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Volumn 4, Issue 1, 2012, Pages 6-24

Bioactive peptides from marine processing waste and shellfish: A review

Author keywords

Amino acids; Bioactive molecules; Functional foods; Marine organisms; Peptides; Proteins

Indexed keywords

CRUSTACEA; MOLLUSCA;

EID: 84857689220     PISSN: 17564646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jff.2011.09.001     Document Type: Review
Times cited : (545)

References (188)
  • 1
    • 35649028748 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization and recombinant expression of a crustin-like antimicrobial peptide from black tiger shrimp Penaeus monodon
    • Amparyup P., Kondo H., Hirono I., Aoki T., Tassanakajon A. Molecular cloning, genomic organization and recombinant expression of a crustin-like antimicrobial peptide from black tiger shrimp Penaeus monodon. Molecular Immunology 2008, 45:1085-1093.
    • (2008) Molecular Immunology , vol.45 , pp. 1085-1093
    • Amparyup, P.1    Kondo, H.2    Hirono, I.3    Aoki, T.4    Tassanakajon, A.5
  • 2
    • 0036232442 scopus 로고    scopus 로고
    • Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini
    • Anderson W.G., Ali M.F., Einarsdóttir I.E., Schäffer L., Hazon N., Conlon J.M. Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini. General and Comparative Endocrinology 2002, 126:113-122.
    • (2002) General and Comparative Endocrinology , vol.126 , pp. 113-122
    • Anderson, W.G.1    Ali, M.F.2    Einarsdóttir, I.E.3    Schäffer, L.4    Hazon, N.5    Conlon, J.M.6
  • 3
    • 73049083337 scopus 로고    scopus 로고
    • Molecular characterization of a crustin-like, putative antimicrobial peptide, Fi-crustin, from the Indian white shrimp, Fenneropenaeus indicus
    • Antony S.P., Bright Singh I.S., Philip R. Molecular characterization of a crustin-like, putative antimicrobial peptide, Fi-crustin, from the Indian white shrimp, Fenneropenaeus indicus. Fish & Shellfish Immunology 2010, 28:216-220.
    • (2010) Fish & Shellfish Immunology , vol.28 , pp. 216-220
    • Antony, S.P.1    Bright Singh, I.S.2    Philip, R.3
  • 4
    • 0036071479 scopus 로고    scopus 로고
    • Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus
    • Bartlett T.C., Cuthbertson B.J., Shepard E.F., Chapman R.W., Gross P.S., Warr G.W. Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus. Marine Biotechnology 2002, 4:278-293.
    • (2002) Marine Biotechnology , vol.4 , pp. 278-293
    • Bartlett, T.C.1    Cuthbertson, B.J.2    Shepard, E.F.3    Chapman, R.W.4    Gross, P.S.5    Warr, G.W.6
  • 5
    • 44749083354 scopus 로고    scopus 로고
    • Isolation and characterisation of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus
    • Battison A.L., Summerfield R., Patrzykat A. Isolation and characterisation of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus. Fish & Shellfish Immunology 2008, 25:181-187.
    • (2008) Fish & Shellfish Immunology , vol.25 , pp. 181-187
    • Battison, A.L.1    Summerfield, R.2    Patrzykat, A.3
  • 7
    • 34249339959 scopus 로고    scopus 로고
    • New anticoagulants
    • Bauer A.K. New anticoagulants. Hematology 2006, 1:450-460.
    • (2006) Hematology , vol.1 , pp. 450-460
    • Bauer, A.K.1
  • 8
    • 33751286330 scopus 로고    scopus 로고
    • Fish, wales, crustaceans, mollusks
    • Springer, Berlin, Heidelberg,
    • Belitz H.D., Grosch W., Schieberle P. Fish, wales, crustaceans, mollusks. Food chemistry 2004, Springer, Berlin, Heidelberg, (pp. 619-642).
    • (2004) Food chemistry , pp. 619-642
    • Belitz, H.D.1    Grosch, W.2    Schieberle, P.3
  • 9
    • 62549143935 scopus 로고    scopus 로고
    • Effects of flavourzyme on yield and some biological activities of Mungoong, an extract paste from the cephalothorax of white shrimp
    • Benjakul S., Binsan W., Visessanguan W., Osako K., Tanaka M. Effects of flavourzyme on yield and some biological activities of Mungoong, an extract paste from the cephalothorax of white shrimp. Journal of Food Science 2009, 74:S73-80.
    • (2009) Journal of Food Science , vol.74
    • Benjakul, S.1    Binsan, W.2    Visessanguan, W.3    Osako, K.4    Tanaka, M.5
  • 10
    • 67349249429 scopus 로고    scopus 로고
    • Characteristics of gelatin from the skins of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus
    • Benjakul S., Oungbho K., Visessanguan W., Thiansilakul Y., Roytrakul S. Characteristics of gelatin from the skins of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus. Food Chemistry 2009, 116:445-451.
    • (2009) Food Chemistry , vol.116 , pp. 445-451
    • Benjakul, S.1    Oungbho, K.2    Visessanguan, W.3    Thiansilakul, Y.4    Roytrakul, S.5
  • 13
    • 41949114268 scopus 로고    scopus 로고
    • Crustin expression following bacterial injection and temperature change in the shore crab Carcinus maenas
    • Brockton V., Smith V.J. Crustin expression following bacterial injection and temperature change in the shore crab Carcinus maenas. Developmental and Comparative Immunology 2008, 32:1027-1033.
    • (2008) Developmental and Comparative Immunology , vol.32 , pp. 1027-1033
    • Brockton, V.1    Smith, V.J.2
  • 14
    • 0034951098 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin
    • Byun H.G., Kim S.K. Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin. Process Biochemistry 2001, 36:1155-1162.
    • (2001) Process Biochemistry , vol.36 , pp. 1155-1162
    • Byun, H.G.1    Kim, S.K.2
  • 16
    • 0029810861 scopus 로고    scopus 로고
    • Innate immunity: Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis
    • Charlet M., Chernysh S., Philippe H., Hetru C., Hoffmann J.A., Bulet P. Innate immunity: Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis. The Journal of Biological Chemistry 1996, 271:21808-21813.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 21808-21813
    • Charlet, M.1    Chernysh, S.2    Philippe, H.3    Hetru, C.4    Hoffmann, J.A.5    Bulet, P.6
  • 17
    • 0030957967 scopus 로고    scopus 로고
    • Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder
    • Cole A.M., Weis P., Diamond G. Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. The Journal of Biological Chemistry 1997, 272:12008-12013.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 12008-12013
    • Cole, A.M.1    Weis, P.2    Diamond, G.3
  • 18
    • 84857687994 scopus 로고
    • Treatment of astheno-depressive conditions by Minaprine-Multi-center study of 248 cases assessed by Fatigue Study Group Scale #4
    • Crocq L., Bugard P., Viaud P. Treatment of astheno-depressive conditions by Minaprine-Multi-center study of 248 cases assessed by Fatigue Study Group Scale #4. Psychologie Medicale 1980, 12:643-661.
    • (1980) Psychologie Medicale , vol.12 , pp. 643-661
    • Crocq, L.1    Bugard, P.2    Viaud, P.3
  • 19
    • 46949088271 scopus 로고    scopus 로고
    • Peptides from fish and crustacean by-products hydrolysates stimulate cholecystokinin release in STC-1 cells
    • Cudennec B., Ravallec-Plé R., Courois E., Fouchereau-Peron M. Peptides from fish and crustacean by-products hydrolysates stimulate cholecystokinin release in STC-1 cells. Food Chemistry 2008, 111:970-975.
    • (2008) Food Chemistry , vol.111 , pp. 970-975
    • Cudennec, B.1    Ravallec-Plé, R.2    Courois, E.3    Fouchereau-Peron, M.4
  • 20
    • 0036380652 scopus 로고    scopus 로고
    • Diversity of the penaeidin antimicrobial peptides in two shrimp species
    • Cuthbertson B.J., Shepard E.F., Chapman R.W., Gross P.S. Diversity of the penaeidin antimicrobial peptides in two shrimp species. Immunogenetics 2002, 54:442-445.
    • (2002) Immunogenetics , vol.54 , pp. 442-445
    • Cuthbertson, B.J.1    Shepard, E.F.2    Chapman, R.W.3    Gross, P.S.4
  • 21
    • 4444238114 scopus 로고    scopus 로고
    • Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis
    • Dávalos A., Miguel M., Bartolomé B., López-Fandiño R. Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis. Journal of Food Protection 2004, 67:1939-1944.
    • (2004) Journal of Food Protection , vol.67 , pp. 1939-1944
    • Dávalos, A.1    Miguel, M.2    Bartolomé, B.3    López-Fandiño, R.4
  • 22
  • 25
    • 0035861645 scopus 로고    scopus 로고
    • Crustacean immunity. Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge
    • Destoumieux-Garzón D., Saulnier D., Garnier J., Jouffrey C., Bulet P., Bachère E. Crustacean immunity. Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge. The Journal of Biological Chemistry 2001, 276:47070-47077.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 47070-47077
    • Destoumieux-Garzón, D.1    Saulnier, D.2    Garnier, J.3    Jouffrey, C.4    Bulet, P.5    Bachère, E.6
  • 27
    • 85078389689 scopus 로고    scopus 로고
    • Scientific opinion on the safety of 'sardine peptide product' as a novel food ingredient
    • EFSA Panel on Dietetic Products, Nutrition and Allergies
    • EFSA Panel on Dietetic Products, Nutrition and Allergies Scientific opinion on the safety of 'sardine peptide product' as a novel food ingredient. EFSA Journal 2010, 8:1684-1700.
