臺灣博碩士論文加值系統

劍蝦有將近 45% 原料重被作為副產物丟棄，然而其中含有豐富的蛋白質，有製備活性胜肽之潛力。本篇研究目的為通過蛋白質體學鑑定劍蝦副產物中之蛋白質，並分別以電腦模擬和體外試驗探討其潛在活性胜肽。將凍乾之劍蝦副產物以十二烷基硫酸鈉聚丙烯醯胺凝膠電泳 (Sodium dodecyl sulfate polyacrylamide gel electrophoresis, SDS-PAGE) 分開蛋白質混合物，接著裁切 9 個條帶中的蛋白質進行膠內消化，再將萃取出之胜肽以質譜分析並比對 Mascot 資料庫來鑑定之。精胺酸激酶、原肌球蛋白、微管蛋白 β-2 鏈、微管蛋白 β-1 鏈、微管蛋白α-3鏈、內質網鈣 ATP 酶和 α-肌動蛋白為劍蝦副產物中主要之 7 種蛋白質。將被鑑定出之蛋白質以 BIOPEP 資料庫進行潛在活性胜肽預測和模擬酵素水解，結果顯示劍蝦蛋白具有抑制血管收縮素I轉化酶 (Angiotensin-converting enzyme, ACE)、二肽基肽酶 - 4 (Dipeptidyl peptidase-4, DPP-4)、抗氧化的胜肽序列，其中又以具有抑制 DPP-IV 功效的胜肽頻率最高 (0.435 - 0.547)，其次是抑制 ACE 的胜肽 (0.24 - 0.35) 和抗氧化胜肽 (0.002 - 0.058)，由此推測劍蝦蛋白質可能具有降血糖、降血壓及抗氧化的功效。劍蝦副產物分別以 Papain、Bromelain 及 Pepsin 酵素進行水解 1 至 7 小時，再選用各酵素最適水解條件之水解液測定其 ACE 抑制能力，以 Pepsin 水解 5 小時之水解物 (1mg/mL) 具 ACE 抑制率最高 (94.59 ± 0.41 %)，其 ACE 抑制活性 IC50 值為 0.21 ± 0.16 mg/mL；另將 Pepsin 水解物以分子量進行劃分 （低於1 kDa、1-5 kDa、5-10 kDa 和高於 10 kDa），以低於 1 kDa 胜肽的 ACE 抑制效果最佳 (91.27 ± 0.97 %)。綜合上述，實驗結果與 BIOPEP 預測結果吻合，Pepsin 水解物產生的 ACE 抑制胜肽最多。劍蝦副產物具有調節血壓的潛力，未來可以進一步純化分析劍蝦副產物中的血管收縮素轉換酶抑制胜肽，並且定序其胺基酸組成。

About 45% by weight of spear shrimp (Parapenaeopsis hardwickii) raw materials being discarded as by-products, including heads and shells. Spear shrimp by-products contains 44% protein. The high protein content of the by-products may serve as a potential source of functional ingredients and could be used as raw material for producing value-added products. The aim of this study was to identify spear shrimp by-products potential bioactive peptides, and improve the value of by-products with proteomic approach in silico analyses. Seven major proteins, including arginine kinase, tropomyosin, tubulin beta-2 chain, tubulin beta-1 chain, tubulin alpha-3 chain, endoplasmic reticulum calcium ATPase and α-actin were characterized through proteomics techniques from nine protein bands of the sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Consequently, arginine kinase and tropomyosin were selected to analyze the profile of bioactive peptides using BIOPEP-UWM database because of the phylogenetic relationship based on protein sources were similar to Parapenaeopsis hardwickii. As a result, spear shrimp by-products were predicted to have bioactive peptides such as dipeptidyl peptidase IV (DPP-IV) inhibitor, angiotensin converting enzyme (ACE) inhibitor, antioxidative and other activities. Spear shrimp by-products protein hydrolysates was produced from spear shrimp by-products using papain, bromelain, or pepsin. The hydrolysate produced by 5 hour hydrolysis with pepsin had the highest ACE inhibitory activity (94.59 ± 0.41 %), and IC_50 value is 0.21 ± 0.16 mg / mL. Consequently, the hydrolysate was fractionated into four fractions (<1 kDa, 1–5 kDa, 5–10 kDa, and >10 kDa). The <1 kDa fraction showed the highest ACE inhibitory activity (91.27 ± 0.97%). These results indicate that the experimental results are consistent with BIOPEP prediction results. Spear shrimp by-products have a great potential to convert this underutilized material to value-added products as nutraceutical biomatrix or ingredients.

