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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 李英周(Yin-Chou Lee) | |
dc.contributor.author | Chun-Hui Huang | en |
dc.contributor.author | 黃均蕙 | zh_TW |
dc.date.accessioned | 2021-06-08T02:55:35Z | - |
dc.date.copyright | 2017-08-11 | |
dc.date.issued | 2017 | |
dc.date.submitted | 2017-08-04 | |
dc.identifier.citation | Alemán, A., Giménez, B., Montero, P., and Gómez-Guillén, M. C. (2011a). Antioxidant activity of several marine skin gelatins. LWT-Food Science and Technology, 44(2), 407-413.
Alemán, A., Giménez, B., Pérez-Santin, E., Gómez-Guillén, M. C., and Montero, P. (2011b). Contribution of Leu and Hyp residues to antioxidant and ACE-inhibitory activities of peptide sequences isolated from squid gelatin hydrolysate. Food Chemistry, 125(2), 334-341. Amado, I. R., Vázquez, J. A., González, M. P., and Murado, M. A. (2013). Production of antihypertensive and antioxidant activities by enzymatic hydrolysis of protein concentrates recovered by ultrafiltration from cuttlefish processing wastewaters. Biochemical engineering journal, 76, 43-54. Arancibia, M. Y., Alemán, A., Calvo, M. M., López-Caballero, M. E., Montero, P., and Gómez-Guillén, M. C. (2014). Antimicrobial and antioxidant chitosan solutions enriched with active shrimp (Litopenaeus vannamei) waste materials. Food Hydrocolloids, 35, 710-717. Bass, J. K., and Chan, G. M. (2006). Calcium nutrition and metabolism during infancy. Nutrition, 22(10), 1057-1066. Benito-Ruiz, P., Camacho-Zambrano, M. M., Carrillo-Arcentales, J. N., Mestanza-Peralta, M. A., Vallejo-Flores, C. A., Vargas-López, S. V., and Zurita-Gavilanes, L. A. (2009). A randomized controlled trial on the efficacy and safety of a food ingredient, collagen hydrolysate, for improving joint comfort. International journal of food sciences and nutrition, 60(sup2), 99-113. Benjakul, S., Yarnpakdee, S., Senphan, T., Halldorsdottir, S. M., and Kristinsson, H. G. (2014). Fish protein hydrolysates: production, bioactivities and applications. Antioxidants and functional components in aquatic foods, 1st ed. Reykjavik, Iceland: Matil Ltd, 237-83. Boldyrev, A. A., Dupin, A. M., Siambela, M., and Stvolinsky, S. L. (1988). The level of natural antioxidant glutathione and histidine-containing dipeptides in skeletal muscles of developing chick embryos. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 89(1), 197-200. Byun, H. G., and Kim, S. K. (2001). Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin. Process Biochemistry, 36(12), 1155-1162. Cai, Y., Luo, Q., Sun, M., and Corke, H. (2004). Antioxidant activity and phenolic compounds of 112 traditional Chinese medicinal plants associated with anticancer. Life sciences, 74(17), 2157-2184. Carrasco-Castilla, J., Hernández-Álvarez, A. J., Jiménez-Martínez, C., Jacinto-Hernández, C., Alaiz, M., Girón-Calle and Dávila-Ortiz, G. (2012). Antioxidant and metal chelating activities of peptide fractions from phaseolin and bean protein hydrolysates. Food chemistry, 135(3), 1789-1795. Chen, F. Y., Lee, M. T., and Huang, H. W. (2003). Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Biophysical journal, 84(6), 3751-3758. Christofilogiannis, P. (2001). Current inoculation methods in MIC determination. Aquaculture, 196(3), 297-302. Choonpicharn, S., Jaturasitha, S., Rakariyatham, N., Suree, N., and Niamsup, H. (2015). Antioxidant and antihypertensive activity of gelatin hydrolysate from Nile tilapia skin. Journal of food science and technology, 52(5), 3134-3139. Decker, E. A., and Welch, B. (1990). Role of ferritin as a lipid oxidation catalyst in muscle food. Journal of Agricultural and food Chemistry, 