Startseite Analysis and improvement of stability of pepsin-solubilized collagen from skin of carp (Cyprinus carpio)
Artikel
Lizenziert
Nicht lizenziert Erfordert eine Authentifizierung

Analysis and improvement of stability of pepsin-solubilized collagen from skin of carp (Cyprinus carpio)

  • Rui Duan EMAIL logo , Jun-Jie Zhang , Kunihiko Konno , Mei-Hua Wu , Jing Li und Ye Chen
Veröffentlicht/Copyright: 22. Juni 2012
Veröffentlichen auch Sie bei De Gruyter Brill

Abstract

Pepsin is widely used for the extraction of pepsin-solubilized collagens (PSC) from many resources. PSC-A and PSC-P were prepared from carp skin using 0.1 mol L−1 acetic acid and 0.02 mol L−1 Na2HPO4 (pH 7.2) as the dialysis solution, respectively. SDS-PAGE patterns showed PSC-A and PSC-P as type I collagens, as well as acid soluble collagen (ASC). When incubated at 40°C, no degradation was observed for ASC, but PSC-A and PSC-P were degraded into short peptides, showing lower stability than ASC. The results indicate that pepsin remaining in the PSCs resulted in their degradation, which was confirmed by the inhibition using pepstatin. This research revealed the behavior of the remaining pepsin in pepsin-solubilized collagens and an approach to the PSC stability improvement was proposed. Chromatography profiles showed that new PSC prepared by the improved method had almost the same stability as ASC.

[1] Bailey, A. J., & Light, N. D. (1989). Connective tissue in meat and meat products (pp. 238–242). London, UK: Elsevier Applied Science. Suche in Google Scholar

[2] Bornstein, P., Kang A. H., & Piez, I. A. (1966). The nature and location of intramolecular cross-links in collagen. Proceedings of the National Academy of Sciences, 55, 417–424. http://dx.doi.org/10.1073/pnas.55.2.41710.1073/pnas.55.2.417Suche in Google Scholar

[3] Cavallaro, J. F., Kemp, P. D., & Kraus, K. H. (1994). Collagen fabrics as biomaterials. Biotechnology and Bioengineering, 43, 781–791. DOI: 10.1002/bit.260430813. http://dx.doi.org/10.1002/bit.26043081310.1002/bit.260430813Suche in Google Scholar

[4] Duan, R., Zhang, J., Du, X., Yao, X., & Konno, K. (2009). Properties of collagen from skin, scale and bone of carp(Cyprinus carpio). Food Chemistry, 112, 702–706. DOI: 10.1016/j.foodchem.2008.06.020. http://dx.doi.org/10.1016/j.foodchem.2008.06.02010.1016/j.foodchem.2008.06.020Suche in Google Scholar

[5] Gross, J., & Lapiere, C. M. (1962). Collagenolytic activity in amphibian tissues: a tissue culture assay. Proceedings of the National Academy of Sciences, 48, 1014–1022. http://dx.doi.org/10.1073/pnas.48.6.101410.1073/pnas.48.6.1014Suche in Google Scholar

[6] Hood, L. L. (1987). Collagen in sausage casings. In A. M. Pearson, T. R. Dutson, & A. J. Bailey (Eds.), Advances in meat research (Vol. 4, pp. 109–129). New York, NY, USA: Nostrand Reinhold. Suche in Google Scholar

[7] Ikoma, T., Kobayashi, H., Tanaka, J., Walsh, D., & 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, 199–204. DOI: 10.1016/s0141-8130(03)00054-0. http://dx.doi.org/10.1016/S0141-8130(03)00054-010.1016/S0141-8130(03)00054-0Suche in Google Scholar

[8] Kimura, S., Ohno Y., Miyauchi Y., & Uchida, N. (1987). Fish skin type I collagen: wide distribution of an α3 subunit in teleost. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 88, 27–34. DOI: 10.1016/0305-0491(87)90074-5. http://dx.doi.org/10.1016/0305-0491(87)90074-510.1016/0305-0491(87)90074-5Suche in Google Scholar

[9] Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 277, 680–685. DOI: 10.1038/227680a0. http://dx.doi.org/10.1038/227680a010.1038/227680a0Suche in Google Scholar

[10] Mizuta, S., Hwang, J., & Yoshinaka, R. (2002a). Molecular species of collagen from wing muscle of skate (Raja kenojei). Food Chemistry, 76, 53–58. DOI: 10.1016/s0308-8146(01)00249-7. http://dx.doi.org/10.1016/S0308-8146(01)00249-710.1016/S0308-8146(01)00249-7Suche in Google Scholar

[11] Mizuta, S., Miyagi, T., Nishimiya, T., & Yoshinaka, R. (2002b). Partial characterization of collagen in mantle and adductor of pearl oyster (Pinctada fucata). Food Chemistry, 79, 319–325. DOI: 10.1016/s0308-8146(02)00148-6. http://dx.doi.org/10.1016/S0308-8146(02)00148-610.1016/S0308-8146(02)00148-6Suche in Google Scholar

[12] Nagai, T., Araki, Y., & Suzuki, N. (2002). Collagen of the skin of ocellate puffer fish (Takifugu rubripes). Food Chemistry, 78, 173–177. DOI: 10.1016/s0308-8146(01)00396-x. http://dx.doi.org/10.1016/S0308-8146(01)00396-X10.1016/S0308-8146(01)00396-XSuche in Google Scholar

[13] Nagai, T., & Suzuki, N. (2000). Isolation of collagen from fish waste material — skin, bone and fins. Food Chemistry, 68, 277–281. DOI: 10.1016/s0308-8146(99)00188-0. http://dx.doi.org/10.1016/S0308-8146(99)00188-010.1016/S0308-8146(99)00188-0Suche in Google Scholar

[14] Nagai, T., Worawattanamateekul, W., Suzuki, N., Nakamura, T., Ito, T., Fujiki, K., Nakao, M., & Yano, T. (2000). Isolation and characterization of collagen from rhizostomous jellyfish (Rhopilema asamushi). Food Chemistry, 70, 205–208. DOI: 10.1016/s0308-8146(00)00081-9. http://dx.doi.org/10.1016/S0308-8146(00)00081-910.1016/S0308-8146(00)00081-9Suche in Google Scholar

[15] Neurath, H., Hill, R. L., & Boeder, C. L. (1975). The proteins. New York, NY, USA: Academic Press. Suche in Google Scholar

[16] Ogawa, M., Moody, M. W., Portier, R. J., Bell, J., Schexnayder, M. A., & Losso, J. N. (2003). Biochemical properties of black drum and sheepshead seabream skin collagen. Journal of Agricultural and Food Chemistry, 51, 8088–8092. DOI: 10.1021/jf034350r. http://dx.doi.org/10.1021/jf034350r10.1021/jf034350rSuche in Google Scholar PubMed

[17] Ogawa, M., Portier, R. J., Moody, M. W., Bell, J., Schexnayder, M. A., & 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, 495–501. DOI: 10.1016/j.foodchem.2004.02.006. http://dx.doi.org/10.1016/j.foodchem.2004.02.00610.1016/j.foodchem.2004.02.006Suche in Google Scholar

Published Online: 2012-6-22
Published in Print: 2012-7-1

© 2012 Institute of Chemistry, Slovak Academy of Sciences

Heruntergeladen am 27.11.2025 von https://www.degruyterbrill.com/document/doi/10.2478/s11696-012-0172-0/pdf
Button zum nach oben scrollen