Processing and Industrial Aspects of Fish-scale Collagen: A Biomaterials Perspective
Santanu Dhara
Biomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India
Search for more papers by this authorPallab Datta
Biomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India
Search for more papers by this authorPallabi Pal
Biomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India
Search for more papers by this authorSoumi Dey Sarkar
Biomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India
Search for more papers by this authorSantanu Dhara
Biomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India
Search for more papers by this authorPallab Datta
Biomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India
Search for more papers by this authorPallabi Pal
Biomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India
Search for more papers by this authorSoumi Dey Sarkar
Biomaterials and Tissue Engineering Laboratory, School of Medical Science and Technology, Indian Institute of Technology, Kharagpur, India
Search for more papers by this authorSe-Kwon Kim
Marine Bioprocess Research Center, Pukyong National University, Busan, Republic of Korea
Department of Chemistry, Pukyoung National University, Nam-Gu, Busan, Republic of Korea
Search for more papers by this authorSummary
Marine animals are emerging as a leading resource for the identification and extraction bioactive peptides. These peptides have been described as a source of pharmaceutical products with beneficial effects of humans. Beyond their basic nutritional roles, peptides are involved in many processes in living organisms, based on their function as hormones, neuropeptides, alkaloids, antibiotics, toxins and regulation peptides. Studies are underway to explore further sources of these marine peptides, especially from underutilized marine-processing byproducts. Their bioavailabilities, possible physiological functions and mechanisms of action are also being investigated. Much attention has been paid to unraveling the structural, compositional and sequential properties of bioactive peptides. Marine bioactive peptides may be produced by one of three methods: solvent extraction, enzymatic hydrolysis, and microbial fermentation of food proteins. The enzymatic-hydrolysis method is preferred in the food and pharmaceutical industries because of the lack of residual organic solvents and toxic chemicals in its products.
References
- Aberoumand, A. (2012). Comparative study between different methods of collagen extraction from fish and its properties. World Applied Sciences Journal, 16, 319–319.
- Addad, S. et al. (2011). Isolation, characterization and biological evaluation of jellyfish collagen for use in biomedical applications. Marine Drugs, 9, 967–983.
- Ahmad, M., Benjakul, S. (2010). Extraction and characterisation of pepsin-solubilised collagen from the skin of unicorn leatherjacket (Aluterus monocerous). Food Chemistry, 120, 817–824.
- Ahmad, M., Benjakul, S., Nalinanon, S. (2010). Compositional and physicochemical characteristics of acid solubilized collagen extracted from the skin of unicorn leatherjacket (Aluterus monoceros). Food Hydrocolloids, 24, 588–594.
- Akbal, C. et al. (2006). Bladder augmentation with acellular dermal biomatrix in a diseased animal model. Journal of Urology, 176, 1706–1711.
- Angele, P. et al. (2004). Influence of different collagen species on physico-chemical properties of crosslinked collagen matrices. Biomaterials, 25, 2831–2841.
- Auger, F. A. et al. (1998). Tissue-engineered human skin substitutes developed from collagen populated hydrated gels: clinical and fundamental applications. Medical & Biological Engineering & Computing, 36, 801–812.
- Aumailley, M., Gayraud, B. (1998). Structure and biological activity of the extracellular matrix. Journal of Molecular Medicine, 76, 253–265.
-
Avery, N. C., Bailey, A. J. (2008). Restraining Cross-Links Responsible for the Mechanical Properties of Collagen Fibers: Natural and Artificial. In: P. Fratzl, ed. Collagen: Structure and Mechanics. Springer Science + Business Media.
10.1007/978-0-387-73906-9_4 Google Scholar
- Bae, I. et al. (2008). Biochemical properties of acid-soluble collagens extracted from the skins of underutilised fishes. Food Chemistry, 108(49–54).
- Bama, P. et al. (2010). Extraction of collagen from cat fish (Tachysurus maculatus) by pepsin digestion and preparation and characterization of collagen chitosan sheet. International Journal of Pharmacy and Pharmaceutical Sciences, 2.
- Bechetoille, N. et al. (2007). Effects of solar ultraviolet radiation on engineered human skin equivalent containing both Langerhans cells and dermal dendritic cells. Tissue Engineering, 13, 2667–2679.
- Bender, A. et al. (1996). Efficiency of nanoparticles as a carrier system for antiviral agents in human monocytes/macrophages in vitro. Antimicrobial Agents and Chemotherapy, 40, 1467–1471.