38(3), 674-677. Di Bernardini, R., Harnedy, P., Bolton, D., Kerry, J., O’Neill, E., Mullen, A. M., and Hayes, M. (2011). Antioxidant and antimicrobial peptidic hydrolysates from muscle protein sources and by-products. Food Chemistry, 124(4), 1296-1307. Di Bernardini, R., Mullen, A. M., Bolton, D., Kerry, J., O'Neill, E., and Hayes, M. (2012). Assessment of the angiotensin-I-converting enzyme (ACE-I) inhibitory and antioxidant activities of hydrolysates of bovine brisket sarcoplasmic proteins produced by papain and characterisation of associated bioactive peptidic fractions. Meat science, 90(1), 226-235. Dong, C., and Lv, Y. (2016). Application of collagen scaffold in tissue engineering: recent advances and new perspectives. Polymers, 8(2), 42. Dong, S., Zeng, M., Wang, D., Liu, Z., Zhao, Y., and Yang, H. (2008). Antioxidant and biochemical properties of protein hydrolysates prepared from Silver carp (Hypophthalmichthys molitrix). Food Chemistry, 107(4), 1485-1493. Eastoe, J. E. (1957). The amino acid composition of fish collagen and gelatin. Biochemical Journal, 65(2), 363. Eastoe, J. E., and Leach, A. A. (1958). A survey of recent work on the amino acid composition of vertebrate collagen and gelatin. Recent advances in gelatin and glue research, 173. Ennaas, N., Hammami, R., Beaulieu, L., and Fliss, I. (2015). Purification and characterization of four antibacterial peptides from protamex hydrolysate of Atlantic mackerel (Scomber scombrus) by-products. Biochemical and biophysical research communications, 462(3), 195-200. Ezejiofor, T. I. N., Enebaku, U. E., and Ogueke, C. (2014). Waste to Wealth-Value Recovery from Agro-food Processing Wastes Using Biotechnology: A Review. Flaudrops, C., Armstrong, N., Raoult, D., and Chabrière, E. (2015). Determination of the animal origin of meat and gelatin by MALDI-TOF-MS. Journal of Food Composition and Analysis, 41, 104-112. Floris, R., Recio, I., Berkhout, B., and Visser, S. (2003). Antibacterial and antiviral effects of milk proteins and derivatives thereof. Current pharmaceutical design, 9(16), 1257-1275. Gajanan, P. G., Elavarasan, K., and Shamasundar, B. A. (2016). Bioactive and functional properties of protein hydrolysates from fish frame processing waste using plant proteases. Environmental Science and Pollution Research, 23(24), 24901-24911. Gallo, R. L., Ono, M., Povsic, T., Page, C., Eriksson, E., Klagsbrun, M., and Bernfield, M. (1994). Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proceedings of the National Academy of Sciences, 91(23), 11035-11039. Ghanbari, R., Ebrahimpour, A., Abdul-Hamid, A., Ismail, A., and Saari, N. (2012). Actinopyga lecanora hydrolysates as natural antibacterial agents. International journal of molecular sciences, 13(12), 16796-16811. Giménez, B., Alemán, A., Montero, P., and Gómez-Guillén, M. C. (2009). Antioxidant and functional properties of gelatin hydrolysates obtained from skin of sole and squid. Food Chemistry, 114(3), 976-983. Gómez-Guillén, M. C., Giménez, B., López-Caballero, M. A., and Montero, M. P. (2011). Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food hydrocolloids, 25(8), 1813-1827. Guo, H., Kouzuma, Y., and Yonekura, M. (2009). Structures and properties of antioxidative peptides derived from royal jelly protein. Food Chemistry, 113(1), 238-245. Guo, L., Harnedy, P. A., Li, B., Hou, H., Zhang, Z., Zhao, X., and Fitz Gerald, R. J. (2014). Food protein-derived chelating peptides: biofunctional ingredients for dietary mineral bioavailability enhancement. Trends in food science and technology, 37(2), 92-105. Guo, L., Harnedy, P. A., O’Keeffe, M. B., Zhang, L., Li, B., Hou, H., and