    • (2010) EFSA Journal , vol.8 , pp. 1684-1700
  • 28
    • 19544388839 scopus 로고    scopus 로고
    • Symptom reduction in irritable bowel syndrome with pre-digested fish protein supplement
    • Englender C. Symptom reduction in irritable bowel syndrome with pre-digested fish protein supplement. Townsend Letter 2000, 205(206):60-64.
    • (2000) Townsend Letter , vol.205 , Issue.206 , pp. 60-64
    • Englender, C.1
  • 29
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    • Erdmann K., Cheung B.W.Y., Schröder H. The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. The Journal of Nutritional Biochemistry 2008, 19:643-654.
    • (2008) The Journal of Nutritional Biochemistry , vol.19 , pp. 643-654
    • Erdmann, K.1    Cheung, B.W.Y.2    Schröder, H.3
  • 30
    • 33746603552 scopus 로고    scopus 로고
    • The ACE inhibitory dipeptide Met-Tyr diminishes free radical formation in human endothelial cells via induction of heme oxygenase-1 and ferritin
    • Erdmann K., Grosser N., Schipporeit K., Schröder H. The ACE inhibitory dipeptide Met-Tyr diminishes free radical formation in human endothelial cells via induction of heme oxygenase-1 and ferritin. The Journal of Nutrition 2006, 136:2148-2152.
    • (2006) The Journal of Nutrition , vol.136 , pp. 2148-2152
    • Erdmann, K.1    Grosser, N.2    Schipporeit, K.3    Schröder, H.4
  • 31
    • 2542580915 scopus 로고    scopus 로고
    • Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales
    • Fahmi A., Morimura S., Guo H.C., Shigematsu T., Kida K., Uemura Y. Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales. Process Biochemistry 2004, 39:1195-1200.
    • (2004) Process Biochemistry , vol.39 , pp. 1195-1200
    • Fahmi, A.1    Morimura, S.2    Guo, H.C.3    Shigematsu, T.4    Kida, K.5    Uemura, Y.6
  • 32
    • 70349798625 scopus 로고    scopus 로고
    • Chemical composition and antioxidative activity of Thai traditional fermented shrimp and krill products
    • Faithong N., Benjakul S., Phatcharat S., Binsan W. Chemical composition and antioxidative activity of Thai traditional fermented shrimp and krill products. Food Chemistry 2010, 119:133-140.
    • (2010) Food Chemistry , vol.119 , pp. 133-140
    • Faithong, N.1    Benjakul, S.2    Phatcharat, S.3    Binsan, W.4
  • 33
    • 84857686635 scopus 로고    scopus 로고
    • FAO.. The state of world fisheries and aquaculture 2008. Rome: Food and Agriculture Organization of the United Nations.
    • FAO. (2009). The state of world fisheries and aquaculture 2008. Rome: Food and Agriculture Organization of the United Nations. http://www.fao.org.
    • (2009)
  • 37
    • 0014947216 scopus 로고
    • Gamma-aminobutyric acid (GABA) in fish erythrocytes
    • Fugelli K. Gamma-aminobutyric acid (GABA) in fish erythrocytes. Cellular and Molecular Life Sciences 1970, 26:361.
    • (1970) Cellular and Molecular Life Sciences , vol.26 , pp. 361
    • Fugelli, K.1
  • 38
    • 0034814575 scopus 로고    scopus 로고
    • Effects of an ace-inhibitory agent, katsuobushi oligopeptide, in the spontaneously hypertensive rat and in borderline and mildly hypertensive subjects
    • Fujita H., Yamagami T., Ohshima K. Effects of an ace-inhibitory agent, katsuobushi oligopeptide, in the spontaneously hypertensive rat and in borderline and mildly hypertensive subjects. Nutrition Research 2001, 21:1149-1158.
    • (2001) Nutrition Research , vol.21 , pp. 1149-1158
    • Fujita, H.1    Yamagami, T.2    Ohshima, K.3
  • 39
    • 70349900829 scopus 로고    scopus 로고
    • Marine-derived protein hydrolysates, their biological activities and potential as functional food ingredients: ACE-inhibitory peptides derived from bonito
    • CRC Press, Boca Raton, FL, C. Barrow, F. Shahidi (Eds.)
    • Fujita N., Yoshikawa M. Marine-derived protein hydrolysates, their biological activities and potential as functional food ingredients: ACE-inhibitory peptides derived from bonito. Marine nutraceuticals and functional foods 2008, 247-258. CRC Press, Boca Raton, FL. C. Barrow, F. Shahidi (Eds.).
    • (2008) Marine nutraceuticals and functional foods , pp. 247-258
    • Fujita, N.1    Yoshikawa, M.2
  • 40
    • 59849113425 scopus 로고    scopus 로고
    • Antioxidant and functional properties of gelatin hydrolysates obtained from skin of sole and squid
    • Giménez B., Alemán A., Montero P., Gómez-Guillén M.C. Antioxidant and functional properties of gelatin hydrolysates obtained from skin of sole and squid. Food Chemistry 2009, 114:976-983.
    • (2009) Food Chemistry , vol.114 , pp. 976-983
    • Giménez, B.1    Alemán, A.2    Montero, P.3    Gómez-Guillén, M.C.4
  • 41
    • 40649111368 scopus 로고    scopus 로고
    • Current concepts: Renin inhibition in the treatment of hypertension
    • Gradman A.H., Pinto R., Kad R. Current concepts: Renin inhibition in the treatment of hypertension. Current Opinion in Pharmacology 2008, 8:120-126.
    • (2008) Current Opinion in Pharmacology , vol.8 , pp. 120-126
    • Gradman, A.H.1    Pinto, R.2    Kad, R.3
  • 42
    • 0022474854 scopus 로고
    • Effect of peptide chain length on amino acid and nitrogen absorption from two lactalbumin hydrolysates in the normal human jejunum
    • Grimble G.K., Keohane P.P., Higgins B.E., Kaminski M.V., Silk D.B. Effect of peptide chain length on amino acid and nitrogen absorption from two lactalbumin hydrolysates in the normal human jejunum. Clinical Science 1986, 71:65-69.
    • (1986) Clinical Science , vol.71 , pp. 65-69
    • Grimble, G.K.1    Keohane, P.P.2    Higgins, B.E.3    Kaminski, M.V.4    Silk, D.B.5
  • 44
    • 33750728894 scopus 로고    scopus 로고
    • Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis
    • Hai-Lun H., Xiu-La C., Cai-Yun S., Yu-Zhong Z., Bai-Cheng Z. Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis. Journal of Peptide Science 2006, 12:726-733.
    • (2006) Journal of Peptide Science , vol.12 , pp. 726-733
    • Hai-Lun, H.1    Xiu-La, C.2    Cai-Yun, S.3    Yu-Zhong, Z.4    Bai-Cheng, Z.5
  • 45
    • 79953294692 scopus 로고    scopus 로고
    • Bioactive proteins, peptides and amino acids from macroalgae
    • Harnedy P.A., Fitzgerald R.J. Bioactive proteins, peptides and amino acids from macroalgae. Journal of Phycology 2011, 47:218-232.
    • (2011) Journal of Phycology , vol.47 , pp. 218-232
    • Harnedy, P.A.1    Fitzgerald, R.J.2
  • 46
    • 33644829821 scopus 로고    scopus 로고
    • Cloning of a crustin-like, single whey-acidic-domain, antibacterial peptide from the haemocytes of the European lobster, Homarus gammarus, and its response to infection with bacteria
    • Hauton C., Brockton V., Smith V.J. Cloning of a crustin-like, single whey-acidic-domain, antibacterial peptide from the haemocytes of the European lobster, Homarus gammarus, and its response to infection with bacteria. Molecular Immunology 2006, 43:1490-1496.
    • (2006) Molecular Immunology , vol.43 , pp. 1490-1496
    • Hauton, C.1    Brockton, V.2    Smith, V.J.3
  • 47
    • 67349162521 scopus 로고    scopus 로고
    • Development of antioxidant rich peptides from milk protein by microbial proteases and analysis of their effects on lipid peroxidation in cooked beef
    • Hogan S., Zhang L., Li J., Wang H., Zhou K. Development of antioxidant rich peptides from milk protein by microbial proteases and analysis of their effects on lipid peroxidation in cooked beef. Food Chemistry 2009, 117:438-443.
    • (2009) Food Chemistry , vol.117 , pp. 438-443
    • Hogan, S.1    Zhang, L.2    Li, J.3    Wang, H.4    Zhou, K.5
  • 48
    • 23944499810 scopus 로고    scopus 로고
    • Nutraceuticals, vitamins, antioxidants, and minerals in the prevention and treatment of hypertension
    • Houston M.C. Nutraceuticals, vitamins, antioxidants, and minerals in the prevention and treatment of hypertension. Progress in Cardiovascular Diseases 2005, 47:396-449.