壹、前言 1
貳、文獻回顧 2
一、劍蝦的簡介 2
二、蝦副產物利用 2
1.幾丁質萃取 3
2.蝦紅素回收 3
3.飼料利用 4
4.蛋白質萃取 4
三、蛋白質水解方式 5
1.化學水解 5
2.酵素水解 5
3.微生物水解 6
四、蛋白質水解物生理活性 6
1.降血壓活性 6
2.抗氧化活性 9
3.抗菌活性 9
4.降血糖活性 10
五、影響蛋白質水解之因子 10
1. 酵素濃度 10
2. 水解時間 11
六、蛋白質鑑定 11
1. 胜肽質量指紋法 (peptide mass fingerprinting, PMF) 12
2. 串聯式質譜法 (tandem mass spectrometry, MS/MS) 13
參、實驗架構 15
肆、實驗材料與方法 16
一、實驗材料 16
1. 樣品 16
2. 酵素 16
二、實驗方法 16
1.電泳分析 16
1.1膠片製作 16
1.2 樣品製備 17
1.3電泳分析 17
2.蛋白質鑑定 17
2.1膠片裁切 17
2.2膠內消化 17
2.3胜肽萃取 18
2.4純化胜肽 18
2.5液相層析串聯質譜儀分析 18
2.6資料庫比對與蛋白質鑑定 19
3.生物資訊工具分析 19
4.酵素水解物製備 20
4.1可溶性蛋白質含量測定 20
4.2水解率分析 20
4.3胜肽含量測定 21
5.抑制血管收縮轉換酵素活性試驗 21
5.1 ACE抑制活性實驗與計算 21
5.2 IC50 值的測定 22
6. 超過濾 22
7. 統計分析 22
伍、結果與討論 23
一、劍蝦副產物之一般成分分析結果 23
二、劍蝦副產物蛋白質鑑定結果 23
三、以 BIOPEP 預測劍蝦副產物蛋白質中潛在活性胜肽之結果 24
1. 潛在活性胜肽預測 25
2. 模擬酵素水解 25
四、劍蝦副產物之酵素水解物抑制血管轉換收縮素酶之能力分析結果 26
1. 水解物特徵分析結果 26
2. 抑制血管轉換收縮素酶之能力 27
陸、結論 29
柒、未來研究方向 30
捌、參考文獻 31

漁業署。(2018)。漁業統計年報，台北市，臺灣。
黃登福, & 鄭森雄. (1985)。 以蝦類廢棄物製造蝦溶漿和蝦粉養殖淡水大蝦之效果。臺灣水產學會刊，12(1)，74-81。
Ahn, C. B., Lee, K. H., & Je, J. Y. (2010). Enzymatic production of bioactive protein hydrolysates from tuna liver: effects of enzymes and molecular weight on bioactivity. International journal of food science & technology, 45(3), 562-568.
Ambigaipalan, P., & Shahidi, F. (2017). Bioactive peptides from shrimp shell processing discards: antioxidant and biological activities. Journal of Functional Foods, 34, 7-17.
Arcan, I., & Yemenicioğlu, A. (2010). Effects of controlled pepsin hydrolysis on antioxidant potential and fractional changes of chickpea proteins. Food Research International, 43(1), 140-147.
Arcidiacono, S., & Kaplan, D. (1992). Molecular weight distribution of chitosan isolated from Mucor rouxii under different culture and processing conditions. Biotechnology Bioengineering, 39(3), 281-286.