- Beveridge, J. M. R., Lucas, C. C. (1944). Amino acids of isinglass. The Journal of Biological Chemistry, 155, 547–556.
- Blais, M., Grenier, M., Berthod, F. (2009). Improvement of nerve regeneration in tissue-engineered skin enriched with schwann cells. Journal of Investigative Dermatology, 129, 2895–2900.
- Brodsky, B. et al. (2005). Molecular structure of the collagen triple helix. Adv Protein Chem, 70, 301–339.
- Brodsky, B., Ramshaw, J. A. M. (1997). The collagen triple-helix structure. Matrix Biolage, 15, 545–554.
- Brown, E. M. et al. (2000). Influence of neutral salts on the hydrothermal stability of acidsoluble collagen. Journal of Protein Chemistry, 19, 85–92.
- Burghagen (1999). Collagen. In: H. D. Belitz, W. Grosch, eds. Food Chemistry. Springer-Verlag: Berlin, Heidelberg. pp. 540–547.
-
Burjanadze, T. V. (2000). New analysis of the phylogenetic change of collagen thermostability. Biopolymers, 53, 523–528.
10.1002/(SICI)1097-0282(200005)53:6<523::AID-BIP8>3.0.CO;2-7 CAS PubMed Web of Science® Google Scholar
- Caissie, R. et al. (2006). In vivo enhancement of sensory perception recovery in a tissue engineered skin enriched with laminin. Biomaterials, 27, 2988–2993.
- Che, Z. M. et al. (2006). Collagen-based coculture for invasive study on cancer cells-fibroblasts interaction. Biochemical and Biophysical Research Communications, 346, 268–275.
- Chen, L. et al. (2011). Extraction and partial characterization of pepsin-soluble collagens from the skin of Amiurus nebulosus. Advanced Materials Research, 236–238, 2926–2934.
- Cliche, S. et al. (2003). Extraction and characterization of collagen with or without telopeptides from chicken skin. Poultry Science, 82, 503–509.
- Cluzel, C. et al. (2000). Sea urchin fibrillar collagen 2α chain participates in heterotrimeric molecules of (1α)22α stoichiometry. Matrix Biology, 19, 545–547.
- Cohen-Solal, L. et al. (1981). Absence of maturation of collagen crosslinks in fish skin. FEBS Letters, 123, 282–284.
- Corriveau, M. P. et al. (2009). The fibrotic phenotype of systemic sclerosis fibroblasts varies with disease duration and severity of skin involvement: Reconstitution of skin fibrosis development using a tissue engineering approach. Journal of Pathology, 217, 534–542.
- Cui, F.-X. et al. (2007). Characterization and subunit composition of collagen from the body wall of sea cucumber Stichopus japonicus. Food Chemistry, 100, 1120–1125.
- Damodaran, S., Paraf, A. (1997). Food Proteins and Their Applications. Marcel Dekker: New York, pp. 356–359.
- DeVore, D. P. (1995). Collagen as an ophthalmic biomaterial. In: D. L Wise. et al., eds. Encyclopedic Handbook of Biomaterials and Bioengineering. Marcel Dekker: New York, pp. 1233–1260.
- Dhara, S., Adhikari, B., Pati, F. (2011) A process for production of collagen and by-products from fresh water fish origin and applications thereof: complete application submitted. Patent number 212/KOL/2011.
- Doillon, C. J., Silver, F. H. (1986). Collagen-based wound dressing: effects of hyaluronic acid and fibronectin on wound healing. Biomaterials, 7, 3–8.
- Duan, R. et al. (2009). Properties of collagen from skin, scale and bone of carp (Cyprinus carpio). Food Chemistry, 112, 702–706.
- Eastoe, J. E. (1956). The Amino Acid Composition of Fish Collagen and Gelatin. The British Gelatine and Glue Research Association, London.
-
Edwards, G. A. et al. (1997). In vivo evaluation of a collagenous membrane as an absorbable adhesion barrier. Journal of Biomedical Materials Research, 34, 291–297.
10.1002/(SICI)1097-4636(19970305)34:3<291::AID-JBM3>3.0.CO;2-F CAS PubMed Web of Science® Google Scholar
- el-Kassaby, A., AbouShwareb, T., Atala, A. (2008). Randomized comparative study between buccal mucosal and acellular bladder matrix grafts in complex anterior urethral strictures. Journal of Urology, 179, 1432–1436.