    • (2005) Progress in Cardiovascular Diseases , vol.47 , pp. 396-449
    • Houston, M.C.1
  • 49
    • 0029842737 scopus 로고    scopus 로고
    • A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis)
    • Hubert F., Noel T., Roch P. A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis). European Journal of Biochemistry 1996, 240:302-306.
    • (1996) European Journal of Biochemistry , vol.240 , pp. 302-306
    • Hubert, F.1    Noel, T.2    Roch, P.3
  • 51
    • 0022506916 scopus 로고
    • Relationship between dietary proteins, their in vitro digestion products, and serum cholesterol in rats
    • Jacques H., Deshaies Y., Savoie L. Relationship between dietary proteins, their in vitro digestion products, and serum cholesterol in rats. Atherosclerosis 1986, 61:89-98.
    • (1986) Atherosclerosis , vol.61 , pp. 89-98
    • Jacques, H.1    Deshaies, Y.2    Savoie, L.3
  • 52
    • 22644441738 scopus 로고    scopus 로고
    • Preparation and antioxidative activity of hoki frame protein hydrolysate using ultrafiltration membranes
    • Je J.Y., Kim S.Y., Kim S.K. Preparation and antioxidative activity of hoki frame protein hydrolysate using ultrafiltration membranes. European Food Research and Technology 2005, 221:157-162.
    • (2005) European Food Research and Technology , vol.221 , pp. 157-162
    • Je, J.Y.1    Kim, S.Y.2    Kim, S.K.3
  • 53
    • 20544449674 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme (ACE) inhibitory peptide derived from the sauce of fermented blue mussel, Mytilus edulis
    • Je J.Y., Park P.J., Byun H.G., Jung W.K., Kim S.K. Angiotensin I converting enzyme (ACE) inhibitory peptide derived from the sauce of fermented blue mussel, Mytilus edulis. Bioresource Technology 2005, 96:1624-1629.
    • (2005) Bioresource Technology , vol.96 , pp. 1624-1629
    • Je, J.Y.1    Park, P.J.2    Byun, H.G.3    Jung, W.K.4    Kim, S.K.5
  • 54
    • 7044274319 scopus 로고    scopus 로고
    • Isolation of angiotensin I converting enzyme (ACE) inhibitor from fermented oyster sauce, Crassostrea gigas
    • Je J.Y., Park J.Y., Jung W.K., Park P.J., Kim S.K. Isolation of angiotensin I converting enzyme (ACE) inhibitor from fermented oyster sauce, Crassostrea gigas. Food Chemistry 2005, 90:809-814.
    • (2005) Food Chemistry , vol.90 , pp. 809-814
    • Je, J.Y.1    Park, J.Y.2    Jung, W.K.3    Park, P.J.4    Kim, S.K.5
  • 55
    • 7444222906 scopus 로고    scopus 로고
    • Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate
    • Je J.Y., Park P.J., Kim S.K. Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Research International 2005, 38:45-50.
    • (2005) Food Research International , vol.38 , pp. 45-50
    • Je, J.Y.1    Park, P.J.2    Kim, S.K.3
  • 56
    • 11144233214 scopus 로고    scopus 로고
    • A novel angiotensin I converting enzyme inhibitory peptide from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate
    • Je J.Y., Park P.J., Kwon J.Y., Kim S.K. A novel angiotensin I converting enzyme inhibitory peptide from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Journal of Agricultural and Food Chemistry 2004, 52:7842-7845.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 7842-7845
    • Je, J.Y.1    Park, P.J.2    Kwon, J.Y.3    Kim, S.K.4
  • 57
    • 34047153515 scopus 로고    scopus 로고
    • Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis
    • Je J.Y., Qian Z.J., Byun H.G., Kim S.K. Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis. Process Biochemistry 2007, 42:840-846.
    • (2007) Process Biochemistry , vol.42 , pp. 840-846
    • Je, J.Y.1    Qian, Z.J.2    Byun, H.G.3    Kim, S.K.4
  • 58
    • 0032727216 scopus 로고    scopus 로고
    • Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes
    • Jeon Y.J., Byun H.G., Kim S.K. Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes. Process Biochemistry 1999, 35:471-478.
    • (1999) Process Biochemistry , vol.35 , pp. 471-478
    • Jeon, Y.J.1    Byun, H.G.2    Kim, S.K.3
  • 60
    • 7444234213 scopus 로고    scopus 로고
    • Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein
    • Jun S.Y., Park P.J., Jung W.K., Kim S.K. Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. European Food Research and Technology 2004, 219:20-26.
    • (2004) European Food Research and Technology , vol.219 , pp. 20-26
    • Jun, S.Y.1    Park, P.J.2    Jung, W.K.3    Kim, S.K.4
  • 62
    • 33746380547 scopus 로고    scopus 로고
    • Recovery of a novel Ca-binding peptide from Alaska pollack (Theragra chalcogramma) backbone by pepsinolytic hydrolysis
    • Jung W.K., Karawita R., Heo S.J., Lee B.J., Kim S.K., Jeon Y.J. Recovery of a novel Ca-binding peptide from Alaska pollack (Theragra chalcogramma) backbone by pepsinolytic hydrolysis. Process Biochemistry 2006, 41:2097-2100.
    • (2006) Process Biochemistry , vol.41 , pp. 2097-2100
    • Jung, W.K.1    Karawita, R.2    Heo, S.J.3    Lee, B.J.4    Kim, S.K.5    Jeon, Y.J.6
  • 63
    • 33847757801 scopus 로고    scopus 로고
    • Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame
    • Jung W.K., Kim S.K. Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame. European Food Research and Technology 2007, 224:763-767.
    • (2007) European Food Research and Technology , vol.224 , pp. 763-767
    • Jung, W.K.1    Kim, S.K.2
  • 64
    • 67649336586 scopus 로고    scopus 로고
    • Isolation and characterisation of an anticoagulant oligopeptide from blue mussel, Mytilus edulis
    • Jung W.K., Kim S.K. Isolation and characterisation of an anticoagulant oligopeptide from blue mussel, Mytilus edulis. Food Chemistry 2009, 117:687-692.
    • (2009) Food Chemistry , vol.117 , pp. 687-692
    • Jung, W.K.1    Kim, S.K.2
  • 65
    • 32844454569 scopus 로고    scopus 로고
    • Fish-bone peptide increases calcium solubility and bioavailability in ovariectomised rats
    • Jung W.K., Lee B.J., Kim S.K. Fish-bone peptide increases calcium solubility and bioavailability in ovariectomised rats. British Journal of Nutrition 2006, 95:124-128.
    • (2006) British Journal of Nutrition , vol.95 , pp. 124-128
    • Jung, W.K.1    Lee, B.J.2    Kim, S.K.3
  • 66
    • 21544467786 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats
    • Jung W.K., Mendis E., Je J.Y., Park P.J., Son B.W., Kim H.C., Choi Y.K., Kim S.K. Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats. Food Chemistry 2005, 94:26-32.
    • (2005) Food Chemistry , vol.94 , pp. 26-32
    • Jung, W.K.1    Mendis, E.2    Je, J.Y.3    Park, P.J.4    Son, B.W.5    Kim, H.C.6    Choi, Y.K.7    Kim, S.K.8
  • 67
    • 10044280151 scopus 로고    scopus 로고
    • Preparation of hoki (Johnius belengerii) bone oligophosphopeptide with a high affinity to calcium by carnivorous intestine crude proteinase
    • Jung W.K., Park P.J., Byun H.G., Moon S.H., Kim S.K. Preparation of hoki (Johnius belengerii) bone oligophosphopeptide with a high affinity to calcium by carnivorous intestine crude proteinase. Food Chemistry 2005, 91:333-340.
    • (2005) Food Chemistry , vol.91 , pp. 333-340
    • Jung, W.K.1    Park, P.J.2    Byun, H.G.3    Moon, S.H.4    Kim, S.K.5
  • 68
    • 84996358779 scopus 로고
    • Effect of pH and metal ions on the fungicidal action of salmine sulfate
    • Kamal K., Motohiro T. Effect of pH and metal ions on the fungicidal action of salmine sulfate. Nippon Suisan Gakkaishi 1986, 52:1843-1846.
    • (1986) Nippon Suisan Gakkaishi , vol.52 , pp. 1843-1846
    • Kamal, K.1    Motohiro, T.2
  • 69
    • 0036241190 scopus 로고    scopus 로고
    • Calcitonin in osteoporosis
    • Kanis J.A. Calcitonin in osteoporosis. Bone 2002, 30:65-66.
    • (2002) Bone , vol.30 , pp. 65-66
    • Kanis, J.A.1
  • 70
    • 0742323058 scopus 로고    scopus 로고
    • Antihypertensive effect of alkaline protease hydrolysate of the pearl oyster Pinctada fucata martencii and separation and identification of angiotensin-I converting enzyme inhibitory peptides
    • Katano S., Oki T., Matsuo Y., Yoshihira K., Nara Y., Miki T., Matsui T., Matsumoto K. Antihypertensive effect of alkaline protease hydrolysate of the pearl oyster Pinctada fucata martencii and separation and identification of angiotensin-I converting enzyme inhibitory peptides. Nippon Suisan Gakkaishi 2003, 69:975-980.
