臺灣博碩士論文加值系統

摘要
一、以本省產之黃金蜆為原料，將生鮮蜆肉以熱水抽出法或將剩餘蜆肉經由凍乾成粉末後，利用蛋白酶Protease N(PN)、Protamex(PX)於50℃進行一次或二次(Flavourzyme)水解，探討熱水抽出物與蛋白酶水解物對血管升壓素轉換酶(ACE)之抑制。由熱水抽出法得到蜆肉之抽出物其可溶性蛋白質含量為85 mg/g，胜肽含量為84 mg/g。而對ACE之抑制IC50值為1.95 mg/ml。蜆肉粉末水解物中可溶性蛋白含量以Protease N一次水解2小時者(PN2)最高，為635 mg/g。胜肽含量以Protease N一次水解五小時再經Flavourzyme二次水解0.5小時者(PN5F0.5)最高，為348 mg/g。對ACE抑制能力而言，蜆肉粉末以Protamex一次水解5小時(PX5)者最佳，IC50值為0.043 mg/ml。另一方面，PX5水解物與Captopril 分別屬於混合型抑制劑與競爭型抑制劑，其Ki值分別為0.032 mg/ml 與0.0067 μg/ml。將蜆肉粉末水解物(PX5)以G-25膠體層析法進行劃分，可得到四個主要波峯，其中以分子量介於420至380 Da間之劃分物具有最強的ACE抑制活性，其有效抑制百分比為1314.7%/mg/ml。PX5之劃分收集物主要波峰D1及D2，經鑑定序列分別為Val-Lys-pro及Val-Lys-Lys。

二、以本省產之牡蠣為原料，將生鮮牡蠣以熱水抽出法或將剩餘牡蠣經由凍乾成粉末後，利用蛋白酶Protease N(PN)、Protamex(PX)於50℃進行一次或二次(Flavourzyme)水解，探討熱水抽出物與蛋白酶水解物對血管升壓素轉換酶(ACE)之抑制。由熱水抽出法得到牡蠣粉末之抽出物其可溶性蛋白質含量為244 mg/g，胜肽含量為238 mg/g。而對ACE之抑制IC50值為0.95 mg/ml。牡蠣粉末水解物中可溶性蛋白含量以Protease N一次水解2小時者(PN2)最高，為438 mg/g。胜肽含量以Protease N一次水解五小時再經Flavourzyme二次水解0.5小時者(PN5F0.5)最高，為474 mg/g。對ACE抑制能力而言，牡蠣粉末以Protamex一次水解2小時者再經Flavourzyme二次水解0.5小時者(PN2F0.5)最高最佳，IC50值為0.16 mg/ml。而以不具苦味之水解物(PX5F0.5)以G-25膠體層析法進行劃分，可得到四個主要波峯，其中以分子量介於450至390 Da間之劃分物具有最強的ACE抑制活性，其有效抑制百分比為364.6%/mg/ml。以PX5F0.5水解物餵食原發性高血壓老鼠八週後其收縮壓與舒張壓分別較控制組下降18.6及19.6 mmHg。

Abstract
1.The muscle of golden freshwater clam was extracted using hot water. The residual muscle was freeze dried then hydrolyzed by Protease N (PN) or Protamex (PX) as primary hydrolysis followed by a secondary hydrolysis (Flavourzyme, F) at 50℃. The effects of hot water extracts and hydrolysates on inhibitory activity against angiotensin I converting enzyme (ACE) were investigated. The soluble protein and peptide content of hot water extracts was 85 and 84 mg/g, repectively. The IC50 on ACE was 1.95 mg/ml. The highest value in soluble protein (635 mg/g) and peptide content (348 mg/g) of hydrolysate were obtained from PN hydrolysis for 2 hr or PN hydrolysis for 5 hr followed by F hydrolysis for 0.5 hr, respectively. However, the lowest IC50 of hydrolysate on ACE (0.043 mg/ml) was obtained by PX hydrolysis for 5 hr (PX5). The kinetics of the hydrolysate on ACE-inhibition indicated that PX5 and Captopril produced mixed inhibition and competitive inhibition, respectively. Their Ki values were 0.032 mg/ml and 0.0067 μg/ml, repectively. The hydrolysate of PX5 was fractionated by gel permeation chromatography with Sephadex G-25. The fraction D with molecular weight 420-380 Da showed the highest inhibitory efficiency ratio being 1314.7 %/mg/ml. The amino acid sequences of PX5 main peak of D1 and D2 were Val-Lys-Pro and Val-Lys-Lys, respectively.
