethylammonium chloride as thiol componentModifizierte OPA-Methode mit N, N-Dimethyl-2-mercaptoethylammoniumchlorid als Thiolkomponente," Fresenius′ Zeitschrift fuer Analytische Chemie, vol. 330, no. 7, pp. 631-633, 1988.
[63] Z. Zhang, Q. Jin, G. Lv, L. Fan, H. Pan, and L. Fan, "Comparative study on antioxidant activity of four varieties of F lammulina velutipes with different colour," International Journal of Food Science & Technology, vol. 48, no. 5, pp. 1057-1064, 2013.
[64] K. Shimada, K. Fujikawa, K. Yahara, and T. Nakamura, "Antioxidative properties of xanthan on the autoxidation of soybean oil in cyclodextrin emulsion," Journal of agricultural and food chemistry, vol. 40, no. 6, pp. 945-948, 1992.
[65] T. C. Dinis, V. M. Madeira, and L. M. Almeida, "Action of phenolic derivatives (acetaminophen, salicylate, and 5-aminosalicylate) as inhibitors of membrane lipid peroxidation and as peroxyl radical scavengers," Archives of biochemistry and biophysics, vol. 315, no. 1, pp. 161-169, 1994.
[66] L. L. Canabady-Rochelle, C. Harscoat-Schiavo, V. Kessler, A. Aymes, F. Fournier, and J.-M. Girardet, "Determination of reducing power and metal chelating ability of antioxidant peptides: Revisited methods," Food chemistry, vol. 183, pp. 129-135, 2015.
[67] H.-G. Byun and S.-K. Kim, "Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin," BMB Reports, vol. 35, no. 2, pp. 239-243, 2002.
[68] L. Dei Piu et al., "Exploitation of starch industry liquid by-product to produce bioactive peptides from rice hydrolyzed proteins," Food chemistry, vol. 155, pp. 199-206, 2014.
[69] 陳姵均, "米蛋白酵素水解物之製備及其對血管收縮素轉化酶之抑制效果," 碩士, 食品暨應用生物科技學系所, 國立中興大學, 台中市, 2014.
[70] 彭詩純, "鯖魚肉酵素水解物之游離胺基酸及胜肽與抗氧化性," 碩士, 食品科學系, 國立海洋大學, 基隆市, 2003.
[71] A. Jaiswal, R. Bajaj, B. Mann, and K. Lata, "Iron (II)-chelating activity of buffalo α S-casein hydrolysed by corolase PP, alcalase and flavourzyme," Journal of food science and technology, vol. 52, no. 6, pp. 3911-3918, 2015.
[72] M. Mirzaei, S. Mirdamadi, M. R. Ehsani, and M. Aminlari, "Production of antioxidant and ACE-inhibitory peptides from Kluyveromyces marxianus protein hydrolysates: Purification and molecular docking," Journal of food and drug analysis, vol. 26, no. 2, pp. 696-705, 2018.
[73] S. Gammoh et al., "The effects of protein-phenolic interactions in wheat protein fractions on allergenicity, antioxidant activity and the inhibitory activity of angiotensin I-converting enzyme (ACE)," Food Bioscience, vol. 24, pp. 50-55, 2018.
[74] X. Wang, H. Chen, X. Fu, S. Li, and J. Wei, "A novel antioxidant and ACE inhibitory peptide from rice bran protein: Biochemical characterization and molecular docking study," LWT-Food Science and Technology, vol. 75, pp. 93-99, 2017.
[75] P. Zou, J. L. Wang, G. Q. He, and J. Wu, "Purification, Identification, and In Vivo Activity of Angiotensin I‐Converting Enzyme Inhibitory Peptide, from Ribbonfish (Trichiurus haumela) Backbone," Journal of food science, vol. 79, no. 1, pp. C1-C7, 2014.

指導教授

徐敬衡(Chin-Hang Shu)

審核日期

2019-1-18

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