    • (2003) Nippon Suisan Gakkaishi , vol.69 , pp. 975-980
    • Katano, S.1    Oki, T.2    Matsuo, Y.3    Yoshihira, K.4    Nara, Y.5    Miki, T.6    Matsui, T.7    Matsumoto, K.8
  • 72
    • 21144476007 scopus 로고
    • Physiologically active peptide motif in proteins-peptide inhibitors of ACE from the hydrolysates of antartic krill muscle protein
    • Kawamura Y., Takane T., Satake M., Sugimoto T. Physiologically active peptide motif in proteins-peptide inhibitors of ACE from the hydrolysates of antartic krill muscle protein. Japan Agricultural Research Quarterly 1992, 26:210-213.
    • (1992) Japan Agricultural Research Quarterly , vol.26 , pp. 210-213
    • Kawamura, Y.1    Takane, T.2    Satake, M.3    Sugimoto, T.4
  • 73
    • 0033839717 scopus 로고    scopus 로고
    • Antihypertensive effect of Valyl-Tyrosine, a short chain peptide derived from sardine muscle hydrolyzate, on mild hypertensive subjects
    • Kawasaki T., Seki E., Osajima K., Yoshida M., Asada K., Matsui T., Osajima Y. Antihypertensive effect of Valyl-Tyrosine, a short chain peptide derived from sardine muscle hydrolyzate, on mild hypertensive subjects. Journal of Human Hypertension 2000, 14:519-523.
    • (2000) Journal of Human Hypertension , vol.14 , pp. 519-523
    • Kawasaki, T.1    Seki, E.2    Osajima, K.3    Yoshida, M.4    Asada, K.5    Matsui, T.6    Osajima, Y.7
  • 75
    • 55749095189 scopus 로고    scopus 로고
    • Comparative study on the proteases from fish pyloric caeca and the use for production of gelatin hydrolysate with antioxidative activity
    • Khantaphant S., Benjakul S. Comparative study on the proteases from fish pyloric caeca and the use for production of gelatin hydrolysate with antioxidative activity. Comparative Biochemistry and Physiology. Part B, Biochemistry and Molecular Biology 2008, 151:410-419.
    • (2008) Comparative Biochemistry and Physiology. Part B, Biochemistry and Molecular Biology , vol.151 , pp. 410-419
    • Khantaphant, S.1    Benjakul, S.2
  • 76
    • 0032791277 scopus 로고    scopus 로고
    • Callinectin, an antibacterial peptide from blue crab, Callinectes sapidus, hemocytes
    • Khoo L., Robinette D.W., Noga E.J. Callinectin, an antibacterial peptide from blue crab, Callinectes sapidus, hemocytes. Marine Biotechnology 1999, 1:44-51.
    • (1999) Marine Biotechnology , vol.1 , pp. 44-51
    • Khoo, L.1    Robinette, D.W.2    Noga, E.J.3
  • 77
    • 34548258046 scopus 로고    scopus 로고
    • Purification and characterization of antioxidant peptide from hoki (Johnius belengerii) frame protein by gastrointestinal digestion
    • Kim S.Y., Je J.Y., Kim S.K. Purification and characterization of antioxidant peptide from hoki (Johnius belengerii) frame protein by gastrointestinal digestion. The Journal of Nutritional Biochemistry 2007, 18:31-38.
    • (2007) The Journal of Nutritional Biochemistry , vol.18 , pp. 31-38
    • Kim, S.Y.1    Je, J.Y.2    Kim, S.K.3
  • 79
    • 32544441439 scopus 로고    scopus 로고
    • Bioactive compounds from marine processing byproducts - A review
    • Kim S.K., Mendis E. Bioactive compounds from marine processing byproducts - A review. Food Research International 2006, 39:383-393.
    • (2006) Food Research International , vol.39 , pp. 383-393
    • Kim, S.K.1    Mendis, E.2
  • 80
    • 77957359509 scopus 로고    scopus 로고
    • Marine fisheries by-products as potential nutraceuticals: An overview
    • CRC Press, Boca Raton, FL, C. Barrow, F. Shahidi (Eds.)
    • Kim S.K., Mendis E., Shahidi F. Marine fisheries by-products as potential nutraceuticals: An overview. Marine nutraceuticals and functional foods 2008, 1-22. CRC Press, Boca Raton, FL. C. Barrow, F. Shahidi (Eds.).
    • (2008) Marine nutraceuticals and functional foods , pp. 1-22
    • Kim, S.K.1    Mendis, E.2    Shahidi, F.3
  • 81
    • 77349090649 scopus 로고    scopus 로고
    • Development and biological activities of marine-derived bioactive peptides: A review
    • Kim S.K., Wijesekara I. Development and biological activities of marine-derived bioactive peptides: A review. Journal of Functional Foods 2010, 2:1-9.
    • (2010) Journal of Functional Foods , vol.2 , pp. 1-9
    • Kim, S.K.1    Wijesekara, I.2
  • 82
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: Production and functionality
    • Korhonen H., Pihlanto A. Bioactive peptides: Production and functionality. International Dairy Journal 2006, 16:945-960.
    • (2006) International Dairy Journal , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 83
    • 51649125975 scopus 로고    scopus 로고
    • Functional and bioactive peptides from hydrolyzed aquatic food proteins
    • CRC Press, Boca Raton, FL, C. Barrow, F. Shahidi (Eds.)
    • Kristinsson H.G. Functional and bioactive peptides from hydrolyzed aquatic food proteins. Marine nutraceuticals and functional foods 2008, 229-246. CRC Press, Boca Raton, FL. C. Barrow, F. Shahidi (Eds.).
    • (2008) Marine nutraceuticals and functional foods , pp. 229-246
    • Kristinsson, H.G.1
  • 84
    • 0037409612 scopus 로고    scopus 로고
    • In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): Effects of cathepsins B, D and L
    • Ladrat C., Verrez-Bagnis V., Noël J., Fleurence J. In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): Effects of cathepsins B, D and L. Food Chemistry 2003, 81:517-525.
    • (2003) Food Chemistry , vol.81 , pp. 517-525
    • Ladrat, C.1    Verrez-Bagnis, V.2    Noël, J.3    Fleurence, J.4
  • 85
    • 34147145412 scopus 로고    scopus 로고
    • Losses of taurine, creatine, glycine and alanine from cod (Gadus morhua L.) fillet during processing
    • Larsen R., Stormo S.K., Dragnes B.T., Elvevoll E.O. Losses of taurine, creatine, glycine and alanine from cod (Gadus morhua L.) fillet during processing. Journal of Food Composition and Analysis 2007, 20:396-402.
    • (2007) Journal of Food Composition and Analysis , vol.20 , pp. 396-402
    • Larsen, R.1    Stormo, S.K.2    Dragnes, B.T.3    Elvevoll, E.O.4
  • 88
    • 0037424354 scopus 로고    scopus 로고
    • Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus
    • Lee S.Y., Lee B.L., Söderhäll K. Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus. The Journal of Biological Chemistry 2003, 278:7927-7933.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 7927-7933
    • Lee, S.Y.1    Lee, B.L.2    Söderhäll, K.3
  • 89
    • 0032583529 scopus 로고    scopus 로고
    • Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins
    • Lee T.G., Maruyama S. Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. Biochemical and Biophysical Research Communications 1998, 253:604-608.
    • (1998) Biochemical and Biophysical Research Communications , vol.253 , pp. 604-608
    • Lee, T.G.1    Maruyama, S.2
  • 90
    • 68349102047 scopus 로고    scopus 로고
    • A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats
    • Lee S.H., Qian Z.J., Kim S.K. A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats. Food Chemistry 2010, 118:96-102.
    • (2010) Food Chemistry , vol.118 , pp. 96-102
    • Lee, S.H.1    Qian, Z.J.2    Kim, S.K.3
  • 91
    • 0021050766 scopus 로고
    • Isolation of molluscan opioid peptides
    • Leung M., Stefano G.B. Isolation of molluscan opioid peptides. Life Sciences 1983, 33:77-80.
    • (1983) Life Sciences , vol.33 , pp. 77-80
    • Leung, M.1    Stefano, G.B.2
  • 92
    • 78149344550 scopus 로고    scopus 로고
    • Identification and inhibitory properties of multifunctional peptides from pea protein hydrolysate
    • Li H., Aluko R.E. Identification and inhibitory properties of multifunctional peptides from pea protein hydrolysate. Journal of Agricultural and Food Chemistry 2010, 58:11471-11476.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , pp. 11471-11476
    • Li, H.1    Aluko, R.E.2
  • 93
    • 33750617008 scopus 로고    scopus 로고
    • Radical scavenging properties of protein hydrolysates from jumbo flying squid (Dosidicus eschrichitii steenstrup) skin gelatin
    • Lin L., Li B.F. Radical scavenging properties of protein hydrolysates from jumbo flying squid (Dosidicus eschrichitii steenstrup) skin gelatin. Journal of the Science of Food and Agriculture 2006, 86:2290-2295.
    • (2006) Journal of the Science of Food and Agriculture , vol.86 , pp. 2290-2295
    • Lin, L.1    Li, B.F.2
  • 94
    • 35348887775 scopus 로고    scopus 로고
    • Production of cysteine-rich antimicrobial peptide by digestion of oyster (Crassostrea gigas) with alcalase and bromelin
    • Liu Z., Dong S., Xu J., Zeng M., Song H., Zhao Y. Production of cysteine-rich antimicrobial peptide by digestion of oyster (Crassostrea gigas) with alcalase and bromelin. Food Control 2008, 19:231-235.