FitzGerald, R. J. (2015). Fractionation and identification of Alaska pollock skin collagen-derived mineral chelating peptides. Food chemistry, 173, 536-542. Guo, L., Hou, H., Li, B., Zhang, Z., Wang, S., and Zhao, X. (2013). Preparation, isolation and identification of iron-chelating peptides derived from Alaska pollock skin. Process Biochemistry, 48(5), 988-993. Harrington, W. F., and Von Hippel, P. H. (1962). The structure of collagen and gelatin. Advances in protein chemistry, 16, 1-138. Harrington, W. F., and von Hippel, P. H. (1961). Formation and stabilization of the collagen-fold. Archives of biochemistry and biophysics, 92(1), 100-113. Ikoma, T., Kobayashi, H., Tanaka, J., Walsh, D., and Mann, S. (2003). Microstructure, mechanical, and biomimetic properties of fish scales from Pagrus major. Journal of structural biology, 142(3), 327-333. Ikoma, T., Kobayashi, H., Tanaka, J., Walsh, D., and Mann, S. (2003). Physical properties of type I collagen extracted from fish scales of Pagrus major and Oreochromis niloticas. International journal of biological macromolecules, 32(3), 199-204. Jamilah, B., and Harvinder, K. G. (2002). Properties of gelatins from skins of fish—black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica). Food chemistry, 77(1), 81-84. Je, J. Y., Park, P. J., and Kim, S. K. (2005). Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Research International, 38(1), 45-50. Je, J. Y., Qian, Z. J., Byun, H. G., and Kim, S. K. (2007). Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis. Process Biochemistry, 42(5), 840-846. Jun, S. Y., Park, P. J., Jung, W. K., and Kim, S. K. (2004). Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. European Food Research and Technology, 219(1), 20-26. Jung, W. K., and Kim, S. K. (2007). Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame. European Food Research and Technology, 224(6), 763-767. Jung WK, Lee BJ, Kim SK (2006) Fish-bone peptide increases calcium solubility and bioavailability in ovariectomised rats. Brit J Nutr, 95, 124-128 Jung, W. K., Karawita, R., Heo, S. J., Lee, B. J., Kim, S. K., and Jeon, Y. J. (2006). Recovery of a novel Ca-binding peptide from Alaska Pollack (Theragra chalcogramma) backbone by pepsinolytic hydrolysis. Process Biochemistry, 41(9), 2097-2100. Kielty, C. M., and Shuttleworth, C. A. (1993). The role of calcium in the organization of fibrillin microfibrils. FEBS letters, 336(2), 323-326. Kim, N. H., Jung, S. H., Kim, J., Kim, S. H., Ahn, H. J., and Song, K. B. (2014). Purification of an iron-chelating peptide from spirulina protein hydrolysates. Journal of the Korean Society for Applied Biological Chemistry, 57(1), 91-95. Kim, S. K., and Wijesekara, I. (2010). Development and biological activities of marine-derived bioactive peptides: A review. Journal of Functional foods, 2(1), 1-9. Kim, S. K., Kim, Y. T., Byun, H. G., Nam, K. S., Joo, D. S., and Shahidi, F. (2001). Isolation and characterization of antioxidative peptides from gelatin hydrolysate of Alaska pollack skin. Journal of Agricultural and Food Chemistry, 49(4), 1984-1989. Kim, S. K., Perera, U. M. S. P., and Rajapakse, N. (2016). Seafood Processing By-Products. Springer-Verlag New York. Sharma, O. P., and Bhat, T. K. (2009). DPPH antioxidant assay revisited. Food chemistry, 113(4), 1202-1205. Kim, S. Y., Je, J. Y., and 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. Kimura, S., Miyauchi, Y., and Uchida, N. (1991). Scale and bone type I collagens of carp (Cyprinus carpio). Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 99(2), 473-476. Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., and Shahidi, F. (2012). Gelatin hydrolysate from blacktip shark skin prepared using papaya latex enzyme: antioxidant activity and its potential in model systems. Food Chemistry, 135(3), 1118-1126. Ktari, N., Khaled, H. B., Nasri, R., Jellouli, K., Ghorbel, S., and Nasri, M. (2012). Trypsin from zebra blenny (Salaria basilisca) viscera: Purification, characterisation and potential application as a detergent additive. Food chemistry, 130(3), 467-474. Kumar, B., and Rani, S. (2017). Technical note on the isolation and characterization of collagen from fish waste material. Journal of food science and technology, 54(1), 276-278. Kumar, N. S., Nazeer, R. A., and Jaiganesh, R. (2011). Purification and biochemical characterization of antioxidant peptide from horse mackerel (Magalaspis cordyla) viscera protein. Peptides, 32(7), 1496-1501. Langmaier, F., Mládek, M., Kolomazník, K., and Sukop, S. (2001). Collagenous hydrolysates from untraditional sources of proteins. International journal of cosmetic science, 23(4), 193-199. Lee, C. H., Singla, A., and Lee, Y. (2001). Biomedical applications of collagen. International journal of pharmaceutics, 221(1), 1-22. Lee, J. Y., Choo, J. E., Choi, Y. S., Park, J. B., Min, D. S., Lee, S. J. and Park, Y. J. (2007). Assembly of collagen-binding peptide with collagen as a bioactive scaffold for osteogenesis in vitro and in vivo. Biomaterials, 28(29), 4257-4267. Levine, R. L., Berlett, B. S., Moskovitz, J., Mosoni, L., and Stadtman, E. R. (1999). Methionine residues may protect proteins from critical oxidative damage. Mechanisms of ageing and development, 107(3), 323-332. Liu, Z., 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. Liu, D., Liang, L., Regenstein, J. M., and Zhou, P. (2012). Extraction and characterisation of pepsin-solubilised collagen from fins, scales, skins, bones and swim bladders of bighead carp (Hypophthalmichthys nobilis). Food Chemistry, 133(4), 1441-1448. Mahboob, S. (2015). Isolation and characterization of collagen from fish waste material-skin, scales and fins of Catla catla and Cirrhinus mrigala. Journal of food science and technology, 52(7), 4296. Martínez-Alvarez, O., Chamorro, S., and Brenes, A. (2015). Protein hydrolysates from animal processing by-products as a source of bioactive molecules with interest in animal feeding: A review. Food Research International, 73, 204-212. Matthew, H. W. (2001). Polymers for tissue engineering scaffolds. Polymeric biomaterials, 8, 167-170. McGrory, J., Costa, T., and Cole, W. G. (1996). A novel G499D substitution in the α1 (III) chain of type III collagen produces variable forms of Ehlers‐Danlos syndrome type IV. Human mutation, 7(1), 59-60. Mendis, E., Rajapakse, N., and Kim, S. K. (2005). Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. Journal of agricultural and food chemistry, 53(3), 581-587. Mitchell, A. D., and Taylor, I. E. P. (1970). The spectrophotometric determination of hydroxyproline: an analytical investigation. Analyst, 95(1137), 1003-1011. Morimoto, M., Mori, H., Otake, T., Ueba, N., Kunita, N., Niwa, M. and Iwanaga, S. (1991). Inhibitory effect of tachyplesin I on the proliferation of human immunodeficiency virus in vitro. Chemotherapy, 37(3), 206-211. Morimura, S., Nagata, H., Uemura, Y., Fahmi, A., Shigematsu, T., and Kida, K. (2002). Development of an effective process for utilization of collagen from livestock and fish waste. Process Biochemistry, 37(12), 1403-1412. Nagai, T., Izumi, M., and Ishii, M. (2004). Fish scale collagen. Preparation and partial characterization. International journal of food science and technology, 39(3), 239-244. Nasri, R., Amor, I. B., Bougatef, A., Nedjar-Arroume, N., Dhulster, P., Gargouri, J. and