Korean Journal of Fisheries and Aquatic Sciences (한국수산과학회지)

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
권호 표지
DOI QR코드

DOI QR Code

Characterization of Physicochemical Properties of Collagen from Shark (Isurus oxyrinchus) Skin

청상아리(Isurus oxyrinchus) 껍질 콜라겐의 물리 화학적 특성

  • Park, Soon-Hyung (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kim, Tae-Wan (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kim, Seon-Bong (Department of Food Science and Technology/Institute of Food Science, Pukyong National University)
  • 박순형 (부경대학교 식품공학과/식품연구소) ;
  • 김태완 (부경대학교 식품공학과/식품연구소) ;
  • 김선봉 (부경대학교 식품공학과/식품연구소)
  • Published : 2009.12.31
Download PDF
⟨ Previous Next ⟩

Abstract

Acid- and pepsin-solubilized collagens were extracted from the skin of shark (Isurus oxyrinchus) and their physicochemical properties were characterized by amino acid analysis, SDS-PAGE, the composition of collagen types, solubility and denaturation temperature. Acid - and pepsin-solubilized collagens from shark skin had an imino acid of 188.8 and 186.2 residues/1,000 amino acids, respectively. SDS-PAGE showed two different${\alpha}$ chains ($\alpha1$ and $\alpha2$) and $\beta$-component. The component ratio of type I and V was 10:1, and the type III was not found. Solubility of acid-soluble collagen was low in the range of pH 6.0 to pH 11.0. On the other hand, pepsin-solubilized collagen showed a low solubility in the range of pH 7.0-9.0. Temperature for denaturation of acid- and pepsin-solubilized collagens were $25^{\circ}C$ and $27^{\circ}C$, respectively.