- Engel, J. (1987). Folding and unfolding of collagen triple helices. Advances in Meat Research, 4, 145–161.
- Farahat, Y. A. et al. (2009). Endoscopic urethroplasty using small intestinal submucosal patch in cases of recurrent urethral stricture: a preliminary study. Journal of Endourology, 23, 2001–2005.
- Fiala, R. et al. (2007). Porcine small intestinal submucosa graft for repair of anterior urethral strictures. European Urology, 51, 1702–1708.
- Foegeding, E., Lanier, T. C., Hultin, H. O. (1996). Characteristics of edible muscle tissue. In: O. R. Fennema, ed. Food Chemistry. Marcel Dekker: New York, pp. 879–942.
- Francois, J., Herbage, D., Junqua, S. (1980). Cockroach collagen: isolation, biochemical and biophysical characterization. European Journal of Biochemistry, 112, 389–396.
- Fraser, R. D., MacRae, T. P., Suzuki, E. (1979). Chain conformation in the collagen molecule. Journal of Molecular Biology, 129, 463–481.
- Friess, W. (1998). Collagen-biomaterial for drug delivery. European Journal of Pharmaceutics and Biopharmaceutics, 45, 113–136.
- Fujioka, K. et al. (1998). Protein release from collagen matrices. Advanced Drug Delivery Reviews, 31, 247–266.
- Gelsea, K., Pöschlb, E., Aigner, T. (2003). Collagens—structure, function, and biosynthesis. Advanced Drug Delivery Reviews, 55, 1531–1546.
- Gingras, M. et al. (2008). In vitro study of axonal migration and myelination of motor neurons in a three-dimensional tissue-engineered model. Glia, 56, 354–364.
- Gudmundsson, M., Hafsteinsson, H. (1997). Gelatin from cod skins as affected by chemical treatments. Journal of Food Science and Technology, 62, 33–39.
- Gurdak, E. et al. (2006). Influence of collagen denaturation on the nanoscale organization of adsorbed layers. Journal of Colloid and Interface Science, 302, 475–484.
- Hao, L., Li, B. (1999). Extraction of collagen from body wall of Asterias amurensis. Journal of Fishery Sciences of China, 6, 18–21.
-
Heidemann, E., Roth, W. (1982). Synthesis and investigation of collagen model peptides. Advances in Polymer Science, 42, 143–203.
10.1007/3-540-11048-8_3 Google Scholar
- Heino, J. (2000). The collagen receptor integrins have distinct ligand recognition and signaling functions. Matrix Biology, 19, 319–323.
- Heu, M. S. et al. (2010). Characterization of acid- and pepsin-soluble collagens from flatfish skin. Food Science Biotechnology, 19, 27–33.
- Hofmann, H., Fietzek, P. P., Kuhn, K. (1978). The role of polar and hydrophobic interactions for the molecular packing of type I collagen: a three-dimensional evaluation of the amino acid sequence. Journal of Molecular Biology, 125, 137–165.
- Hsu, F. Y., Chueh, S. C. (1999). Microspheres of hydroxyapatite/reconstituted collagen as supports for osteoblast cell growth. Biomaterials, 20, 1931–1936.
- Huang, Y. C. et al. (2005). Epidermal morphogenesis in an in-vitro model using a fibroblastsembedded collagen scaffold. Journal of Biomedical Science, 12, 855–867.
- Huang, Y.-R. et al. (2011). Isolation and characterization of acid and pepsin-solubilized collagens from the skin of balloon fish (Diodon holocanthus). Food Hydrocolloids, 25, 1507–1513.
-
Hulmes, D. J. S. (2008). Collagen diversity, synthesis and assembly. In: P. Fratzl, ed. Collagen: Structure and Mechanics. Springer Science + Business Media.
10.1007/978-0-387-73906-9_2 Google Scholar
- Hwang, J. H. et al. (2007). Purification and characterization of molecular species of collagen in the skin of skate (Raja kenojei). Food Chemistry, 100, 921–925.
- Ikoma, T. et al. (2003). Physical properties of type I collagen extracted from fish scales of Pagrus major and Oreochromis niloticas. International Journal of Biological Macromolecules, 32, 199–204.
- Jean, J. et al. (2009). Development of an in vitro psoriatic skin model by tissue engineering. Journal of Dermatological Science, 53, 19–25.
- Jerome, A., Ramshaw, J. A. M. (1995). Collagen-based biomaterials. Biotechnology and Genetic Engineering Reviews, 9, 137–139.