Astawan, M., Wahyuni, M., Yasuhara, T., Yamada, K., Tadokoro, T., & Maekawa, A. (1995). Effects of angiotensin I-converting enzyme inhibitory substances derived from Indonesian dried-salted fish on blood pressure of rats. Bioscience, Biotechnology, 59(3), 425-429.
Bartlett, T. C., Cuthbertson, B. J., Shepard, E. F., Chapman, R. W., Gross, P. S., & Warr, G. W. (2002). Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus. Marine Biotechnology, 4(3), 278-293.
Battison, A. L., Summerfield, R., & Patrzykat, A. (2008). Isolation and characterisation of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus. Fish Shellfish Immunology, 25(1-2), 181-187.
Bauw, G., Van Damme, J., Puype, M., Vandekerckhove, J., Gesser, B., Ratz, G., Lauridsen, J., & Celis, J. (1989). Protein-electroblotting and-microsequencing strategies in generating protein data bases from two-dimensional gels. Proceedings of the National Academy of Sciences, 86(20), 7701-7705.
Benjakul, S., & Morrissey, M. T. (1997). Protein hydrolysates from Pacific whiting solid wastes. Agricultural and Food Chemistry, 45(9), 3423-3430.
Blanco-Pascual, N., Koldeweij, R., Stevens, R., Montero, M., Gómez-Guillén, M., & Ten Cate, A. (2014). Peptide microencapsulation by core-shell printing technology for edible film application. Food and Bioprocess Technology, 7(9), 2472-2483.
Bougatef, A. (2013). Trypsins from fish processing waste: characteristics and biotechnological applications-comprehensive review. Journal of Cleaner Production, 57, 257-265.
Bulet, P., Stöcklin, R., & Menin, L. (2004). Anti‐microbial peptides: from invertebrates to vertebrates. Immunological Reviews, 198(1), 169-184.
Chakrabarti, R. (2002). Carotenoprotein from tropical brown shrimp shell waste by enzymatic process. Food Biotechnology, 16(1), 81-90.
Chalamaiah, M., Rao, G. N., Rao, D. G., & Jyothirmayi, T. (2010). Protein hydrolysates from meriga (Cirrhinus mrigala) egg and evaluation of their functional properties. Food Chemistry, 120(3), 652-657.
Cheftel, C., Ahern, M., Wang, D. I., & Tannenbaum, S. R. (1971). Enzymic solubilization of fish protein concentrate: batch studies applicable to continuous enzyme recycling processes. Agricultural and Food Chemistry, 19(1), 155-161.
Chen, H.-M., Muramoto, K., & Yamauchi, F. (1995). Structural analysis of antioxidative peptides from Soybean β-Conglycinin. Journal of Agricultural Food Chemistry, 43(3), 574-578.
Chen, H.-M., Muramoto, K., Yamauchi, F., & Nokihara, K. (1996). Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein. Journal of Agricultural Food Chemistry, 44(9), 2619-2623.
Cheong, J. Y., Azwady, A. N., Rusea, G., Noormasshela, U., Shaziera, A. N., Azleen, A., & Muskhazli, M. (2014). The availability of astaxanthin from shrimp shell wastes through microbial fermentations, aeromonas hydrophila and cell disruptions. International Journal of Agriculture and Biology, 16(2).
Cheung, I. W., & Li-Chan, E. C. (2010). Angiotensin-I-converting enzyme inhibitory activity and bitterness of enzymatically-produced hydrolysates of shrimp (Pandalopsis dispar) processing byproducts investigated by Taguchi Design. Food Chemistry, 122(4), 1003-1012.
Clare, D., & Swaisgood, H. (2000). Bioactive milk peptides: a prospectus. Journal of Dairy Science, 83(6), 1187-1195.
Coward-Kelly, G., Agbogbo, F. K., & Holtzapple, M. T. (2006). Lime treatment of shrimp head waste for the generation of highly digestible animal feed. Bioresource Technology, 97(13), 1515-1520.