2.The muscle of oyster was extracted using hot water. The residual muscle was freeze dried then hydrolyzed by Protease N (PN) or Protamex (PX) as primary hydrolysis followed by a secondary hydrolysis (Flavourzyme, F) at 50℃. The effects of hot water extracts and hydrolysate on inhibitory activity against angiotensin I converting enzyme (ACE) was investigated. The soluble protein and peptide content of hot water extracts was 244 and 238 mg/g, repectively. The IC50 of ACE was 0.95 mg/ml. The highest value in soluble protein (438 mg/g) and peptide content (474 mg/g) of hydrolysate were obtained from PN hydrolysis for 2 hr or PN hydrolysis for 5 hr followed by F hydrolysis for 0.5 hr, respectively. However, the lowest IC50 of hydrolysate on ACE (0.16 mg/ml) was obtained by PX hydrolysis for 2 hr followed by F hydrolysis for 0.5 hr (PX2F0.5). No bitterness was obtained by PX hydrolysis for 5 hr followed by F hydrolysis for 0.5 hr (PX5F0.5). The hydrolysate of PX5F0.5 was fractionated by gel permeation chromatography with Sephadex G-25. The fraction C with molecular weight 450-390 Da showed the highest inhibitory efficiency ratio being 364.6 %/mg/m. Oyster hydrolysate (PX5F0.5) was orally administrated to spontaneously hypertensive rats (SHR). After 8 weeks oral administration of hydrolysate, the systolic blood pressure and diastolic blood pressure of SHR were significantly reduced by 18.6 and 19.6 mmHg, respectively.

目 錄
頁次
中文摘要.................................................. Ⅰ
英文摘要.................................................. Ⅲ
壹、前言...................................................
貳、文獻整理............................................... 1
3
一、台灣重要經濟貝類....................................... 3
1.台灣蜆.............................................. 3
(1)蜆之介紹.......................................... 3
(2)蜆養殖情況........................................ 3
(3)蜆之成分分析...................................... 4
(4)蜆之加工及保健機能................................ 4
2.牡蠣................................................ 5
(1)牡蠣之介紹........................................ 5
(2)牡蠣養殖情況...................................... 6
(3)牡蠣之成分分析.................................... 6
(4)牡蠣之加工及保健機能............................... 6
二、蛋白質水解產物......................................... 7
1.蛋白質水解產物之簡介................................ 7
(1)分類.............................................. 7
(2)特性及應用........................................ 7
(3)苦味性............................................ 9
2.蛋白質水解方式...................................... 10
3.影響酵素水解蛋白質之因子............................ 12
(1)酵素種類......................................... 12
(2)pH值與溫度....................................... 12
三、高血壓之定義與分類.................................... 13
1.定義................................................ 13
2.分類................................................ 14
(1)原發性高血壓...................................... 14
(2)續發性高血壓...................................... 15
四、血管升壓素轉換(ACE)之生化特性....................... 15
1.ACE的生化特性....................................... 15
2.ACE的抑制原理....................................... 17
五、ACE抑制劑之來源....................................... 18
1.水產物蛋白水解物中的ACEI............................ 18
(1)沙丁魚............................................. 18
(2)鹽漬乾燥鮪魚肉..................................... 19
(3)烏賊............................................... 19
(4)鰹柴魚............................................. 19
(5)鰹魚內臟........................................... 20
(6)貝類............................................... 20
六、原發性高血壓老鼠簡介................................... 21
参、實驗材料與方法........................................ 23
一、實驗材料.............................................. 23
二、實驗方法.............................................. 23
1.蜆肉熱水抽出物與蜆肉粉末酵素水解物的製備............ 23
2.牡蠣粉末熱水抽出物與牡蠣粉末酵素水解物的製備........ 24
3.產製率的測定........................................ 24
4.可溶性蛋白質含量的測定............................... 25
5.胜肽含量的測定....................................... 25
6.ACE抑制能力之測定................................... 25
7.IC50值的測定......................................... 26
8.水解物對ACE抑制類型之評估及Ki之測定................ 26
9.水解物主要胜肽之收集................................. 27
10.劃分收集物對ACE抑制活性之測定...................... 27
11.水解物主要胜肽之純化、鑑定.......................... 28
12.胺基酸組成分析...................................... 28
13.胺基酸序列分析...................................... 29
14.動物飲液的製備...................................... 29
15.實驗動物飼養條件及實驗項目.......................... 29
16.老鼠血壓之測定...................................... 29
17.統計分析............................................ 30
肆、結果與討論............................................. 31
一、蜆..................................................... 31
(一) 不同蛋白酶與水解時間對蜆肉粉末水解物性質之影響.... 31
1.苦味性及可溶性固形物............................... 31
2.可溶性蛋白質與胜肽含量.............................. 31
3.分子量分佈.......................................... 32
(二)蜆肉粉末水解物對抑制血管升壓素轉換(ACE)之IC50值的響..................................................