- Jongjareonrak, A. et al. (2005). Isolation and characterisation of acid and pepsin-solubilised collagens from the skin of Brownstripe red snapper (Lutjanus vitta). Food Chemistry, 93, 475–484.
- Kadler, K. E. et al. (2007). Collagens at a glance. J Cell Sci, 120, 1955–1958.
- Kadler, K. E. et al. (1996). Collagen fibril formation. Biochem. J., 316, 1–11.
- Khan, S. B. et al. (2009). Isolation and biochemical characterization of collagens from seaweed pipefish, Syngnathus schlegeli. Biotechnology and Bioprocess Engineering, 14, 436–442.
- Kimura, S., Tanaka, H. (1983). Characterization of top shell muscle collagen comprising three identical α 1 chains. Bulletin of the Japanese Society of Scientific Fisheries, 49, 229–232.
- Kimura, S. et al. (1988). Characterization of fish muscle type I collagen. Journal of Food Science, 53, 1315–1318.
- Kimura, S. (1992). Wide distribution of the skin type I collagen α3 chain in bony fish. Comp Biochem Physiol, 102, 780–786.
- Kimura, S. et al. (1987). Fish skin type I collagen: wide distribution of an α3 subunit in teleosts. Comparative Biochemistry and Physiology, 88, 27–34.
- Kimura, S., Miyauchi, Y., Uchida, N. (1991). Scale and bone type I collagens of carp (Cyprinus carpio). Comparative Biochemistry and Physiology, 99, 473–476.
- Kimura, S., Takema, Y., Kubota, M. (1981). Octopus skin collagen: isolation and characterization of collagen comprising two distinct (α chains). The Journal of Biological Chemistry, 256, 13230–13234.
- Kittiphattanabawon, P. et al. (2005). Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chemistry, 89, 363–372.
- Kittiphattanabawon, P. et al. (2010a). Isolation and characterisation of collagen from the skin of brownbanded bamboo shark (Chiloscyllium punctatum). Food Chemistry, 119, 1519–1526.
- Kittiphattanabawon, P. et al. (2010b). Isolation and characterization of collagen from the cartilages of brownbanded bamboo shark (Chiloscyllium punctatum) and blacktip shark (Carcharhinus limbatus). Food Science and Technology, 43, 792–800.
- Klomklao, S. S., Visessanguan, W. (2004). Comparative studies on proteolytic activity of splenic extract from three tuna species commonly used in Thailand. Journal of Food Biochemistry, 28, 355–372.
- Komsa-Penkova, R. et al. (1999). Discrete reduction of type I collagen thermal stability upon oxidation. Biophysical Chemistry, 83, 185–195.
- Lee, C. H., Singla, A. (2001). Biomedical applications of collagen. Int. J. Pharm., 221, 1–22.
- Lee, K.-J. et al. (2009). Biochemical characterization of collagen from the starfish Asterias amurensis. Journal of the Korean Society for Applied Biological Chemistry, 52, 221–226.
- Lewis, M. S., Piez, K. A. (1964). The characterization of collagen from the skin of the dogfish shark, Sgualus acanthias. Journal of Biological Chemistry, 239.
- Li, C.-M. et al. (2008). Preparation and thermal stability of collagen from scales of grass carp (Ctenopharyngodon idellus). European Food Research and Technology, 227, 1467–1473.
- Lina, Y. S. et al. (2011). Mechanical properties and the laminate structure of Arapaima gigas scales. Journal of the Mechanical Behavior of Biomedical Materials, 4, 1145–1156.
- Liu, D. (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).
- Liu, H., Li, D., Guo, S. (2007). Studies on collagen from the skin of channel catfish (Ictalurus punctaus). Food Chemistry, 101.
- Liu, Y. et al. (2009). Optimization of a natural collagen scaffold to aid cell-matrix penetration for urologic tissue engineering. Biomaterials, 30, 3865–3873.
- Love, R. M. et al. (1976). The connective tissue and collagen of cod during starvation. Comparative Biochemistry and Physiology Part B, 55, 487–492.
- Lullo, G. A. D. et al. (2002). Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. Journal of Biological Chemistry, 277, 4223–4231.
- Lynn A. K., Yannas I. V. (2004). Antigenity and immunogenicity of collagen. J Biomed Mater Res Part B Appl Biomater, 71B, 343–353.