    • (2008) Food Control , vol.19 , pp. 231-235
    • Liu, Z.1    Dong, S.2    Xu, J.3    Zeng, M.4    Song, H.5    Zhao, Y.6
  • 95
    • 33748416072 scopus 로고    scopus 로고
    • Antibacterial activity of peptides and folding variants from milk proteins
    • López Expósito I., Recio I. Antibacterial activity of peptides and folding variants from milk proteins. International Dairy Journal 2006, 16:1294-1305.
    • (2006) International Dairy Journal , vol.16 , pp. 1294-1305
    • López Expósito, I.1    Recio, I.2
  • 96
    • 33748297647 scopus 로고    scopus 로고
    • Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity
    • López-Fandiño R., Otte J., Van Camp J. Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. International Dairy Journal 2006, 16:1277-1293.
    • (2006) International Dairy Journal , vol.16 , pp. 1277-1293
    • López-Fandiño, R.1    Otte, J.2    Van Camp, J.3
  • 97
    • 0036877738 scopus 로고    scopus 로고
    • Taurine: a conditionally essential amino acid in humans? An overview in health and disease
    • Lourenço R., Camilo M.E. Taurine: a conditionally essential amino acid in humans? An overview in health and disease. Nutrición Hospitalaria 2002, 17:262-270.
    • (2002) Nutrición Hospitalaria , vol.17 , pp. 262-270
    • Lourenço, R.1    Camilo, M.E.2
  • 99
    • 0034005620 scopus 로고    scopus 로고
    • Novel marine-derived anticancer agents: A phase I clinical, pharmacological, and pharmacodynamic study of dolastatin 10 (NSC 376128) in patients with advanced solid tumors
    • Madden T., Tran H.T., Beck D., Huie R., Newman R.A., Pusztai L., Wright J.J., Abbruzzese J.L. Novel marine-derived anticancer agents: A phase I clinical, pharmacological, and pharmacodynamic study of dolastatin 10 (NSC 376128) in patients with advanced solid tumors. Clinical Cancer Research 2000, 6:1293-1301.
    • (2000) Clinical Cancer Research , vol.6 , pp. 1293-1301
    • Madden, T.1    Tran, H.T.2    Beck, D.3    Huie, R.4    Newman, R.A.5    Pusztai, L.6    Wright, J.J.7    Abbruzzese, J.L.8
  • 100
    • 77952875414 scopus 로고    scopus 로고
    • Extraction and characterization of chitin, chitosan, and protein hydrolysates prepared from shrimp waste by treatment with crude protease from Bacillus cereus SV1
    • Manni L., Ghorbel-Bellaaj O., Jellouli K., Younes I., Nasri M. Extraction and characterization of chitin, chitosan, and protein hydrolysates prepared from shrimp waste by treatment with crude protease from Bacillus cereus SV1. Applied Biochemistry and Biotechnology 2010, 162:345-357.
    • (2010) Applied Biochemistry and Biotechnology , vol.162 , pp. 345-357
    • Manni, L.1    Ghorbel-Bellaaj, O.2    Jellouli, K.3    Younes, I.4    Nasri, M.5
  • 101
    • 49849093907 scopus 로고    scopus 로고
    • Clinical trial: Protective effect of a commercial fish protein hydrolysate against indomethacin (NSAID)-induced small intestinal injury
    • Marchbank T., Limdi J.K., Mahmood A., Elia G., Playford R.J. Clinical trial: Protective effect of a commercial fish protein hydrolysate against indomethacin (NSAID)-induced small intestinal injury. Alimentary Pharmacology & Therapeutics 2008, 28:799-804.
    • (2008) Alimentary Pharmacology & Therapeutics , vol.28 , pp. 799-804
    • Marchbank, T.1    Limdi, J.K.2    Mahmood, A.3    Elia, G.4    Playford, R.J.5
  • 103
    • 0242361291 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin, a novel immune stimulant with promising anticancer activity in Barrett's esophageal adenocarcinoma
    • Mcfadden D.W., Riggs D.R., Jackson B.J., Vona-Davis L. Keyhole limpet hemocyanin, a novel immune stimulant with promising anticancer activity in Barrett's esophageal adenocarcinoma. The American Journal of Surgery 2003, 186:552-555.
    • (2003) The American Journal of Surgery , vol.186 , pp. 552-555
    • Mcfadden, D.W.1    Riggs, D.R.2    Jackson, B.J.3    Vona-Davis, L.4
  • 104
    • 16444386368 scopus 로고    scopus 로고
    • Multifunctional peptides encrypted in milk proteins
    • Meisel H. Multifunctional peptides encrypted in milk proteins. BioFactors 2004, 21:55-61.
    • (2004) BioFactors , vol.21 , pp. 55-61
    • Meisel, H.1
  • 106
    • 23744500077 scopus 로고    scopus 로고
    • Investigation of jumbo squid (Dosidicus gigas) skin gelatin peptides for their in vitro antioxidant effects
    • Mendis E., Rajapakse N., Byun H.G., Kim S.K. Investigation of jumbo squid (Dosidicus gigas) skin gelatin peptides for their in vitro antioxidant effects. Life Sciences 2005, 77:2166-2178.
    • (2005) Life Sciences , vol.77 , pp. 2166-2178
    • Mendis, E.1    Rajapakse, N.2    Byun, H.G.3    Kim, S.K.4
  • 107
    • 13244279441 scopus 로고    scopus 로고
    • Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate
    • Mendis E., Rajapakse N., Kim S.K. Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. Journal of Agricultural and Food Chemistry 2005, 53:581-587.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 581-587
    • Mendis, E.1    Rajapakse, N.2    Kim, S.K.3
  • 108
    • 33644595324 scopus 로고    scopus 로고
    • Physico-chemical and functional properties of myofibrillar proteins from different species of molluscs
    • Mignino L.A., Paredi M.E. Physico-chemical and functional properties of myofibrillar proteins from different species of molluscs. LWT-Food Science and Technology 2006, 39:35-42.
    • (2006) LWT-Food Science and Technology , vol.39 , pp. 35-42
    • Mignino, L.A.1    Paredi, M.E.2
  • 109
    • 0036453947 scopus 로고    scopus 로고
    • Treatment of hypertension with oral taurine: Experimental and clinical studies
    • Militante J.D., Lombardini J.B. Treatment of hypertension with oral taurine: Experimental and clinical studies. Amino Acids 2002, 23:381-393.
    • (2002) Amino Acids , vol.23 , pp. 381-393
    • Militante, J.D.1    Lombardini, J.B.2
  • 110
    • 0034098230 scopus 로고    scopus 로고
    • Mytilin B and MGD2, two antimicrobial peptides of marine mussels: Gene structure and expression analysis
    • Mitta G., Hubert F., Dyrynda E.A., Boudry P., Roch P. Mytilin B and MGD2, two antimicrobial peptides of marine mussels: Gene structure and expression analysis. Developmental and Comparative Immunology 2000, 24:381-393.
    • (2000) Developmental and Comparative Immunology , vol.24 , pp. 381-393
    • Mitta, G.1    Hubert, F.2    Dyrynda, E.A.3    Boudry, P.4    Roch, P.5
  • 111
    • 0033214630 scopus 로고    scopus 로고
    • Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis
    • Mitta G., Hubert F., Noël T., Roch P. Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis. European Journal of Biochemistry 1999, 265:71-78.
    • (1999) European Journal of Biochemistry , vol.265 , pp. 71-78
    • Mitta, G.1    Hubert, F.2    Noël, T.3    Roch, P.4
  • 112
    • 0033490117 scopus 로고    scopus 로고
    • Mussel defensins are synthesised and processed in granulocytes then released into the plasma after bacterial challenge
    • Mitta G., Vandenbulcke F., Hubert F., Roch P. Mussel defensins are synthesised and processed in granulocytes then released into the plasma after bacterial challenge. Journal of Cell Science 1999, 112:4233-4242.
    • (1999) Journal of Cell Science , vol.112 , pp. 4233-4242
    • Mitta, G.1    Vandenbulcke, F.2    Hubert, F.3    Roch, P.4
  • 113
    • 0034672657 scopus 로고    scopus 로고
    • Original involvement of antimicrobial peptides in mussel innate immunity
    • Mitta G., Vandenbulcke F., Roch P. Original involvement of antimicrobial peptides in mussel innate immunity. FEBS Letters 2000, 486:185-190.
    • (2000) FEBS Letters , vol.486 , pp. 185-190
    • Mitta, G.1    Vandenbulcke, F.2    Roch, P.3
  • 114
    • 0024741960 scopus 로고
    • Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: Chemical structures and biological activity
    • Miyata T., Tokunaga F., Yoneya T., Yoshikawa K., Iwanaga S., Niwa M., Takao T., Shimonishi Y. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: Chemical structures and biological activity. The Journal of Biochemistry 1989, 106:663-668.
    • (1989) The Journal of Biochemistry , vol.106 , pp. 663-668
    • Miyata, T.1    Tokunaga, F.2    Yoneya, T.3    Yoshikawa, K.4    Iwanaga, S.5    Niwa, M.6    Takao, T.7    Shimonishi, Y.8
  • 115
    • 0036660813 scopus 로고    scopus 로고
    • Development of an effective process for utilization of collagen from livestock and fish waste
    • Morimura S., Nagata H., Uemura Y., Fahmi A., Shigematsu T., Kida K. Development of an effective process for utilization of collagen from livestock and fish waste. Process Biochemistry 2002, 37:1403-1412.