Nasri, M. (2012). Anticoagulant activities of goby muscle protein hydrolysates. Food chemistry, 133(3), 835-841. Najafian, L., and Babji, A. S. (2012). A review of fish-derived antioxidant and antimicrobial peptides: their production, assessment, and applications. Peptides, 33(1), 178-185. Ngo, D. H., Qian, Z. J., Ryu, B., Park, J. W., and Kim, S. K. (2010). In vitro antioxidant activity of a peptide isolated from Nile tilapia (Oreochromis niloticus) scale gelatin in free radical-mediated oxidative systems. Journal of Functional Foods, 2(2), 107-117. Ogawa, M., Portier, R. J., Moody, M. W., Bell, J., Schexnayder, M. A., and Losso, J. N. (2004). Biochemical properties of bone and scale collagens isolated from the subtropical fish black drum (Pogonia cromis) and sheepshead seabream (Archosargus probatocephalus). Food chemistry, 88(4), 495-501. Pati, F., Adhikari, B., and Dhara, S. (2010). Isolation and characterization of fish scale collagen of higher thermal stability. Bioresource technology, 101(10), 3737-3742. Papargyropoulou, E., Lozano, R., Steinberger, J. K., Wright, N., & bin Ujang, Z. (2014). The food waste hierarchy as a framework for the management of food surplus and food waste. Journal of Cleaner Production, 76, 106-115. Pihlanto-Leppälä, A. (2000). Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides. Trends in Food Science and Technology, 11(9), 347-356. Powers, J. P. S., and Hancock, R. E. (2003). The relationship between peptide structure and antibacterial activity. Peptides, 24(11), 1681-1691. Prior, R. L., Wu, X., and Schaich, K. (2005). Standardized methods for the determination of antioxidant capacity and phenolics in foods and dietary supplements. Journal of agricultural and food chemistry, 53(10), 4290-4302. Raksakulthai, R., and Haard, N. F. (2003). Exopeptidases and their application to reduce bitterness in food: a review. Reddy, G. K., and Enwemeka, C. S. (1996). A simplified method for the analysis of hydroxyproline in biological tissues. Clinical biochemistry, 29(3), 225-229. Reddy, R. D., and Yao, J. K. (1996). Free radical pathology in schizophrenia: a review. Prostaglandins, Leukotrienes and Essential Fatty Acids, 55(1-2), 33-43. Sae-leaw, T., O’Callaghan, Y. C., Benjakul, S., and O’Brien, N. M. (2016). Antioxidant activities and selected characteristics of gelatin hydrolysates from seabass (Lates calcarifer) skin as affected by production processes. Journal of food science and technology, 53(1), 197-208. Saiga, A. I., Tanabe, S., and Nishimura, T. (2003). Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment. Journal of agricultural and food chemistry, 51(12), 3661-3667. Samaranayaka, A. G., Kitts, D. D., and Li-Chan, E. C. (2010). Antioxidative and angiotensin-I-converting enzyme inhibitory potential of a Pacific hake (Merluccius productus) fish protein hydrolysate subjected to simulated gastrointestinal digestion and Caco-2 cell permeation. Journal of Agricultural and Food Chemistry, 58(3), 1535-1542. Senaratne, L. S., Park, P. J., and Kim, S. K. (2006). Isolation and characterization of collagen from brown backed toadfish (Lagocephalus gloveri) skin. Bioresource technology, 97(2), 191-197. Shahidi, F., Synowiecki, J., and Balejko, J. (1994). Proteolytic hydrolysis of muscle proteins of harp seal (Phoca groenlandica). Journal of Agricultural and Food Chemistry, 42(11), 2634-2638. Sharma, O. P., and Bhat, T. K. (2009). DPPH antioxidant assay revisited. Food chemistry, 113(4), 1202-1205. Shimuzu, Y., Natsume, T., Makihara, T., Akasaka, M., and Sakakibara, H. (1997). U.S. Patent No. 5,679,372. Washington, DC: U.S. Patent and Trademark Office. Sionkowska, A., Skrzyński, S., Śmiechowski, K., and Kołodziejczak, A. (2017). The review of versatile application of collagen. Polymers for Advanced Technologies, 28(1), 4-9. Šližytė, R., Mozuraitytė, R., Martínez-Alvarez, O., Falch, E., Fouchereau-Peron, M., and Rustad, T. (2009). Functional, bioactive and antioxidative properties of hydrolysates obtained from cod (Gadus morhua) backbones. Process Biochemistry, 44(6), 668-677. Stadtman, E. R. (1990). Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Radical Biology and Medicine, 9(4), 315-325. Stadtman, E. R., and Levine, R. L. (2003). Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino acids, 25(3-4), 207-218. Storcksdieck, S., Bonsmann, G., and Hurrell, R. F. (2007). Iron‐binding properties, amino acid composition, and structure of muscle tissue peptides from in vitro digestion of different meat sources. Journal of Food Science, 72(1). Stribling, K. V. (1997). U.S. Patent No. 5,599,570. Washington, DC: U.S. Patent and Trademark Office. Sun, J., Chen, Y., Li, M., and Ge, Z. (1998). Role of antioxidant enzymes on ionizing radiation resistance. Free Radical Biology and Medicine, 24(4), 586-593. Swatschek, D., Schatton, W., Kellermann, J., Müller, W. E., and Kreuter, J. (2002). Marine sponge collagen: isolation, characterization and effects on the skin parameters surface-pH, moisture and sebum. European Journal of Pharmaceutics and Biopharmaceutics, 53(1), 107-113. Trivedi, V., Rathore, R. P. S., Kamble, P. R., Goyal, M., and Singh, N. (2013). Pepsin, Papain and Hyaluronidase Enzyme Analysis: A Review. International Journal of Research in Pharmacy and Science, 3(1). Tang, W., Zhang, H., Wang, L., Qian, H., and Qi, X. (2015). Targeted separation of antibacterial peptide from protein hydrolysate of anchovy cooking wastewater by equilibrium dialysis. Food chemistry, 168, 115-123. Üner, N., Oruç, E. Ö., Canli, M., and Sevgler, Y. (2001). Effects of cypermethrin on antioxidant enzyme activities and lipid peroxidation in liver and kidney of the freshwater fish, Oreochromis niloticus and Cyprinus carpio L. Bulletin of environmental contamination and toxicology, 67(5), 657-664. Vishal, T., Rathore, R. P. S., Kamble, P. R., Manish, G., and Singh, N. (2013). Pepsin, Papain and Hyaluronidase Enzyme Analysis: A Review. Int. J. Res. Pharm. Sci, 3(1), 01-18. Varzakas, T. H., and Arvanitoyannis, I. S. (2010). Functional bioactive dairy ingredients (pp. 197-227). Taylor and Francis, Oxford, UK. Vázquez, J. A., Rodríguez-Amado, I., Montemayor, M. I., Fraguas, J., González, M. D. P., and Murado, M. A. (2013). Chondroitin sulfate, hyaluronic acid and chitin/chitosan production using marine waste sources: Characteristics, applications and eco-friendly processes: A review. Marine drugs, 11(3), 747-774. Vishal, T., Rathore, R. P. S., Kamble, P. R., Manish, G., and Singh, N. (2013). Pepsin, Papain and Hyaluronidase Enzyme Analysis: A Review. International Journal of Pharmaceutical Sciences and Research, 3(1), 01-18. Wang, L., An, X., Yang, F., Xin, Z., Zhao, L., and Hu, Q. (2008). Isolation and characterisation of collagens from the skin, scale and bone of deep-sea redfish (Sebastes mentella). Food chemistry, 108(2), 616-623. Wang, W., Mejia, D., and Gonzalez, E. (2005). A new frontier in soy bioactive peptides that may prevent age‐related chronic diseases. Comprehensive reviews in food science and food safety, 4(4), 63-78. Wei, A., and Shibamoto, T. (2010). Antioxidant/lipoxygenase inhibitory activities and chemical compositions of selected essential oils. Journal of agricultural and food chemistry, 58(12), 7218-7225. Wieprecht, T., Dathe, M., Beyermann, M., Krause, E., Maloy, W. L., MacDonald, D. L., and Bienert, M. (1997). Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry, 36(20), 6124-6132. Wu, H., Liu, Z., Zhao, Y., and Zeng, M. (2012). Enzymatic preparation and characterization of iron-chelating peptides from anchovy (Engraulis japonicus) muscle protein. Food research international, 48(2), 435-441. Xu, G., and Chance, M. R. (2005). Radiolytic modification of sulfur-containing amino acid residues in model peptides: fundamental studies for protein footprinting. Analytical chemistry, 77(8), 2437-2449. Yamauchi, K., Goda, T., Takeuchi, N., Einaga, H., and Tanabe, T. (2004). Preparation of collagen/calcium phosphate multilayer sheet using enzymatic mineralization. Biomaterials, 25(24), 5481-5489. You, L., Zhao, M., Cui, C., Zhao, H., and Yang, B. (2009). Effect of degree of hydrolysis on the antioxidant activity of loach (Misgurnus anguillicaudatus) protein hydrolysates. Innovative food science and emerging technologies, 10(2), 235-240. Zhang, J., Zhang, H., Wang, L., Guo, X., Wang, X., and Yao, H. (2010). Isolation and identification of antioxidative peptides from rice endosperm protein enzymatic hydrolysate by consecutive chromatography and MALDI-TOF/TOF MS/MS. Food Chemistry, 119(1), 226-234. Zhang, Y., Duan, X., and Zhuang, Y. (2012). Purification and characterization of novel antioxidant peptides from enzymatic hydrolysates of tilapia (Oreochromis niloticus) skin gelatin. Peptides, 38(1), 13-21. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/20617 | - |
dc.description.abstract | 魚鱗等副產物僅少數能再加工創造二次經濟價值,早期作為廢棄物處置,造成環境污染和社會成本增加,若能回收廢棄魚鱗中的膠原蛋白作為生物活性胜肽原料,不僅能轉變為具附加價值的產品同時降低資源的浪費。魚鱗膠原蛋白的水解胜肽被發現具有生物功能如抗氧化功能、抗菌功能、降血壓、抑制腫瘤等功能,且因界面活性表面應可用於食品乳化劑、抑制冰晶形成作為蛋白質保護劑、抑菌功能在農業上則可降低草莓灰黴病發病率。本研究使用虱目魚魚鱗以木瓜酵素水解成胜肽後進行膠原蛋白含量測試、胺基酸組成分析,同時依分子量分為大分子量 (>10kDa)、中分子量 (3-10kDa)及小分子量胜肽(<3kDa)。小分子量胜肽進行分子量測試及定序,再利用Mobyle @ RPBS Net進行其結構預測。將大中小分子量胜肽進行功能測試分別為抗氧化能力、金屬離子螯合能力、還原力、抑菌率及最小抑菌濃度測試。結果指出,虱目魚鱗的膠原蛋白含量為12%,其中 Gly、Pro、Hyp 胺基酸含量最高,分別為27%、11%、10.4%。小分子胜肽分子量介於567-2775 Da間,其中胜肽2693含27個胺基酸,序列為KPTKDGVTVAVISGEALGIKICFTSTG,有40%的疏水性胺基酸且帶電量為+1,結構為β-sheet,構型特殊因此委託明欣生技公司合成。虱目魚魚鱗胜肽、>10kDa、3-10kDa、<3kDa及胜肽2693抗氧化能力(DPPH自由基清除能力,濃度1μg/ml)分別為51.27%、41.28%、63.98%、64.20%及52.01%,亞鐵離子螯合能力(freeozine model,EDTA濃度1μg/ml) 分別為40.93%、75.99%、68.09%、5.76%但胜肽2693無亞鐵離子螯合能力;還原力結果(FRAP,EDTA1 μg/ml)分別為10.26%、17.18%、14.11%、8.66%及3.06%, <3kDa及2693 peptide對金黃色葡萄球菌(Staphylococcus aureus)最小抑菌濃度(MIC)結果為7μg/ml (83.3%)及15-30μg/ml (84.3%),其餘無抑菌能力。虱目魚鱗膠原蛋白胜肽含多種生物活性胜證實能成功的將水產品廢棄物有效利用,未來可發展醫療、食品等產業,則可針對胜肽的功能性來選擇蛋白酵素分離不同分子量的胜肽。 | zh_TW |
dc.description.abstract | The hydrolyzed peptides of fish scale collagen are founded to have biological function such as antioxidant activity, antibacterial activity, lowering blood pressure, inhibiting tumor and so on… In this study, milkfish scales are used. The collagen content of milkfish scale are analyzed by soften the fish scale and hydrolyze the fish scale into collagen peptide. The compositions of amino acid are divided into three groups based on the molecular weight: high molecular peptides (>10kDa), medium molecular weight peptides (3-10kDa) and small molecular weight peptides (<3kDa). The molecular weight distribution of MALDI-TOF / MS is measured by small molecular weight peptides and its structure is predicted by Mobyle @ RPBS Net. The result shows that the content of collagen was 12%, and the contents of Gly, Pro and Hyp were 27%, 11% and 10.4% respectively. The molecular weight of the small molecule peptide is between 567-2775, in which the peptide 2693 contains 27 amino acids and the sequence is KPTKDGVTVAVISGEALGIKICFTSTG. There is 40% hydrophobic amino acid and the charge is +1 and the structure is β-sheet. The antioxidant capacity of milkfish peptide, >10kDa, 3-10kDa, <3kDa and peptide 2693 were 51.27%, 41.28%, 63.98%, 64.20% and 52.01%, respectively. The ferrous ion chelating ability was 40.93%, 75.99%, 68.09%, 5.76%, respectively, while peptide 2693 doesn’t have such ability. And the result of recovering is 10.26%, 17.18%, 14.11%, 8.66% and 3.06%, respectively. As for <3kDa and 2693 peptide, the minimum inhibitory concentration of Staphylococcus aureus