- Ma, W. et al. (2004). CNS stem and progenitor cell differentiation into functional neuronal circuits in three-dimensional collagen gels. Experimental Neurology, 190, 276–288.
- Marty, J. J., Openheim, R.C., Speiser, P. (1978). Nanoparticles a new colloidal drug delivery system. Pharmaceutica Acta Helvetiae, 53, 17–23.
- Mingyan, Y., Bafang, L., Xue, Z. (2009). Isolation and characterization of collagen from squid (Ommastrephes bartrami) skin. Journal of Ocean University of China, 8, 191–196.
- Miyauchi, Y., Kimura, S. (1990). Characterization of an α3 chain from carp skin type I collagen. Nippon Suisan Gakkaishi, 56, 1509–1514.
- Mizuta, S. et al. (1992). Subunit composition of distinct types of collagens in the muscle of the kuruma prawn Penaeus japonicus. Comparative Biochemistry and Physiology, 102, 803–811.
- Mizuta, S. et al. (1994a). Isolation and partial characterization of two distinct types of collagen in the muscle and skin of the squid Todarodes pacificus. Fisheries Science, 60, 467–471.
- Mizuta, S. et al. (1994b). Subunit composition of two distinct types of collagen in the muscle of the squid Todarodes pacificus. Fisheries Science, 60, 597–602.
- Mizuta, S. et al. (2002). Partial characterization of collagen in mantle and adductor of pearl oyster (Pinctada fucata). Food Chemistry, 79, 319–325.
- Mizuta, S. et al. (2005). Biochemical and immunochemical detection of types I and V collagens in tiger puffer Takifugu rubripes. Food Chemistry, 89, 373–377.
- Montero, P. et al. (1990). Characterization of hake (Merluccius merluccius L.) and trout (Salmo irideus Gibb) collagen. Journal of Agricultural and Food Chemistry, 38, 604–609.
- Montero, P. et al. (1995). Plaice skin collagen extraction and functional properties. Journal of Food Science, 60, 1–3.
- Muralidharan, N. et al. (2011). Skin, bone and muscle collagen extraction from the trash fish, leather jacket (Odonus niger) and their characterization. Journal of Food Science and Technology.
- Murata, M. et al. (1999). Bone augmentation by recombinant human BMP-2 and collagen on adult rat parietal bone. International Journal of Oral and Maxillofacial Surgery, 28, 232–237.
- Muyonga J. H., Cole C. G. B. (2004). Characterization of acid soluble collagen from skins of young and adult Nile perch (Lates niloticus). Food Chemistry, 85, 81–89.
- Myllyharju, J. et al. (2004). Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet, 20, 33–43.
- Myllyharju, J. (2000). Recombinant collagen trimers from insect cells and yeast. Methods in Molecular Biology, 139, 39–48.
- Nagai, T., Suzuki, N. (2000a). Isolation of collagen from fish waste material—skin, bone and fins. Food Chemistry, 68, 277–281.
- Nagai, T., Suzuki, N. (2000b). Partial characterization of collagen from purple sea urchin (Anthocidaris crassispina) test. International Journal of Food Science and Technology, 35, 497–401.
- Nagai, T., Suzuki, N. (2000c). Preparation and characterization of several fish bone collagens. Journal of Food Biochemistry, 24, 427–436.
- Nagai, T., Suzuki, N. (2002a). Preparation and partial characterization of collagen from paper nautilus (Argonauta argo, Linnaeus) outer skin. Food Chemistry, 76, 149–153.
- Nagai, T., Suzuki, N. (2002b). Collagen from the underutilized resources of aquatic organisms. In: T. Brittain et al., eds. Trends in Comparative Biochemistry and Physiology. Research Trends: India, pp. 259–268.
- Nagai, T. (2004a). Characterization of collagen from Japanese sea bass caudal fin as waste material. European Food Research and Technology, 218, 424–427.
- Nagai, T. (2004b). Collagen from diamondback squid (Thysanoteuthis rhombus) outer skin. Zeitschrift für Naturforschung, 59, 271–275.
-
Nagai, T. et al. (1999). Collagen of edible jellyfish exumbrella. Journal of the Science of Food and Agriculture, 79, 855–858.
10.1002/(SICI)1097-0010(19990501)79:6<855::AID-JSFA299>3.0.CO;2-N CAS Web of Science® Google Scholar
- Nagai, T. et al. (2000). Isolation and characterization of collagen from rhizostomous jellyfish (Rhopilema asamushi). Food Chemistry, 70, 205–208.