    • (2002) Process Biochemistry , vol.37 , pp. 1403-1412
    • Morimura, S.1    Nagata, H.2    Uemura, Y.3    Fahmi, A.4    Shigematsu, T.5    Kida, K.6
  • 116
    • 0026076922 scopus 로고
    • Direct virus inactivation of tachyplesin I and its isopeptides from horseshoe crab hemocytes
    • Murakami T., Niwa M., Tokunaga F., Miyata T., Iwanaga S. Direct virus inactivation of tachyplesin I and its isopeptides from horseshoe crab hemocytes. Chemotherapy 1991, 37:327-334.
    • (1991) Chemotherapy , vol.37 , pp. 327-334
    • Murakami, T.1    Niwa, M.2    Tokunaga, F.3    Miyata, T.4    Iwanaga, S.5
  • 117
    • 84857689022 scopus 로고    scopus 로고
    • The composition of fish. Torry advisory note no. 38, Torry Research Station, Aberdeen.
    • Murray, J., & Burt, J. R. (2001). The composition of fish. Torry advisory note no. 38, Torry Research Station, Aberdeen. http://www.fao.org.
    • (2001)
    • Murray, J.1    Burt, J.R.2
  • 118
    • 34247148223 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemistry, bioactivity and production
    • Murray B.A., FitzGerald R.J. Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemistry, bioactivity and production. Current Pharmaceutical Design 2007, 13:773-791.
    • (2007) Current Pharmaceutical Design , vol.13 , pp. 773-791
    • Murray, B.A.1    FitzGerald, R.J.2
  • 119
    • 84887216344 scopus 로고    scopus 로고
    • Cholestrol-lowering proteins and peptides
    • CRC Press, Boca Raton, Y. Mine, F. Shahidi (Eds.)
    • Nagaoka S. Cholestrol-lowering proteins and peptides. Nutraceutical proteins and peptides in health and disease 2006, 41-67. CRC Press, Boca Raton. Y. Mine, F. Shahidi (Eds.).
    • (2006) Nutraceutical proteins and peptides in health and disease , pp. 41-67
    • Nagaoka, S.1
  • 121
    • 59649100770 scopus 로고    scopus 로고
    • Comparison of ACE inhibitory and DPPH radical scavenging activities of fish muscle hydrolysates
    • Nakajima K., Yoshie-Stark Y., Ogushi M. Comparison of ACE inhibitory and DPPH radical scavenging activities of fish muscle hydrolysates. Food Chemistry 2009, 114:844-851.
    • (2009) Food Chemistry , vol.114 , pp. 844-851
    • Nakajima, K.1    Yoshie-Stark, Y.2    Ogushi, M.3
  • 125
    • 0026764566 scopus 로고
    • Mechanisms of antibacterial action of tachyplesins and polyphemusins, a group of antimicrobial peptides isolated from horseshoe crab hemocytes
    • Ohta M., Ito H., Masuda K., Tanaka S., Arakawa Y., Wacharotayankun R., Kato N. Mechanisms of antibacterial action of tachyplesins and polyphemusins, a group of antimicrobial peptides isolated from horseshoe crab hemocytes. Antimicrobial Agents and Chemotheraphy 1992, 36:1460-1465.
    • (1992) Antimicrobial Agents and Chemotheraphy , vol.36 , pp. 1460-1465
    • Ohta, M.1    Ito, H.2    Masuda, K.3    Tanaka, S.4    Arakawa, Y.5    Wacharotayankun, R.6    Kato, N.7
  • 126
    • 0017578611 scopus 로고
    • Design of specific inhibitors of angiotensin-converting enzyme: New class of orally active antihypertensive agents
    • Ondetti M.A., Rubin B., Cushman D.W. Design of specific inhibitors of angiotensin-converting enzyme: New class of orally active antihypertensive agents. Science 1977, 196:441-444.
    • (1977) Science , vol.196 , pp. 441-444
    • Ondetti, M.A.1    Rubin, B.2    Cushman, D.W.3
  • 127
    • 0029947232 scopus 로고    scopus 로고
    • A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from moses sole fish Pardachirus marmoratus
    • Oren Z., Shai Y. A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from moses sole fish Pardachirus marmoratus. European Journal of Biochemistry 1996, 237:303-310.
    • (1996) European Journal of Biochemistry , vol.237 , pp. 303-310
    • Oren, Z.1    Shai, Y.2
  • 129
    • 0343709388 scopus 로고    scopus 로고
    • Establishment of GABA as an inhibitory neurotransmitter at crustacean neuromuscular junction and in the mammalian central nervous system
    • Birkhauser Verlag, Basel, C. Tanaka, N.G. Bowery (Eds.)
    • Otsuka M. Establishment of GABA as an inhibitory neurotransmitter at crustacean neuromuscular junction and in the mammalian central nervous system. GABA: Receptors, transporters and metabolism 1996, 1-6. Birkhauser Verlag, Basel. C. Tanaka, N.G. Bowery (Eds.).
    • (1996) GABA: Receptors, transporters and metabolism , pp. 1-6
    • Otsuka, M.1
  • 131
    • 0031567605 scopus 로고    scopus 로고
    • A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus
    • Park C.B., Lee J.H., Park I.Y., Kim M.S., Kim S.C. A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus. FEBS Letters 1997, 411:173-178.
    • (1997) FEBS Letters , vol.411 , pp. 173-178
    • Park, C.B.1    Lee, J.H.2    Park, I.Y.3    Kim, M.S.4    Kim, S.C.5
  • 132
    • 0032561422 scopus 로고    scopus 로고
    • Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus
    • Park I.Y., Park C.B., Kim M.S., Kim S.C. Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus. FEBS Letters 1998, 437:258-262.
    • (1998) FEBS Letters , vol.437 , pp. 258-262
    • Park, I.Y.1    Park, C.B.2    Kim, M.S.3    Kim, S.C.4
  • 134
    • 0031751633 scopus 로고    scopus 로고
    • Specific activities of dolastatin 10 and peptide derivatives against Cryptococcus neoformans
    • Pettit R.K., Pettit G.R., Hazen K.C. Specific activities of dolastatin 10 and peptide derivatives against Cryptococcus neoformans. Antimicrobial Agents and Chemotheraphy 1998, 42:2961-2965.
    • (1998) Antimicrobial Agents and Chemotheraphy , vol.42 , pp. 2961-2965
    • Pettit, R.K.1    Pettit, G.R.2    Hazen, K.C.3
  • 135
    • 84857689023 scopus 로고    scopus 로고
    • Disposal and re-utilisation of fish and fish processing waste (including aquaculture waste). NDP Marine RTDI Desk Study series.
    • Pfeiffer, N. (2003). Disposal and re-utilisation of fish and fish processing waste (including aquaculture waste). NDP Marine RTDI Desk Study series.
    • (2003)
    • Pfeiffer, N.1
  • 136
    • 70349218017 scopus 로고    scopus 로고
    • Use of pyloric caeca extract from bigeye snapper (Priacanthus macracanthus) for the production of gelatin hydrolysate with antioxidative activity
    • Phanturat P., Benjakul S., Visessanguan W., Roytrakul S. Use of pyloric caeca extract from bigeye snapper (Priacanthus macracanthus) for the production of gelatin hydrolysate with antioxidative activity. LWT-Food Science and Technology 2010, 43:86-97.
    • (2010) LWT-Food Science and Technology , vol.43 , pp. 86-97
    • Phanturat, P.1    Benjakul, S.2    Visessanguan, W.3    Roytrakul, S.4
  • 139
    • 23444461388 scopus 로고    scopus 로고
    • Inhibition of foodborne bacteria by native and modified protamine: Importance of electrostatic interactions
    • Potter R., Truelstrup Hansen L., Gill T.A. Inhibition of foodborne bacteria by native and modified protamine: Importance of electrostatic interactions. International Journal of Food Microbiology 2005, 103:23-34.
    • (2005) International Journal of Food Microbiology , vol.103 , pp. 23-34
    • Potter, R.1    Truelstrup Hansen, L.2    Gill, T.A.3
  • 140
    • 85122907024 scopus 로고    scopus 로고
    • Membrane-based fractionation and purification strategies for bioactive peptides
    • CRC Press, Boca Raton, Y. Mine, F. Shahidi (Eds.)
    • Pouliot Y., Gauthier S.F., Groleau P.E. Membrane-based fractionation and purification strategies for bioactive peptides. Nutraceutical proteins and peptides in health and disease 2006, 639-658. CRC Press, Boca Raton. Y. Mine, F. Shahidi (Eds.).
    • (2006) Nutraceutical proteins and peptides in health and disease , pp. 639-658
    • Pouliot, Y.1    Gauthier, S.F.2    Groleau, P.E.3
  • 141
    • 14844359987 scopus 로고    scopus 로고
    • A novel anticoagulant purified from fish protein hydrolysate inhibits factor XIIa and platelet aggregation
    • Rajapakse N., Jung W.K., Mendis E., Moon S.H., Kim S.K. A novel anticoagulant purified from fish protein hydrolysate inhibits factor XIIa and platelet aggregation. Life Sciences 2005, 76:2607-2619.