De Holanda, H. D., & Netto, F. M. (2006). Recovery of components from shrimp (Xiphopenaeus kroyeri) processing waste by enzymatic hydrolysis. Journal of Food Science, 71(5), C298-C303.
Dietrich, K. (1984). Use of chitinous polymers in food: A challenge for food research and development. Food Technology.
Dziuba, J., Iwaniak, A., & Minkiewicz, P. (2003). Computer-aided characteristics of proteins as potential precursors of bioactive peptides. POLIMERY-WARSAW-, 48(1), 50-53.
Elias, R. J., Kellerby, S. S., & Decker, E. A. (2008). Antioxidant activity of proteins and peptides. Critical Reviews in Food Science Nutrition, 48(5), 430-441.
Ennaas, N., Hammami, R., Beaulieu, L., & Fliss, I. (2015). Purification and characterization of four antibacterial peptides from protamex hydrolysate of Atlantic mackerel (Scomber scombrus) by-products. Biochemical Biophysical Research Communications, 462(3), 195-200.
Faisal, M., Vasiljevic, T., & Donkor, O. N. (2019). Effects of selected processing treatments on antigenicity of banana prawn (Fenneropenaeus merguiensis) tropomyosin. International Journal of Food Science & Technology, 54(1), 183-193.
Ferrer, J., Paez, G., Marmol, Z., Ramones, E., Garcia, H., & Forster, C. (1996). Acid hydrolysis of shrimp-shell wastes and the production of single cell protein from the hydrolysate. Bioresource Technology, 57(1), 55-60.
Fu, Y., Young, J. F., Løkke, M. M., Lametsch, R., Aluko, R. E., & Therkildsen, M. (2016). Revalorisation of bovine collagen as a potential precursor of angiotensin I-converting enzyme (ACE) inhibitory peptides based on in silico and in vitro protein digestions. Journal of Functional Foods, 24, 196-206.
Gangopadhyay, N., Wynne, K., O’Connor, P., Gallagher, E., Brunton, N. P., Rai, D. K., & Hayes, M. (2016). In silico and in vitro analyses of the angiotensin-I converting enzyme inhibitory activity of hydrolysates generated from crude barley (Hordeum vulgare) protein concentrates. Food Chemistry, 203, 367-374.
García-Orozco, K. D., Aispuro-Hernández, E., Yepiz-Plascencia, G., Calderón-De-La-Barca, A. M., & Sotelo-Mundo, R. R. (2007). Molecular characterization of arginine kinase, an allergen from the shrimp Litopenaeus vannamei. International Archives of Allergy and Immunology, 144(1), 23-28.
Gildberg, A., & Stenberg, E. (2001). A new process for advanced utilisation of shrimp waste. Process Biochemistry, 36(8-9), 809-812.
Gill, I., López-Fandiño, R., Jorba, X., & Vulfson, E. (1996). Biologically active peptides and enzymatic approaches to their production. Enzyme and Microbial Technology, 18(3), 162-183.
Gillett, R. (2008). Global study of shrimp fisheries (Vol. 475): Food and Agriculture Organization of the United Nations Rome.
Gimeno, M., Ramírez-Hernández, J. Y., Mártinez-Ibarra, C., Pacheco, N., García-Arrazola, R., Bárzana, E., & Shirai, K. (2007). One-solvent extraction of astaxanthin from lactic acid fermented shrimp wastes. Journal of Agricultural Food Chemistry, 55(25), 10345-10350.
Harris, T., Cook, E., Kannel, W., Schatzkin, A., & Goldman, L. (1985). Blood pressure experience and risk of cardiovascular disease in the elderly. Hypertension, 7(1), 118-124.
Healy, M., Romo, C., & Bustos, R. (1994). Bioconversion of marine crustacean shell waste. Resources, Conservation and Recycling, 11(1-4), 139-147.
Hjernø, K. (2007). Protein identification by peptide mass fingerprinting. In Mass Spectrometry Data Analysis in Proteomics, (pp. 61-75): Springer.