33
(三)蜆肉粉末水解物之胜肽含量與抑制血管升壓素轉換酶(ACE)活性百分比之間的關係................................
33
(四)蜆肉粉末水解物之胺基酸組成分析...................... 33
1.蜆肉粉末水解物之劃分收集物的胺基酸組成分析........... 34
(五)蜆肉粉末水解物之劃分收集物主要胜肽的純化分離........ 34
(六)蜆肉粉末蛋白酶水解物(PX5)之劃分收集物主要波峰的N-端胺基酸序列分析......................................
35
(七)抑制物之IC50值，抑制常數及抑制類型.................. 35
二、牡蠣................................................... 36
(一)不同蛋白酶與水解時間對牡蠣粉末水解物性質之影響...... 36
1.苦味性及可溶性固形物................................ 36
2.可溶性蛋白質與胜肽含量............................... 36
3.分子量分佈........................................... 37
(二)蜆肉粉末水解物對抑制血管升壓素轉換(ACE)之IC50值影響..................................................
38
(三)牡蠣粉末水解物之胜肽含量與抑制血管升壓素轉換酶(ACE)活性百分比之間的關係................................
38
(四)牡蠣粉末水解物之胺基酸分析.......................... 39
(五)比較蜆肉粉末水解物(PX5)與牡蠣粉末水解物(PX5F0.5)之數據..................................................
39
(六)牡蠣粉末水解物對原發性高血壓老鼠的影響.............. 40
1.飲液、飼料攝取量..................................... 40
2.收縮壓的變化......................................... 41
3.舒張壓的變化......................................... 41
4.收縮壓增加量......................................... 42
5.心跳速率............................................. 42
6.體重................................................. 42
伍、結論................................................... 43
陸、參考文獻............................................... 44
圖表...................................................... 53

六、參考文獻
Abebe, W., and Mozaffari, M. S. 2000. Effects of chronic taurine treatment on reactivity of the rat aorta. Amino Acids. 19:615-623.
Alder-Nissen, J.1986. “Enzymatic Hydrolysis of Food Proteins”. Elsevier Applied Science Pub. New York.
Ariyoshi, Y. 1993. Angiotensin-converting enzyme inhibitors derived from food proteins. Trends in Food Sci. and Technol. 4:139-144.
Astawan, M., Wahyun I, M., Yasuhara, T., Yamada, K.,Tadokoro, T., and Maekawa, A. 1995. Effect of angiotensin I-converting enzyme inhibitory substances derived from Indonesian dried-salted fish on blood pressure of rats. Biosci. Biotech. Biochem. 59(3):425-429.
Cheftel, C., Aherm, M., Wang, D. I. C., and Tannenbaun, S. R. 1971. Enzyme solubilization of fish protein concentrate : Batch studies applicable to continuous enzyme recycling processes. J. Agr. Food Chem. 19(1):155-161.
Cheung, H. S. and Chushman, D. W. 1971. spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem. Pharmacol. 20: 1637-1648.
Cheung, H. S., Wang, F. L. Ondetti, M. A,. Sabo, E. F., and Cushman, D. W. 1980. Binding of peptide substrates and inhibitors of angiotensin- converting enzyme. J. Biol. Chem. 255(2):401- 407.
Church, F. C., Swaisgood, H. E., Porter, D. H. and Catignani, G. L. 1983. Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J. Dairy Sci. 66:1219-1227.
Corvol, P., Ewilliams, T. A., and Soubrier, F. 1995. Peptidyl dipeptidease A: angiotensin I-converting enzyme. Methods Enzymol. 248:283-305.
Diniz, E. M. and Martin, A. M. 1997. Effect of the extract of enzymatic hydrolysis on functional properties of shark protein hydrolysate. Lebensm.Wiss. Technol. 30:266-272.