- Nagai, T. et al. (2001a). Collagen of octopus Callistoctopus arakawai arm. International Journal of Food Science and Technology.
- Nagai, T. et al. (2001b). Isolation and characterisation of collagen from the outer skin waste material of cuttlefish (Sepia lycidas). Food Chemistry, 72, 425–429.
- Nagaia, T., Arakib, Y., Suzukia, N. (2002). Collagen of the skin of ocellate puffer fish (Takifugu rubripes). Food Chemistry, 78.
- Nagai, T., Izumi, M., Ishii, M. (2004). Fish scale collagen. Preparation and partial characterization. Journal of Food Science and Technology, 39, 239–244.
- Nagai, T., Suzuki, N., Nagashima, T. (2008). Collagen from common minke whale (Balaenoptera acutorostrata) unesu. Food Chemistry, 111, 296–301.
- Nagai, T. et al. (2010). Characterization of acid-soluble collagen from skins of surf smelt (Hypomesus pretiosus japonicus Brevoort). Food and Nutrition Sciences, 1, 59–66.
- Nalinanon, S. et al. (2011). Type I collagen from the skin of ornate threadfin bream (Nemipterus hexodon): characteristics and effect of pepsin hydrolysis. Food Chemistry, 125, 500–507.
- Nalinanon, S. et al. (2007). Use of pepsin for collagen extraction from the skin of bigeye snapper (Priacanthus tayenus). Food Chemistry, 104, 593–601.
- Neuman, R. E. (1949). The amino acid composition of gelatins, collagens and elastins from different sources. Archives of Biochemistry, 24, 289.
- O'Leary, R., Wood, E. J. (2003). A novel in vitro dermal woundhealing model incorporating a response to mechanical wounding and repopulation of a fibrin provisional matrix. In Vitro Cellular & Developmental Biology—Animal, 39, 204–207.
- Ogawa, M. et al. (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, 495–501.
- Ogawa, M. et al. (2003). Biochemical properties of black drum and sheepshead seabream skin collagen. Journal of Agricultural and Food Chemistry, 51, 8088–8092.
- Olsena D et al. (2003). Recombinant collagen and gelatin for drug delivery. Advance Drug Delivery Reviews, 55, 1547–1567.
- O'Shaughnessy, T. J., Lin, H. J., Ma, W. (2003). Functional synapse formation among rat cortical neurons grown on three-dimensional collagen gels. Neuroscience Letter, 340, 169–172.
- Parenteau-Bareil, R., Gauvin, R., Berthod, F. (2010). Collagen-based biomaterials for tissue engineering applications. Materials, 3, 1863–1887.
- Park, S.-Y. et al. (2012). Pepsin-solubilised collagen (PSC) from Red Sea cucumber (Stichopus japonicus) regulates cell cycle and the fibronectin synthesis in HaCaT cell migration. Food Chemistry, 132, 487–492.
- Pati, F. (2011). Collagen chitosan based fibrous scaffolds for tissue engineering application. School of Medical Science and Technology, Indian Institute of Technology, Kharagpur.
- Pati, F., Adhikari, B., Dhara, S. (2010). Isolation and characterization of fish scale collagen of higher thermal stability. Bioresource Technology, 101, 3737–3742.
- Pati, F. et al. (2012). Collagen scaffolds derived from fresh water fish origin and their biocompatibility. Journal of Biomedical Materials Research Part A, 100A, 1068–1079.
- Payne, K. J., Veis, A. (1988). Fourier transform IR spectroscopy of collagen and gelatin solutions: deconvolution of the amide I band for conformational studies. Bioploymers, 27, 1749–1760.
- Peters, W. J. (1980). Biological dressings in burns—a review. Annals of Plastic Surgery, 4, 133–137.
- Piez, K. A., Eigner, E. A., Lewis, M. S. (1963). The chromatographic separation and amino acid composition of the subunits of several collagens. Biochemistry, 2, 58–66.
- Prystupa, D. A., Donald, A. M. (1996). Infrared study of gelatin conformations in the gel and sol states. Polymer Gels and Networks, 4, 87–110.
- Purna, S. K., Babu, M. (2000). Collagen based dressings—a review. Burns, 26(1), 54–62.
- Rama, S., Chandrakasan, G. (1984). Distribution of different molecular species of collagen in the vertebral cartilage of shark (Carcharius acutus). Connective Tissue Research, 12, 111–118.