    • (2005) Life Sciences , vol.76 , pp. 2607-2619
    • Rajapakse, N.1    Jung, W.K.2    Mendis, E.3    Moon, S.H.4    Kim, S.K.5
  • 142
    • 23944469378 scopus 로고    scopus 로고
    • Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical-mediated oxidative systems
    • Rajapakse N., Mendis E., Byun H.G., Kim S.K. Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical-mediated oxidative systems. The Journal of Nutritional Biochemistry 2005, 16:562-569.
    • (2005) The Journal of Nutritional Biochemistry , vol.16 , pp. 562-569
    • Rajapakse, N.1    Mendis, E.2    Byun, H.G.3    Kim, S.K.4
  • 143
    • 11144293558 scopus 로고    scopus 로고
    • Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties
    • Rajapakse N., Mendis E., Jung W.K., Je J.Y., Kim S.K. Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties. Food Research International 2005, 38:175-182.
    • (2005) Food Research International , vol.38 , pp. 175-182
    • Rajapakse, N.1    Mendis, E.2    Jung, W.K.3    Je, J.Y.4    Kim, S.K.5
  • 144
    • 7544244554 scopus 로고    scopus 로고
    • Cloning of kuruma prawn Marsupenaeus japonicus crustin-like peptide cCNA and analysis of its expression
    • Rattanachai A., Hirono I., Ohira T., Takahashi Y., Aoki T. Cloning of kuruma prawn Marsupenaeus japonicus crustin-like peptide cCNA and analysis of its expression. Fisheries Science 2004, 765:771.
    • (2004) Fisheries Science , vol.765 , pp. 771
    • Rattanachai, A.1    Hirono, I.2    Ohira, T.3    Takahashi, Y.4    Aoki, T.5
  • 145
    • 0033198883 scopus 로고    scopus 로고
    • Purification and characterization of a cysteine-rich 11.5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas
    • Relf J.M., Chisholm J.R.S., Kemp G.D., Smith V.J. Purification and characterization of a cysteine-rich 11.5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas. European Journal of Biochemistry 1999, 264:350-357.
    • (1999) European Journal of Biochemistry , vol.264 , pp. 350-357
    • Relf, J.M.1    Chisholm, J.R.S.2    Kemp, G.D.3    Smith, V.J.4
  • 147
    • 24344442307 scopus 로고    scopus 로고
    • Antiprotozoan and antiviral activities of non-cytotoxic truncated and variant analogues of mussel defensin
    • Roch P., Beschin A., Bernard E. Antiprotozoan and antiviral activities of non-cytotoxic truncated and variant analogues of mussel defensin. Evidenced-based Complementary and Alternative Medicine 2004, 1:167-174.
    • (2004) Evidenced-based Complementary and Alternative Medicine , vol.1 , pp. 167-174
    • Roch, P.1    Beschin, A.2    Bernard, E.3
  • 148
    • 0038045648 scopus 로고    scopus 로고
    • Key role of the loop connecting the two beta strands of mussel defensin in its antimicrobial activity
    • Romestand B., Molina F., Richard V., Roch P., Granier C. Key role of the loop connecting the two beta strands of mussel defensin in its antimicrobial activity. European Journal of Biochemistry 2004, 270:2805-2813.
    • (2004) European Journal of Biochemistry , vol.270 , pp. 2805-2813
    • Romestand, B.1    Molina, F.2    Richard, V.3    Roch, P.4    Granier, C.5
  • 149
    • 79251639867 scopus 로고    scopus 로고
    • Fundamental functionality: Recent developments in understanding the structure-activity relationships of lantibiotic peptides
    • Ross A.C., Vederas J.C. Fundamental functionality: Recent developments in understanding the structure-activity relationships of lantibiotic peptides. The Journal of Antibiotics 2011, 64:27-34.
    • (2011) The Journal of Antibiotics , vol.64 , pp. 27-34
    • Ross, A.C.1    Vederas, J.C.2
  • 151
    • 77956688199 scopus 로고    scopus 로고
    • Antioxidative peptides from food proteins: A review
    • Sarmadi B.H., Ismail A. Antioxidative peptides from food proteins: A review. Peptides 2010, 31:1949-1956.
    • (2010) Peptides , vol.31 , pp. 1949-1956
    • Sarmadi, B.H.1    Ismail, A.2
  • 153
    • 0026059199 scopus 로고
    • Antithrombotic efficacy of recombinant tick anticoagulant peptide. A potent inhibitor of coagulation factor Xa in a primate model of arterial thrombosis
    • Schaffer L.W., Davidson J.T., Vlasuk G.P., Siegl P.K. Antithrombotic efficacy of recombinant tick anticoagulant peptide. A potent inhibitor of coagulation factor Xa in a primate model of arterial thrombosis. Circulation 1991, 84:1741-1748.
    • (1991) Circulation , vol.84 , pp. 1741-1748
    • Schaffer, L.W.1    Davidson, J.T.2    Vlasuk, G.P.3    Siegl, P.K.4
  • 154
    • 0029762649 scopus 로고    scopus 로고
    • Purification and characterization of a proline-rich antibacterial peptide, with sequence similarity to Bactenecin-7, from the haemocytes of the shore crab, Carcinus maenas
    • Schnapp D., Kemp G.D., Smith V.J. Purification and characterization of a proline-rich antibacterial peptide, with sequence similarity to Bactenecin-7, from the haemocytes of the shore crab, Carcinus maenas. European Journal of Biochemistry 1996, 240:532-539.
    • (1996) European Journal of Biochemistry , vol.240 , pp. 532-539
    • Schnapp, D.1    Kemp, G.D.2    Smith, V.J.3
  • 155
    • 36749053463 scopus 로고    scopus 로고
    • Antioxidants: Regulatory status
    • John Wiley and Sons Inc. F. Shahidi (Ed.)
    • Shahidi F., Zhong Y. Antioxidants: Regulatory status. Bailey's industrial oil and fat products 2005, 491-521. John Wiley and Sons Inc. F. Shahidi (Ed.).
    • (2005) Bailey's industrial oil and fat products , pp. 491-521
    • Shahidi, F.1    Zhong, Y.2
  • 156
    • 41949114267 scopus 로고    scopus 로고
    • Risk assessment for the amino acids taurine, l-glutamine and l-arginine
    • Shao A., Hathcock J.N. Risk assessment for the amino acids taurine, l-glutamine and l-arginine. Regulatory Toxicology and Pharmacology 2008, 50:376-399.
    • (2008) Regulatory Toxicology and Pharmacology , vol.50 , pp. 376-399
    • Shao, A.1    Hathcock, J.N.2
  • 158
    • 0033991719 scopus 로고    scopus 로고
    • Isolation and structures of grammistins, peptide toxins from the skin secretion of the soapfish Grammistes sexlineatus
    • Shiomi K., Igarashi T., Yokota H., Nagashima Y., Ishida M. Isolation and structures of grammistins, peptide toxins from the skin secretion of the soapfish Grammistes sexlineatus. Toxicon 2000, 38:91-103.
    • (2000) Toxicon , vol.38 , pp. 91-103
    • Shiomi, K.1    Igarashi, T.2    Yokota, H.3    Nagashima, Y.4    Ishida, M.5
  • 159
    • 0035001105 scopus 로고    scopus 로고
    • Primary and secondary structures of grammistins, peptide toxins isolated from the skin secretion of the soapfish Pogonoperca punctata
    • Shiomi K., Yokota H., Nagashima Y., Ishida M. Primary and secondary structures of grammistins, peptide toxins isolated from the skin secretion of the soapfish Pogonoperca punctata. Fisheries Science 2001, 67:163-169.
    • (2001) Fisheries Science , vol.67 , pp. 163-169
    • Shiomi, K.1    Yokota, H.2    Nagashima, Y.3    Ishida, M.4
  • 162
    • 0034093866 scopus 로고    scopus 로고
    • Antioxidant peptides from the protease digest of prawn (Penaeus japonicus) muscle
    • Suetsuna K. Antioxidant peptides from the protease digest of prawn (Penaeus japonicus) muscle. Marine Biotechnology 2000, 2:5-10.
    • (2000) Marine Biotechnology , vol.2 , pp. 5-10
    • Suetsuna, K.1
  • 163
    • 15044363987 scopus 로고    scopus 로고
    • Further isolation and characterization of grammistins from the skin secretion of the soapfish Grammistes sexlineatus
    • Sugiyama N., Araki M., Ishida M., Nagashima Y., Shiomi K. Further isolation and characterization of grammistins from the skin secretion of the soapfish Grammistes sexlineatus. Toxicon 2005, 45:595-601.
    • (2005) Toxicon , vol.45 , pp. 595-601
    • Sugiyama, N.1    Araki, M.2    Ishida, M.3    Nagashima, Y.4    Shiomi, K.5
  • 164
    • 77949912175 scopus 로고    scopus 로고
    • Molecular cloning and characterization of three crustins from the Chinese white shrimp, Fenneropenaeus chinensis
    • Sun C., Du X.J., Xu W.T., Zhang H.W., Zhao X.F., Wang J.X. Molecular cloning and characterization of three crustins from the Chinese white shrimp, Fenneropenaeus chinensis. Fish & Shellfish Immunology 2010, 28:517-524.