Huang, B.-B., Lin, H.-C., & Chang, Y.-W. (2015). Analysis of proteins and potential bioactive peptides from tilapia (Oreochromis spp.) processing co-products using proteomic techniques coupled with BIOPEP database. Journal of Functional Foods, 19, 629-640.
Huang, G.-R., Zhao, J., & Jiang, J.-X. (2011). Effect of defatting and enzyme type on antioxidative activity of shrimp processing byproducts hydrolysate. Food Science and Biotechnology, 20(3), 651-657.
Hussein, G., Sankawa, U., Goto, H., Matsumoto, K., & Watanabe, H. (2006). Astaxanthin, a carotenoid with potential in human health and nutrition. Journal of Natural Products, 69(3), 443-449.
Jeon, Y.-J., Byun, H.-G., & Kim, S.-K. (1999). Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes. Process Biochemistry, 35(5), 471-478.
Jun, S.-Y., Park, P.-J., Jung, W.-K., & Kim, S.-K. (2004). Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. European Food Research Technology, 219(1), 20-26.
Kan, F., You, Z., Teng, Y., Xue, C., & Mao, X. (2015). The Fermentation of Antarctic Krill Juice by a Variety of Microorganisms. Journal of Aquatic Food Product Technology, 24(8), 824-831.
Kim, S.-Y., Je, J.-Y., & Kim, S.-K. (2007). Purification and characterization of antioxidant peptide from hoki (Johnius belengerii) frame protein by gastrointestinal digestion. The Journal of Nutritional Biochemistry, 18(1), 31-38.
Kirk, O., Borchert, T. V., & Fuglsang, C. C. (2002). Industrial enzyme applications. Current Opinion in Biotechnology, 13(4), 345-351.
Knorr, D. (1991). Recovery and utilization of chitin and chitosan in food processing waste management. Food Technology, 45(1), 114-122.
Kong, X., Guo, M., Hua, Y., Cao, D., & Zhang, C. (2008). Enzymatic preparation of immunomodulating hydrolysates from soy proteins. Bioresource Technology, 99(18), 8873-8879.
Krichen, F., Sila, A., Caron, J., Kobbi, S., Nedjar, N., Miled, N., Blecker, C., Besbes, S., & Bougatef, A. (2018). Identification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste. Engineering in Life Sciences, 18(9), 682-691.
Latorres, J., Rios, D., Saggiomo, G., Wasielesky, W., & Prentice-Hernandez, C. (2018). Functional and antioxidant properties of protein hydrolysates obtained from white shrimp (Litopenaeus vannamei). Journal of Food Science Technology, 55(2), 721-729.
Lee, J. K., Jeon, J.-K., & Byun, H.-G. (2014). Antihypertensive effect of novel angiotensin I converting enzyme inhibitory peptide from chum salmon (Oncorhynchus keta) skin in spontaneously hypertensive rats. Journal of Functional Foods, 7, 381-389.
Lehman, W., Orzechowski, M., Li, X. E., Fischer, S., & Raunser, S. (2013). Gestalt-binding of tropomyosin on actin during thin filament activation. Journal of Muscle Research and Cell Motility, 34(3-4), 155-163.
Li, C., Haug, T., Styrvold, O. B., Jørgensen, T. Ø., & Stensvåg, K. (2008). Strongylocins, novel antimicrobial peptides from the green sea urchin, Strongylocentrotus droebachiensis. Developmental Comparative Immunology, 32(12), 1430-1440.
Lin, H.-C., Alashi, A. M., Aluko, R. E., Sun Pan, B., & Chang, Y.-W. (2017). Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates. Food & Nutrition Research, 61(1), 1391666.
Lin, Y.-H., Chen, G.-W., Yeh, C. H., Song, H., & Tsai, J.-S. (2018). Purification and identification of angiotensin I-converting enzyme inhibitory peptides and the antihypertensive effect of Chlorella sorokiniana protein hydrolysates. Nutrients, 10(10), 1397.