Keywords

References

  1. Bae IW, Osatomi K, Yoshida A, Osako K, Yamaguchi A and Hara K. 2008. Biochemical properties of acidsoluble collagens extracted from the skins of underutilised fishes. Food Chem 108, 49-54 https://doi.org/10.1016/j.foodchem.2007.10.039
  2. Bailey AJ, Paul RG and Kintt L. 1998. Mechanisms of maturation and ageing of collagen. Mech Ageing Dev 106, 1-56 https://doi.org/10.1016/S0047-6374(98)00119-5
  3. Bella J, Liu J, Kramer R, Reodsky B and Berman HM. 2006. Conformational effects of Gly–X–Gly interruptions in the collagen triple helix. J Mol Biol 362, 298-311 https://doi.org/10.1016/j.jmb.2006.07.014
  4. Bergman I and Loxely R. 1963. Two improved and simplified methods for the spectrophotometric determination of hydroxyproline. Anal Chem 35, 1961-1965 https://doi.org/10.1021/ac60205a053
  5. Brik DE, Fitch JM, Babiarz JP, Doane KJ and Linsenmayer TF. 1990. Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter. J Cell Sci 95, 649-657 https://doi.org/10.1042/BJ20020593
  6. Deyl Z, Miksik I and Eckhardt A. 2003. Preparative procedures and purity assessment of collagen proteins. J Chromatogr B 790, 245-275 https://doi.org/10.1016/S1570-0232(03)00158-2
  7. Doty P and Nishihara T. 1958. Recent advances in gelatin and glue research. In: Stainsby G, ed. Pergamon Press, New York, 263
  8. Epstein HA. 2005. Risk assessment of variant creutzfeldtjakob disease in cosmetics. Skinmed 4, 377-378 https://doi.org/10.1111/j.1540-9740.2005.03991.x
  9. FAO. 2006. Report of the FAO expert consultation on the implementation of the FAO international plan of action for the conservation and management of shark. FAO Fisheries Report 795, 1-23
  10. Friess W. 1998. Collagen-biomaterial for drug delivery. Eur J Pharm Sci 45, 113-136
  11. Gelse K, Poschlb E and Aigner T. 2003. Collagens – structure, function and biosynthesis. Adv Drug Deliv Rev 55, 1531-1546 https://doi.org/10.1016/j.addr.2003.08.002
  12. Gomez-Guillen MC, Turnay J , Fernandez-Diaz MD, Ulmo N, Lizarbe MA and Montero P. 2002. Structural and physical properties of gelatin extracted from different marine species: a comparative study. Food Hydrocolloids 16, 25-34 https://doi.org/10.1016/S0268-005X(01)00035-2
  13. Goll DE, Bray RW and Hoekstra WG. 1963. Age-Associated changes in muscle composition. The isolation and properties of a collagenous residue from bovine muscle. J Food Sci 28, 503-509 https://doi.org/10.1111/j.1365-2621.1963.tb00234.x
  14. Harkness RD. 1961. Biological functions of collagen. Biol Rev 36, 399-455 https://doi.org/10.1111/j.1469-185X.1961.tb01596.x
  15. Helcke T. 2000. Gelatin, the food technologist’s friend or foe?. Int Food Ingredients ed 1, 6–8
  16. Hu Y, Zhao W, Qian X and Zhang L. 2003. Effects of oral administration of type II collagen on adjuvant arthritis in rats and its mechanisms. Chin Med J 116, 284-287
  17. Jongjareonrak A, Benjakul S, Visessanguan W, Nagai T and Tanaka M. 2005. Isolation and characterisation of acid and pepsin-solubilised collagens from the skin of brownstripe red snapper (Lutjanus vitta). Food Chem 93, 475-484 https://doi.org/10.1016/j.foodchem.2004.10.026
  18. Josse J and Harrington WF. 1964. Role of pyrrolidine residues in the structure and stabilization of collagen. J Mol Biol 9, 269-287 https://doi.org/10.1016/S0022-2836(64)80207-2
  19. Kimura S. 1971. Studies on marine Invertebrate collagens-III. Characterization of cuticle collagens in annelids. Nippon Suisan Gakkai 37, 419-431 https://doi.org/10.2331/suisan.37.419
  20. Kimura S, Zhu XP, Matsui R, Shijoh M and Takamizawa S. 1988. Characterization of fish muscle typeⅠcollagen. J Food Sci 53, 1315-1318 https://doi.org/10.1111/j.1365-2621.1988.tb09266.x
  21. Kwon MC, Qadir SA, Kim HS, Ahn JH, Cho NH and Lee HY. 2008. UV protection and whitening effects of collagen isolated from outer layer of the squid Todarodes pacificus. J Kor Fish Soc 41, 7-12
  22. Kwon MC, Kim HC, Kim HS, Syed AQ, Hwang BY and Lee HY. 2007. Anti-wrinkle activity of low molecular weight peptides derived from the collagen isolated from Asterias amurensis. Korean J Food Sci Technol 39, 625-629
  23. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 https://doi.org/10.1038/227680a0
  24. Lee CH, Singla A and Lee Y. 2001. Biomedical applications of collagen. Int J Pharm 221, 1-22 https://doi.org/10.1016/S0378-5173(01)00691-3
  25. Liu HY, Li D and Guo SD. 2007. Studies on collagen from the skin of channel catfish (Ictalurus punctaus). Food Chem 101, 621-625 https://doi.org/10.1016/j.foodchem.2006.01.059