- Ramachandran, G. N. (1988). Stereochemistry of collagen. Journal of Peptide and Protein Research, 31, 1–16.
- Ramachandran, G. N. (1956). Structure of Collagen Nature, 177, 710–711.
- Ramshaw, J. A. M., Shah, N. K., Brodsky, B. (1998). Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides. Structural Biology, 122, 86–91.
- Rangaraj, A., Harding, K., Leaper, D. (2011). Role of collagen in wound management. Wounds, 7(2), 54–63.
- Rao, K.P. (1995). Recent developments of collagen-based materials for medical applications and drug delivery systems. Journal of Biomaterial Science, 7, 623–645.
- Reddi, A. H. (2000). Morphogenesis and tissue engineering of bone and cartilage: inductive signals, stem cells, and biomimetic biomaterials. Tissue Engineering, 6, 351–359.
- Regnier, M. et al. (1997). Integration of Langerhans cells into a pigmented reconstructed human epidermis. Journal of Investigative Dermatology, 109, 510–512.
- Ricard-Blum, S., Ruggiero, F. (2005). The collagen superfamily. Top Curr Chem, 247, 35–84.
- Rigby, B. J. (1968). Amino-acid composition and thermal stability of the skin collagen of the Antarctic ice-fish. Nature, 219, 166–167.
- Rodziewicz-Motowidło, S. et al. (2008). Isolation and characterization of a thermally stable collagen preparation from the outer skin of the silver carp Hypophthalmichthys molitrix. Aquaculture, 285, 130–134.
- Rossler, B., Kreuter, J., Scherer, D. (1995). Collagen microparticles: preparation and properties. Journal of Microencapsulation, 12, 49–57.
- Ruszczak, Z. (2003). Effect of collagen matrices on dermal wound healing. Advanced Drug Delivery Reviews, 55, 1595–1611.
- Sabeh, F., Shimizu-Hirota, R., Weiss, S. J. (2009). Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited. Journal of Cell Biology, 185, 11–19.
- Sadowska, M., Koodziejska, I., Niecikowska, C. (2003). Isolation of collagen from the skins of Baltic cod (Gadus morhua). Food Chemistry, 81, 257–262.
- Sai, K. P., Babu, M. (2001). Studies on Rana tigerina skin collagen. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 128, 81–90.
- Sato, K. et al. (2000). Possible involvement of aminotelopeptide in self-assembly and thermal stability of collagen I as revealed by its removal with proteases. Journal of Biological Chemistry, 275, 25870–25875.
- Senaratne, L. S., Park, P. J., Kim, S. K. (2006). Isolation and characterization of collagen from brown backed toadfish (Lagocephalus gloveri) skin. Bioresource Technology, 97, 191–197.
-
Shadwick, R. E. (1985). Crosslinking and chemical characterization of cephalopod collagens. In: A. Bairati, R. Garrone, eds. Biology of Invertebrate and Lower Vertebrate Collagens. Plenum Press: New York, pp. 337–343.
10.1007/978-1-4684-7636-1_31 Google Scholar
- Sikorski, Z. E., Kolakowska, A., Pan, B. S. (1990). The nutritive composition of the major groups of marine food organisms. In: Z. E. Sikorski, eds. Seafood: Resources, Nutritional Composition and Preservation. CRC Press: Florida, pp. 29–54.
- Singh, P. et al. (2011). Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chemistry, 124, 97–105.
- Soiderer, E. E. et al. (2004). Morphologic study of three collagen materials for body wall repair. J Surg Res, 118, 161–175.
- Songa, E. et al. (2006). Collagen scaffolds derived from a marine source and their biocompatibility. Biomaterials, 27, 2951–2961.
- Spiro, R. C. et al. (2002). Recombinant human collagens for bone & cartilage repair. European Cells and Materials, 4, 16.
- Steinberg, R. H. F., John, S. (2009). Collagen in wound healing: are we onto something new or just repeating the past? The Foot and Ankle Online Journal, 2(9). Available from http://faoj.org/2009/09/01/collagen-in-wound-healing-are-we-onto-something-new-or-just-repeating-the-past/, last accessed November 8, 2012.
- Swatscheka, D. et al. (2002). Marine sponge collagen: isolation, characterization and effects on the skin parameters surface-pH, moisture and sebum. European Journal of Pharmaceutics and Biopharmaceutics, 53, 107–113.