Gildberg, A. and Raa, J. 1977. Properties of propionic acid/formic acid preserved silage of cod viscera. J. Sci. Food Agric. 28:647-635.
Gildberg, A. 1993. Enzymatic processing of marine raw materials. Process
Biologically.
Godfrey, T. and West, S. 1996. Industrial Enzymoloy. Macmillan Press, London.
Harvey, R. A. and Champe, P. C. 1997.“Lippincott’ s Illustrated Reviews Pharmacology.”J. B. Lippincott-Raven Publishers. Washington. pp. 239-251, 501-508.
Higashi, Y., Oshima, T., Ozono, R., Matsuura, H., Kambe, M. and Kajiyama, G. 1999. Effect of L-Arginine infusion on systemic and renal hemodynamic in hypertensive. American Journal of Hypertension. 12:8-15.
Hole, R. and Oines, S. 1991. Can fish silage be used as nutritional solution to reduce aquaculture waste when considering the slaughtering quality of fish. In “Nntritional Strategies and Aquaculture Waste”, PP. 103-109.
Hooper, N. M. and Turner, A. J. 1987. Isolation of two differentially glycosylated froms of peptidyl-dipeptidase A (angiotensin converting enzyme)from pig brain: a re-evaluation of their role in neuropeptide metabolism. Biochem. J. 241:625-633.
Hidalgo, J. and Gamper, E. 1977. Solubility and heat stability whey protein
Concentrates. J. Dairy Sci. 60:1518.
Jost, R. and Monti, J. C. 1997. Partial enzymatic hydrolysis of whey protein
by trypsin. J. Dairy Sci. 60:1387-1393.
Kester, J. J. and Richardson, T. 1984. Modification of whey proteins to improve functionality. J. Dairy Sci. 67:2757-2774.
Korhonen, H., Pihlanto-Leppala, A., Rantamaki, p. and Tupasela, T. 1998. Impact of processing on bioactive proteins and peptides. Food Sci. Technol. 9:307-319.
Laha, W. J. and Braun, S. D. 1994. Emzymatic production of protein hydrolysate for food use. Food Technol. 48(10):68-71.
Lee, T. G. and Maruyama, S. 1998. Isolation of HIV-1 protease-inhibiting peptide from thermolysin hydrolysate of oyster proteins. Biochemical and Biophysical Research Communications. 253(3):604-608.
Lemineux, L. Puchades, P. and Simard, R. E. 1989. Size-exclusion HPLC separation of bitter and astringent fractions from Cheegar made with added Lactobacillus strains to accelerate ripening. J. Food Sci. 54(5):1234-1237.
Liu, D. Z., Lin, Y. S. and Hou, W. C. 2004. Monohydroxamates of aspartic acid and glutamic acid exhibit antioxidant and angiotensin converting enzyme inhibitory. J. Agric. Food Chem. 52:2386-2390.
Lo, K. V., Liao, P. H. and Bullock, C. 1993. Silage production from salmon
Farm mortalities. Aguacultural Engineering. 12:37-45.
Meahashi, K., Matsuzaki, M., Yamamoto, Y., and Udaka, S. 1999.Isolation of peptides from an enzymatic hydrolysate of food proteins and characterization of their taste properties. Biosci. Biotechnol. Biochem. 63(3):555-559.
Mahmoud, M. I. 1994. Physicochemical and functional properties of protein hydrolysates in nutritional product. Food Technol. 48(10):89-95.
Maruyama, S., Nakagomi, K., Tomizuka, N. and Suzuki, H. 1985. Angiotensin I-converting enzyme inhibtor derived from and enzymatic drydrolysate of casein. II. Isolation and Bradykinin- potentiating activity on the uterus and the ileum of rats. Agr. Biol. Chem. 49: 1405-1409.
Matsui, T., Matsufuiji, H., Seki, E., Osajima, K., Nakashima, M., and Osajima, Y.1993. Inhibition of angiotension I-converting enzyme by Bacillus licheniformis alkaline protease hydrolysates derved from sardine muscle. Biosic. Biotech. Biochem.57(6):922-925.
Matsumra, N., Fujii, M., Takeda, Y., and Shimizu, T. 1993. Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels. Biosci. Biotech. Biochem. 57(10):1743-1744.