    • (2010) Fish & Shellfish Immunology , vol.28 , pp. 517-524
    • Sun, C.1    Du, X.J.2    Xu, W.T.3    Zhang, H.W.4    Zhao, X.F.5    Wang, J.X.6
  • 166
    • 84857684907 scopus 로고    scopus 로고
    • Bioactive peptides from marine sources. State of art. Report to the NORA fund, Skrsla Matís 14-09, Reykjavík.
    • Thorkelsson, G., & Kristinsson, H. G. (2009). Bioactive peptides from marine sources. State of art. Report to the NORA fund, Skrsla Matís 14-09, Reykjavík.
    • (2009)
    • Thorkelsson, G.1    Kristinsson, H.G.2
  • 167
    • 44249117319 scopus 로고    scopus 로고
    • ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)
    • Tsai J.S., Chen J.L., Pan B.S. ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria). Process Biochemistry 2008, 43:743-747.
    • (2008) Process Biochemistry , vol.43 , pp. 743-747
    • Tsai, J.S.1    Chen, J.L.2    Pan, B.S.3
  • 168
    • 33646090414 scopus 로고    scopus 로고
    • Antihypertensive peptides and [gamma]-aminobutyric acid from prozyme 6 facilitated lactic acid bacteria fermentation of soymilk
    • Tsai J.S., Lin Y.S., Pan B.S., Chen T.J. Antihypertensive peptides and [gamma]-aminobutyric acid from prozyme 6 facilitated lactic acid bacteria fermentation of soymilk. Process Biochemistry 2006, 41:1282-1288.
    • (2006) Process Biochemistry , vol.41 , pp. 1282-1288
    • Tsai, J.S.1    Lin, Y.S.2    Pan, B.S.3    Chen, T.J.4
  • 169
    • 0031960723 scopus 로고    scopus 로고
    • Treatment of human prostate cancer cells with dolastatin 10, a peptide isolated from a marine shell-less mollusc
    • Turner T., Jackson W.H., Pettit G.R., Wells A., Kraft A.S. Treatment of human prostate cancer cells with dolastatin 10, a peptide isolated from a marine shell-less mollusc. The Prostate 1998, 34:175-181.
    • (1998) The Prostate , vol.34 , pp. 175-181
    • Turner, T.1    Jackson, W.H.2    Pettit, G.R.3    Wells, A.4    Kraft, A.S.5
  • 170
    • 64549083283 scopus 로고    scopus 로고
    • Kinetics of the inhibition of renin and angiotensin I-converting enzyme by flaxseed protein hydrolysate fractions
    • Udenigwe C.C., Lin Y.-S., Hou W.-C., Aluko R.E. Kinetics of the inhibition of renin and angiotensin I-converting enzyme by flaxseed protein hydrolysate fractions. Journal of Functional Foods 2009, 1:199-207.
    • (2009) Journal of Functional Foods , vol.1 , pp. 199-207
    • Udenigwe, C.C.1    Lin, Y.-S.2    Hou, W.-C.3    Aluko, R.E.4
  • 171
    • 0028041981 scopus 로고
    • Evaluation of the antimicrobial activity of protamine
    • Uyttendaele M., Debevere J. Evaluation of the antimicrobial activity of protamine. Food Microbiology 1994, 11:417-427.
    • (1994) Food Microbiology , vol.11 , pp. 417-427
    • Uyttendaele, M.1    Debevere, J.2
  • 172
    • 0033739893 scopus 로고    scopus 로고
    • Phase II study of Dolastatin-10 in patients with hormone-refractory metastatic prostate adenocarcinoma
    • Vaishampayan U., Glode M., Du W., Kraft A., Hudes G., Wright J., Hussain M. Phase II study of Dolastatin-10 in patients with hormone-refractory metastatic prostate adenocarcinoma. Clinical Cancer Research 2000, 6:4205-4208.
    • (2000) Clinical Cancer Research , vol.6 , pp. 4205-4208
    • Vaishampayan, U.1    Glode, M.2    Du, W.3    Kraft, A.4    Hudes, G.5    Wright, J.6    Hussain, M.7
  • 173
    • 77957062245 scopus 로고    scopus 로고
    • Fish proteins from unexploited and underdeveloped sources
    • Elsevier, Amsterdam, G. Doxastakis, V. Kiosseoglou (Eds.)
    • Vareltzis K. Fish proteins from unexploited and underdeveloped sources. Novel macromolecules in food systems 2000, 133-159. Elsevier, Amsterdam. G. Doxastakis, V. Kiosseoglou (Eds.).
    • (2000) Novel macromolecules in food systems , pp. 133-159
    • Vareltzis, K.1
  • 178
    • 27644568624 scopus 로고    scopus 로고
    • ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: A review
    • Vercruysse L., Camp J.V., Smagghe G. ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: A review. Journal of Agricultural and Food Chemistry 2005, 53:8106-8115.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 8106-8115
    • Vercruysse, L.1    Camp, J.V.2    Smagghe, G.3
  • 179
    • 0027216868 scopus 로고
    • Structural and functional characterization of tick anticoagulant peptide (TAP): A potent and selective inhibitor of blood coagulation factor Xa
    • Vlasuk G.P. Structural and functional characterization of tick anticoagulant peptide (TAP): A potent and selective inhibitor of blood coagulation factor Xa. Thrombosis Haemostasis 1993, 70:212-216.
    • (1993) Thrombosis Haemostasis , vol.70 , pp. 212-216
    • Vlasuk, G.P.1
  • 180
    • 51749125991 scopus 로고    scopus 로고
    • Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats
    • Wang J., Hu J., Cui J., Bai X., Du Y., Miyaguchi Y., Lin B. Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats. Food Chemistry 2008, 111:302-308.
    • (2008) Food Chemistry , vol.111 , pp. 302-308
    • Wang, J.1    Hu, J.2    Cui, J.3    Bai, X.4    Du, Y.5    Miyaguchi, Y.6    Lin, B.7
  • 182
    • 0029950818 scopus 로고    scopus 로고
    • Keenamide A, a bioactive cyclic peptide from the marine mollusk Pleurobranchus forskalii
    • Wesson K.J., Hamann M.T. Keenamide A, a bioactive cyclic peptide from the marine mollusk Pleurobranchus forskalii. Journal of Natural Products 1996, 59:629-631.
    • (1996) Journal of Natural Products , vol.59 , pp. 629-631
    • Wesson, K.J.1    Hamann, M.T.2
  • 183
    • 0035180508 scopus 로고    scopus 로고
    • In vitro activities and postantifungal effects of the potent dolastatin 10 derivative auristatin PHE
    • Woyke T., Pettit G.R., Winkelmann G., Pettit R.K. In vitro activities and postantifungal effects of the potent dolastatin 10 derivative auristatin PHE. Antimicrobial Agents and Chemotheraphy 2001, 45:3580-3584.
    • (2001) Antimicrobial Agents and Chemotheraphy , vol.45 , pp. 3580-3584
    • Woyke, T.1    Pettit, G.R.2    Winkelmann, G.3    Pettit, R.K.4
  • 184
    • 10744230552 scopus 로고    scopus 로고
    • Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus)
    • Wu H.C., Chen H.M., Shiau C.Y. Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus). Food Research International 2003, 36:949-957.
    • (2003) Food Research International , vol.36 , pp. 949-957
    • Wu, H.C.1    Chen, H.M.2    Shiau, C.Y.3
  • 185
    • 0008250358 scopus 로고    scopus 로고
    • Interaction of grammistins with lipids and their antibacterial activity
    • Yokota H., Nagashima Y., Shiom K. Interaction of grammistins with lipids and their antibacterial activity. Fisheries Science 2001, 67:928-933.
    • (2001) Fisheries Science , vol.67 , pp. 928-933
    • Yokota, H.1    Nagashima, Y.2    Shiom, K.3
  • 186
    • 0027318991 scopus 로고
    • Influence of dietary fish proteins on plasma and liver cholesterol concentrations in rats
    • Zhang X., Beynen A.C. Influence of dietary fish proteins on plasma and liver cholesterol concentrations in rats. British Journal of Nutrition 1993, 69:767-777.
    • (1993) British Journal of Nutrition , vol.69 , pp. 767-777
    • Zhang, X.1    Beynen, A.C.2
  • 187
    • 3042519102 scopus 로고    scopus 로고
    • Beneficial effects of taurine on serum lipids in overweight or obese non-diabetic subjects
    • Zhang M., Bi L.F., Fang J.H., Su X.L., Da G.L., Kuwamori T., Kagamimori S. Beneficial effects of taurine on serum lipids in overweight or obese non-diabetic subjects. Amino Acids 2004, 26:267-271.
    • (2004) Amino Acids , vol.26 , pp. 267-271
    • Zhang, M.1    Bi, L.F.2    Fang, J.H.3    Su, X.L.4    Da, G.L.5    Kuwamori, T.6    Kagamimori, S.7
  • 188
    • 33845643045 scopus 로고    scopus 로고
    • Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis
    • Zhang J., Li F., Wang Z., Xiang J. Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis. Journal of Biotechnology 2007, 127:605-614.
    • (2007) Journal of Biotechnology , vol.127 , pp. 605-614
    • Zhang, J.1    Li, F.2    Wang, Z.3    Xiang, J.4


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