Linder, M., Fanni, J., Parmentier, M., Sergent, M., & Phan-tan-luu, R. (1995). Protein recovery from veal bones by enzymatic hydrolysis. Food Science, 60(5), 949-952.
Liu, Dong, S., Xu, J., Zeng, M., Song, H., & Zhao, Y. (2008). Production of cysteine-rich antimicrobial peptide by digestion of oyster (Crassostrea gigas) with alcalase and bromelin. Food Control, 19(3), 231-235.
Mao, X., Guo, N., Sun, J., & Xue, C. (2017). Comprehensive utilization of shrimp waste based on biotechnological methods: A review. Cleaner Production, 143, 814-823.
Miki, W. (1991). Biological functions and activities of animal carotenoids. Pure Applied Chemistry, 63(1), 141-146.
Mizani, M., Aminlari, M., & Khodabandeh, M. (2005). An effective method for producing a nutritive protein extract powder from shrimp-head waste. Food Science Technology International, 11(1), 49-54.
Moore, E. K., Harvey, H. R., Faux, J. F., Goodlett, D. R., & Nunn, B. L. (2014). Electrophoretic extraction and proteomic characterization of proteins buried in marine sediments. Chromatography, 1(4), 176-193.
Murray, B., & FitzGerald, R. (2007). Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Current Pharmaceutical Design, 13(8), 773-791.
Najafian, L., & Babji, A. S. (2012). A review of fish-derived antioxidant and antimicrobial peptides: their production, assessment, and applications. Peptides, 33(1), 178-185.
Ni, H., Li, L., Liu, G., & Hu, S.-Q. (2012). Inhibition mechanism and model of an angiotensin I-converting enzyme (ACE)-inhibitory hexapeptide from yeast (Saccharomyces cerevisiae). PloS One, 7(5).
Normah, I., & Anati, N. J. (2015). Characteristics of threadfin bream (Nemipterus japonicas) hydrolysate produced using bilimbi (Averrhoa bilimbi L.) protease and alcalase. International Food Research Journal, 22(6), 2259.
Ornum, J. (1992). Shrimp waste-must it be wasted. Infofish International, 6(92), 48-52.
Pujiastuti, D. Y., Amin, G., Nur, M., Alamsjah, M. A., & Hsu, J.-L. (2019). Marine organisms as potential sources of bioactive peptides that inhibit the activity of angiotensin I converting enzyme: A Review. Molecules, 24(14), 2541.
Quan, C., & Turner, C. (2009). Extraction of astaxanthin from shrimp waste using pressurized hot ethanol. Chromatographia, 70(1-2), 247-251.
Robert, M., Zatylny-Gaudin, C., Fournier, V., Corre, E., Le Corguillé, G., Bernay, B., & Henry, J. (2015). Molecular characterization of peptide fractions of a Tilapia (Oreochromis niloticus) by-product hydrolysate and in vitro evaluation of antibacterial activity. Process Biochemistry, 50(3), 487-492.
Roffman, D. S. (2004). High-versus low-dose ACE inhibitor therapy in chronic heart failure. Annals of Pharmacotherapy, 38(5), 831-838.
Sachindra, Bhaskar, N., & Mahendrakar, N. (2005). Carotenoids in different body components of Indian shrimps. Journal of the Science of Food Agriculture, 85(1), 167-172.
Sachindra, Bhaskar, N., & Mahendrakar, N. (2006). Recovery of carotenoids from shrimp waste in organic solvents. Waste Management, 26(10), 1092-1098.
Shahidi, F., & Synowiecki, J. (1991). Isolation and characterization of nutrients and value-added products from snow crab (Chionoecetes opilio) and shrimp (Pandalus borealis) processing discards. Journal of Agricultural and Food Chemistry, 39(8), 1527-1532.
Smid, E. J., & Lacroix, C. (2013). Microbe–microbe Interactions in Mixed Culture Food Fermentations. Current Opinion in Biotechnology, 24(2), 148-154.