Matsumoto, K., Ogikubo, A., Yoshino, T., Matsui, T., and Osajima, Y. 1994. Separation and purification of angiotensin I converting enzyme Inhibitory peptide in peptic hydrolyzate of oyster. Nippon Shokuhin kogyo
Gakkaishi. 41（9）：589-594.
Nakamura, Y., Yamamoto, N., Sakai, K., Okubo, A., Yamazaki, S., and Takano, T. 1995. Anytihypertensive effect of sour milk and peptides isolated from it that are inhibitors to angiotensin- converting enzyme. J. Dairy Sic. 78: 1253- 1257.
Monti, J. C. and Jost, R. 1978. Enzymeatic solubilulization of heat-denatured chesse whey protein. J. Dairy Sci. 61:1233-1237.
Noguchi, M., Yamashita, M., Arai, S., and Fujimaki, M. 1975. On the bitter-masking activity of a glutamic acid-rich oligopeptide fraction. J. Food Sci. 40:367-369.
Rebebeca, B. D., Pena-vera, M. T., and Diaze-castaneda, M. 1991. Production of fish protein hydrolysates with baterial protease: yield and nutritional value. J. Food Sci. 56(2):309-314.
Rubinstein, I., Houmsse, M., Dacvis, R.G., and Visfhwanatha, J. K. 1992. Tissue angiotensin I-converting enzyme activity in spontaneously hypertensive hamsters. Biochemical and Biophysical Reasearch Communication. 183(3):1117-1123.
Seki, E., Osajima, K., Matsufuji, H., Matsuim, T., and Osajima, Y. 1996. Resistance to gastrointestinal proteases of the short chain peptides having reductive effect in blood pressure. Nippon Shokuhin Kagaku Kogaku Kaishi. 43(5):520-525.
Schaffer, S. W., Lombardini, J. B., and Azuma, J. 2000. Interaction between the action of taurine and angiotensin II. Amino Acides. 18：305-318.
Shinoda, I., Nosho, Y., Kouge, K., Ishibashi, N., Okai, H., Tatsumi, K., Kikuchi, E. 1987. Variation in bitterness potency when introducing gly-gly residue into bitter peptides. Agric. Biol. Chem. 51(8):2103-2110.
Sikorski, Z. E. and Ruiter, A. 1994. Changes in proteins and nonprotein nitrogen compounds in crude fermented and dried seafood. In “Seafood protein”, PP. 113-126. Eds. Zdzislaw, New York.
Suetsuna, K., Yamagami, M., and Kuwata, K. 1988. Inhibitory activity against angiotensin I-converting enzyme of peptides originating from fish and shellfish muscle. Nippon Suisan Gakkaishi. 54（10）：1853.
Suetsuna, K., and Osajima, K. 1989. Blood pressure reduction and vasodilator effects in vivo of peptides originating from sardine muscle. Nippon Eiyo Shokuryo Gakkaishi. 42:47-54.
Suetsuna, K. 2002. Identification of antihypertensive peptides from peptic digest of the short-necked clam tapes philippinarum and the pearl oyster pinctada fucata martensii. Fisheries Science. 68：233-235.
Sugiyama, K., Egana, M., Onzuka, H. and Oba, K. 1991. Characteristics of sardine muscle hydrolysate prepared by various enzymic treatments. Nippon Suisan Gakkaishi. 57:475-479.
Tamura, M., Mori, N., Miyoshi, T., Koyama, S. Kohri, H., and Okai, H. 1990. Practical debittering using model peptides and related compounds. Agric. Biol. Chem. 54(1):41-51.
Tatterson, I. N. and Windesor, M. L. 1974. Fish silage. J. Sci. Food Agric. 25:369-379.
Toshiro, M., Hiroshi, M., Eiji, S., Katsuhiro, O., Masatoshi, N. and Yutaka, O. 1993. Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates derived from sadine muscle. Biosci. Biotech. Biochem. 57(6):922-925.
Ukeda, H., Matsuda, H., Osajima, K., Matsufuji, H., Matsui, T. and Osajima, Y. 1992. Peptides from peptic hydrolyzate of heated sardine meat that inhibit angiotensin I-converting enzyme. Nippon Nogei- kagaku Kaishi 66:25-29.
Valletri, P. A., Billingsley, M. L. and Lovenberg, W. 1985. Thermal denaturation of rat pulmonary and testicular angiotensin-converting enzyme isozymes. Effects of chelators and CoCl2. Biochem. Biophys. Acta 839:71-82.