- Takahashi, T., Yokoyama, W. (1954). Physico-chemical studies on the skin and leather of marine animals—XII. The content of hydroxyproline in the collagen of different fish skins. Bulletin of the Japanese Society of Scientific Fisheries (in Japanese), 20, 525–529.
- Techatanawata, S. et al. (2011). Type I collagen extracted from rat-tail and bovine Achilles tendon for dental application: a comparative study. Asian Biomedicine, 5, 787–798.
- Tomita, M. et al. T(2003). Ransgenic silkworms produce recombinant human type III procollagen in cocoons. Nature Biotechnology, 21.
- Tremblay, P. L. et al. (2005). Inosculation of tissue engineered capillaries with the host'S vasculature in a reconstructed skin transplanted on mice. American Journal of Transplantation, 5, 1002–1010.
- Trottier, V. et al. (2008). IFATS collection: using human adipose-derived stem/stromal cells for the production of new skin substitutes. Stem Cells, 26, 2713–2723.
- Uitto, J., Olsen, D. R., Fazio, M. J. (1989). Extracellular matrix of the skin: 50 years of progress. J Invest Dermatol, 92(4 Suppl), 61S–77S.
- Usha, R., Ramasami, T. (2004a). The effects of urea and n-propanol on collagen denaturation: using DSC, circular dicroism and viscosity. Thermochimica Acta, 409, 201–206.
- Usha, R., Ramasami, T. (2004b). The effects of urea and n-propanol on collagen denaturation: using DSC, circular dicroism and viscosity. Thermochimica Acta, 409, 201–206.
- Usha, R., Ramasami, T. (2005). Colloids Surf B Biointerfaces, 41, 21–24.
- Vore, D. P. D. et al. (1994). Viscoelastic collagen solution for use in cataract surgery. Proceedings of the 20th Annual Meeting, Society for Biomaterials, Birmingham, UK.
- Wallace, D. G. et al. (1988). Injectable collagen for tissue augmentation. In: M. E. Nimni, ed. Collagen. CRC Press: Boca Raton, FL.
- Wang, L. et al. (2008). Isolation and characterisation of collagens from the skin, scale and bone of deep-sea redfish (Sebastes mentella). Food Chemistry, 108, 616–623.
- Wenguang, L. et al. (2008). Recombinant human collagen for tissue engineered corneal substitutes. Biomaterials, 29, 1147–1158.
- Wong, D. W. S. (1989). Mechanism and Theory in Food Chemistry. Nostrand Reinhold: New York, p. 428.
- Wood, A. et al. (2008). Biochemical properties of alligator (Alligator mississippiensis) bone collagen. Comparative Biochemistry and Physiology, 151, 246–249.
- Xu, T. et al. (2009). Electrophysiological characterization of embryonic hippocampal neurons cultured in a 3D collagen hydrogel. Biomaterials, 30, 4377–4383.
- Yang, C. et al. (2004). The application of recombinant human collagen in tissue engineering. Biodrugs, 18, 103–119.
- Yang, W. et al. (1997). Gly-Pro-Arg Confers stability similar to Gly-Pro-Hyp in the collagen triple-helix of host-guest peptides. Journal of Biological Chemistry, 271, 28837–28840.
- Yannas, I. V. et al. (1982). Wound tissue can utilize a polymeric template to synthesize a functional extension of skin. Science, 215, 174–176.
- Yata, M. et al. (2001a). Identification and characterization of molecular species of collagen in fish skin. Journal Food Science, 66, 247–251.
-
Yata, M. et al. (2001b). Identification and characterization of molecular species of collagen in fish skin. Food Chemistry and Toxicology, 66.
10.1111/j.1365-2621.2001.tb11325.x Google Scholar
- Zhang, F. et al. (2011a). Preparation and characterisation of collagen from freshwater fish scales. Food and Nutrition Sciences, 2, 818–823.
- Zhang, J. et al. (2011b). Isolation and characterization of pepsin-solubilized collagen from skin of argentine shortfin squid (Illex argentinus). Advanced Materials Research, 236–238, 19–26.
- Zhang, M., Liu, W., Li, G. (2009). Isolation and characterisation of collagens from the skin of largefin longbarbel catfish (Mystus macropterus). Food Chemistry, 115, 826–831.
- Zhuang, Y. et al. (2009). Effects of collagen and collagen hydrolysate from jellyfish (Rhopilema esculentum) on mice skin photoaging induced by UV irradiation. Journal Food Science, 74, 183–188.