Souissi, N., Bougatef, A., Triki-Ellouz, Y., & Nasri, M. (2007). Biochemical and functional properties of sardinella (Sardinella aurita) by-product hydrolysates. Food Technology and Biotechnology, 45(2), 187-194.
Srinivasan, D., Mechkarska, M., Abdel-Wahab, Y. H., Flatt, P. R., & Conlon, J. M. (2013). Caerulein precursor fragment (CPF) peptides from the skin secretions of Xenopus laevis and Silurana epitropicalis are potent insulin-releasing agents. Biochimie, 95(2), 429-435.
Steiner, H., Hultmark, D., Engström, Å., Bennich, H., & Boman, H. G. (1981). Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature, 292(5820), 246-248.
Stensvåg, K., Haug, T., Sperstad, S. V., Rekdal, Ø., Indrevoll, B., & Styrvold, O. B. (2008). Arasin 1, a proline–arginine-rich antimicrobial peptide isolated from the spider crab, Hyas araneus. Developmental Comparative Immunology, 32(3), 275-285.
Synowiecki, J., & Al-Khateeb, N. A. A. Q. (2000). The recovery of protein hydrolysate during enzymatic isolation of chitin from shrimp crangon processing discards. Food Chemistry, 68(2), 147-152.
Thiede, B., Höhenwarter, W., Krah, A., Mattow, J., Schmid, M., Schmidt, F., & Jungblut, P. R. (2005). Peptide mass fingerprinting. Methods, 35(3), 237-247.
Tzeng, T.-D. (2007). Population structure of the sword prawn (Parapenaeopsis hardwickii) in the east china sea and waters adjacent to Taiwan inferred from the mitochondrial control region. Zoological Studies, 46(5), 561-568.
Udenigwe, C. C. (2016). Towards rice bran protein utilization: In silico insight on the role of oryzacystatins in biologically-active peptide production. Food Chemistry, 191, 135-138.
Vilailak, K., Soottawat, B., Duangporn, K., & Fereidoon, S. (2007). Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chemistry, 102(4), 1317-1327.
Volpe, M., Battistoni, A., Chin, D., Rubattu, S., & Tocci, G. (2012). Renin as a biomarker of cardiovascular disease in clinical practice. Nutrition, Metabolism Cardiovascular Diseases, 22(4), 312-317.
Wald, M., Schwarz, K., Rehbein, H., Bußmann, B., & Beermann, C. (2016). Detection of antibacterial activity of an enzymatic hydrolysate generated by processing rainbow trout by-products with trout pepsin. Food Chemistry, 205, 221-228.
Wijesekara, I., & Kim, S.-K. (2010). Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: Prospects in the pharmaceutical industry. Marine Drugs, 8(4), 1080-1093.
Wilson, J., Hayes, M., & Carney, B. (2011). Angiotensin-I-converting enzyme and prolyl endopeptidase inhibitory peptides from natural sources with a focus on marine processing by-products. Food Chemistry, 129(2), 235-244.
Yu, C.-J., Lin, Y.-F., Chiang, B.-L., & Chow, L.-P. (2003). Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2. The Journal of Immunology, 170(1), 445-453.
Yu, Z., Yin, Y., Zhao, W., Liu, J., & Chen, F. (2012). Anti-diabetic activity peptides from albumin against α-glucosidase and α-amylase. Food Chemistry, 135(3), 2078-2085.
Zambrowicz, A., Eckert, E., Pokora, M., Bobak, Ł., Dąbrowska, A., Szołtysik, M., Trziszka, T., & Chrzanowska, J. (2015). Antioxidant and antidiabetic activities of peptides isolated from a hydrolysate of an egg-yolk protein by-product prepared with a proteinase from Asian pumpkin (Cucurbita ficifolia). RSC Advances, 5(14), 10460-10467.
Zhao, K., Luo, G., Giannelli, S., & Szeto, H. H. (2005). Mitochondria-targeted peptide prevents mitochondrial depolarization and apoptosis induced by tert-butyl hydroperoxide in neuronal cell lines. Biochemical Pharmacology, 70(12), 1796-1806.