Wako, Y., Ishikawa, S., and Muramoto, k. 1996. Angiotensin I-converting enzyme inhibitors in autolysates of squid liver and mantle muscle. Biosci. Biotech. Biochem. 60(8):1353-1355.
Yokoyama, K., Chiba, H.,and Yoshikawa, M. 1992. Peptide inhibitors for angiotensin I-converting enzyme from trermolysin digest of dried bonito. Biosci. Biotech. Biochem. 56(10):1541-1545.
Zhang, X.,Tenner, T.E., Lombardini, J. B. 1999. Inhibtion of rat vascular smooth muscle cell proliferation by taurine and Analogues.
Biochemial Pharmacology. 57:1331-1339.
王文亮與駱秋燕，1989。蜆之衛生調查及醃蜆加工試驗。台灣省水產試驗所報告。43:269-280。
行政院衛生署，2001。中華民國台灣地區公共衛生概況調查。台北。
巫文隆，1979。台灣蜆型態測定學的研究。貝類學報。6:1-12。
行政院主計處，1998。國人十大死亡原因統計。中華民國統計月報: 9月。
何雲達，1995。貝類養殖(三)蜆。台灣農家要覽漁業篇。P.252。豐年社。台北。
邱思魁、蕭泉源、藍惠玲，1997。養殖台灣蜆化學成分之季節變化。食品科學。24:469-478。
林志生，2003。飲用蜆萃取物對酒精性肝臟損傷之影響。中華民國營養學會雜誌。28:26-33。
林志生，1999。蜆萃出物成分對機能保健的探討及提高產製效益之研究。八十八年度農委會主管試驗研究計畫期末摘要報告。
周良雄、楊中平、陳靜暉及劉鴻榮，1991。牛磺酸對大白鼠心血管之作用。北醫學報。20：41-48。
陳聰松，1996。貝類。水產加工。P.94。豐年社。台北。
陳聰松，1999。介紹幾種水產品的特殊機能。潮訊。109:4-11。
陳聰松、馮貢國、高淑雲、朱正名、潘泰安、蔡宗哲、王文亮。1994。蜆精粉加工可行性研究。水產研究。2:75-84。
陳讚昌、廖國焱、巫文隆。1992。台灣蜆(Corbicular fluminea)在本省之研究與展望。貝類學報。17:37-49。
陳慧玲，1996。血管收縮素轉換酶的檢測、純化及性質之研究。台灣
大學農業化學研究所博士論文。
陳美貞，1998。鯖魚肉蛋白質水解物對血管升壓素轉換酶之抑制及其降高血壓的效果。國立台灣海洋大學食品科學系碩士論文。
陳冠文，2001。發酵牛乳萃取液對血管升壓素轉換酶之抑制及其降高血壓的效果。國立台灣海洋大學食品科學系碩士論文。
陳長堅，2003。蜆粉或蜆精對四氯化碳誘發之肝障害大白鼠肝臟脂質過氧化的影響。國立台灣海洋大學食品科學系碩士論文。
陳莉臻、蕭泉源、林瑞堂。2001。泡水處理對牡蠣化學成分與品質之影響。台灣農化與食品科學。39:122-128。
許雅芳，2003。鯖柴魚水解物中胜肽對血管生壓素轉換酶之抑制與其純化。國立台灣海洋大學食品科學系碩士論文。
黄巧淇，2001。文蛤熱水萃取物醣蛋白之細胞凋亡誘導機制。國立台灣海洋大學食品科學系碩士論文。
國家實驗動物中心，1997。實驗動物品系特微。生命科學簡訊。11(5):6-6。
郭仁杰、何雲達，1997。台灣蜆養殖業之經營現況與經濟分析。水產研究。5:141-155。
程竹青，1996。蛋白質水解液苦味之探討。食品工業月刊，28(5):32-39。
馮貢國，1998。養殖台灣蜆的熱水萃取物和蜆肉酵素水解物的生物活性
評估。台灣海洋大學食品科學研究所碩士論文。台北。
揚樂靜，1994。自發性高血壓老鼠(spontaneously hypertensive rat)高血壓神經機制之探討。國立台灣大學動物學研究所博士論文。
賴呈委，2000。文蛤凝集素樣成分之腫瘤細胞凋亡調節作用。國立台灣海洋大學食品科學系碩士論文。
閻貞坊，1994。高血壓藥物之動物實驗簡介。國家實驗動物繁殖及研究中心簡訊。