  26. Love RM, Yanaguchi K, Creach Y and Lavety J. 1976. The connective tissues and collagens of cod during starvation. Comp Biochem Physiol B Biochem Mol Biol 55, 487-492 https://doi.org/10.1016/0305-0491(76)90005-5
  27. Lowry OH, Rosebrough NJ, Farr AL and Randall RJ. 1951. Protein measurement with the folin phenol reagent. J Biol Chem 193, 265-275
  28. McClain PE, Wiley ER, Bodwell CE and Hornstein I. 1971. Amino-acid composition and cross-linkingcharacteristics of collagen from intramuscular connective tissue of striated muscle (bos taurus). Int J Biochem 2, 121-124 https://doi.org/10.1016/0020-711X(71)90050-4
  29. Morales J, Montero J and Moral A. 2000. Isolation and partial characterization of two types of muscle collagen in some cephalopods. J Agric Food Chem 48, 2142-2148 https://doi.org/10.1021/jf990711k
  30. Muyonga JH, Cole CGB and Duodu KG. 2004. Characterisation of acid soluble collagen from skins of young and adult nileperch (Lates niloticus). Food Chem 85, 81-89 https://doi.org/10.1016/j.foodchem.2003.06.006
  31. Nagai T and Suzuki N. 2000a. Preparation and characterization of several fish bone collagens. J Food Biochem 24, 427-436 https://doi.org/10.1111/j.1745-4514.2000.tb00711.x
  32. Nagai T, Worawattanamateekul W, Suzuki N, Nakamura T, Ito T, Fujiki K, Nakao M and Yano T. 2000b. Isolation and characterization of collagen from rhizostomous jellyfish (Rhopilema asamushi). Food Chem 70, 205-208 https://doi.org/10.1016/S0308-8146(00)00081-9
  33. Nagai T, Suzuki N and Nagashima T. 2008. Collagen from common minke whale (Balaenoptera acutorostrata) unesu. Food Chem 111, 296-301 https://doi.org/10.1016/j.foodchem.2008.03.087
  34. Nalinanon S, Benjakul S, Visessanguan W and Kishimura H. 2007. Use of pepsin for collagen extraction from the skin of bigeye snapper (Priacanthus tayenus). Food Chem 104, 593-601 https://doi.org/10.1016/j.foodchem.2006.12.035
  35. Ogawa M, Moody MW, Portier RJ, Bell J, Schexnayder MA and Losso JN. 2003. Biochemical properties of black drum and sheepshead seabream skin collagen. J Agric Food Chem 51, 8088-8092 https://doi.org/10.1021/jf034350r
  36. Piez KA and Gross J. 1960. The amino acid composition of some fish collagens: the relation between composition and structure. The J Biol Chem 235, 995-998
  37. Piez KA. 1985. Collagen In: Encyclopedia of Polymer Science and Engineering. Vol. 3, Mark HF, Bikales N, Overberger CG, Menges G and Kroschwitz JI, Eds. Wiley Interscience, New York, U.S.A., pp. 699–724
  38. Rama S and Chadrakasan G. 1983. Physico-chemical characterization and molecular organization of the collagen from the skin of an air-breathing fish (Ophiocephalus striatus). J Biosci 5, 147-154 https://doi.org/10.1007/BF02716853
  39. Ranganayaki MD, Asghar A and Henrickson RL. 1982. Influence of anion and cation on the waterholding capacity of bovine hide collagen at different ph values. effect of sodium chloride and polyphosphateson hydration. J Food Sci 47, 705-710 https://doi.org/10.1111/j.1365-2621.1982.tb12695.x
  40. Rigby BJ and Prosser CL. 1975. Thermal transitions of collagen from fish recovered from different depths. Comp Biochem Physiol B Biochem Mol Biol 52, 98-90
  41. Spackman DH, Stein WH and Moore S. 1958. Automatic recording apparatus for use in chromatography of amino acids. Anal Chem 30, 1190-1206 https://doi.org/10.1021/ac60139a006
  42. Trevitt CR and Singh PN. 2003. Variant creutzfeldtjakob disease: pathology, epidemiology, and public health implications. Am J Clin Nutr 78, 651s-656s
  43. 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 Chem 108, 616-623 https://doi.org/10.1016/j.foodchem.2007.11.017
  44. Woo JW, Yu SJ, Cho SM, Lee YB and Kim SB. 2008. Extraction optimization and properties of collagen from yellowfin tuna (Thunnus albacares) dorsal skin. Food Hydrocolloids 22, 879-887 https://doi.org/10.1016/j.foodhyd.2007.04.015
  45. Yamashita MS, Arai S, Kokubo S, Aso K and Fujimaki M. 1975. Synthesis and characterization of a glutamic acid enriched plastein with greater solubility. J Agric Food Chem 23, 27-30 https://doi.org/10.1021/jf60197a027

Cited by

  1. Dietary flounder skin improves growth performance, body composition, and stress recovery in the juvenile black rockfish (Sebastes schlegeli) vol.3, pp.1, 2014, https://doi.org/10.1186/2193-1801-3-235
  2. Characterization of off-odor compounds of collagen peptides from tilapia scale using GC-MS-olfactometry vol.24, pp.2, 2015, https://doi.org/10.1007/s10068-015-0053-8
  3. Flounder skin meal as a potential protein source substitute in the diet of juvenile black rockfish (Sebastes schlegeli) vol.47, pp.7, 2016, https://doi.org/10.1111/are.12666