was 7μg / ml (83.3%) and 15-30μg / ml (84.3%). The milkfish peptide produces biologically active peptides by different proteases. The differences of these biologically active peptides are depending on the different molecular weight, amino acid composition and stereospecific structure. The more hydrophobic amino acids and intramolecular hydrogen bonds are more possible to enhance antioxidant activity. The larger space of three-dimensional structure of peptide ensures more metal ions. There is more than 40% hydrophobic amino acid and positive charage in <3kDa small molecules. According to the simulation interaction between peptides 2693 and bacterial cell, we presume that the bacteria are the barrel-attack type of cell membrane. Milkfish scale peptide containing several of biological activities are verifying the effective using of aquatic waste. It is possible that fish scale peptide are using in medical, food and other industries in the future development. | en |
dc.description.provenance | Made available in DSpace on 2021-06-08T02:55:35Z (GMT). No. of bitstreams: 1 ntu-106-R03b45013-1.pdf: 2899706 bytes, checksum: 0f26665f805a53bb8e476f39692772f5 (MD5) Previous issue date: 2017 | en |
dc.description.tableofcontents | 謝辭 iii
中文摘要 vi Abstract vii 目錄 viii 表目錄 x 圖目錄 xi 第一章 前言 1 一、 研究背景 1 二、 魚鱗膠原蛋白 2 三、 膠原蛋白生物活性胜肽 3 (一) 抗氧化活性 4 (二) 金屬離子螯合活性 7 (三) 抗微生物活性 8 四、 魚類生物活性胜肽應用 9 五、 研究興趣及目的 10 第二章 材料與方法 12 一、 材料 12 二、 方法 12 (一) 魚鱗處理 12 (二) 膠原蛋白含量分析 13 (三) 胺基酸組成分析方法 14 (四) 分子量分析 15 (五) 胺基酸定序分析 16 (六) 結構預測 17 (七) 抗氧化活性測試 18 (八) 抗微生物活性測試 20 (九) 2693胜肽合成方法 20 (十) 統計檢定 21 第三章 結果 22 第四章 討論 25 (一) 酸鹼處理與與酵素 28 (二) 抗氧化活性 29 (三) 亞鐵離子螯合活性 31 (四) 還原活性 32 (五) 抗微生物活性 32 第五章 結論 35 表 36 圖 45 參考文獻 64 表目錄 表1. 虱目魚鱗萃取膠原蛋白含量 36 表2. 虱目魚鱗萃取胜肽胺基酸組成 37 表3. 虱目魚鱗萃取胜肽(<3kDa)分子量 38 表4. 胜肽2219胺基酸組成 39 表5. 胜肽2693胺基酸組成 40 表6. 不同分子量胜肽功能比較表 41 表7. 物種別萃取胜肽之結構與清除自由基能力比較表 42 表8. 物種別萃取胜肽之結構與亞鐵離子螯合能力比較表 43 表9. 物種別萃取胜肽之結構與抑菌能力比較表 44 圖目錄 圖1. 實驗操作流程圖 45 圖2. 羥基哺胺酸濃度與吸光值標準曲線 46 圖3. 魚鱗膠原蛋白胜肽m/z與強度之分布全圖(500-4000m/z) 47 圖4. 魚鱗膠原蛋白胜肽m/z與強度之分布圖(500-2000m/z) 48 圖5. 魚鱗膠原蛋白胜肽m/z與強度之分布圖(2000-4000m/z) 49 圖6. 魚鱗膠原蛋白胜肽中2219定序結果圖 50 圖7. 魚鱗膠原蛋白胜肽中2693定序結果圖 51 圖8. 胜肽2219序列與構型機率分布圖 52 圖9. 胜肽2693序列與構型機率分布圖 53 圖10. 胜肽2219分子模擬圖 54 圖11. 胜肽2693 分子模擬圖 55 圖12. 虱目魚鱗膠原蛋白萃取胜肽自由基清除能力(%) 56 圖13. 虱目魚鱗膠原蛋白萃取胜肽亞鐵離子螯合能力(%) 57 圖14. 虱目魚鱗膠原蛋白萃取胜肽還原能力(%) 58 圖15. 虱目魚鱗膠原蛋白萃取胜肽抑菌能力(%) 59 圖16. 胜肽2693與細菌細胞膜交互作用模擬圖 60 圖17. 胜肽結構與清除自由基能力比較圖 61 圖18. 胜肽結構與亞鐵離子螯合能力比較圖 62 圖19. 胜肽結構與抑菌率比較圖 63 | |
dc.language.iso | zh-TW | |
dc.title | 虱目魚鱗胜肽衍生物之生物功能性分析 | zh_TW |
dc.title | Biological function analysis of the peptides derivatives
from milkfish(Chanos chanos) scales | en |
dc.type | Thesis | |
dc.date.schoolyear | 105-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 李宗徽(Tzong-Huei Lee),陳志毅(Jyh-Yih CHEN),黃美瑩(Mei-Ying Huang) | |
dc.subject.keyword | 抗氧化活性,金屬螯合活性,最小抑菌濃度,木瓜蛋白酵素, | zh_TW |
dc.subject.keyword | Antioxidant activity,Iron chelating activity,Minimum inhibitory concentration,Papain, | en |
dc.relation.page | 74 | |
dc.identifier.doi | 10.6342/NTU201702497 | |
dc.rights.note | 未授權 | |
dc.date.accepted | 2017-08-04 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 漁業科學研究所 | zh_TW |
顯示於系所單位: | 漁業科學研究所 |
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