Characterization of the Acid- and Pepsin-Soluble Collagens from Haruan (Channa striatus) Scales
Authors
- Bagus Fajar Pamungkas Faculty of Fisheries and Marine Science, Mulawarman University, Kampus Gn. Kelua, Samarinda 75119, Indonesia
- Supriyadi Department of Food and Agricultural Product Technology, Faculty of Agricultural Technology, Universitas Gadjah Mada, Jl. Flora, Bulaksumur, Yogyakarta 55281, Indonesia
- Agnes Murdiati Department of Food and Agricultural Product Technology, Faculty of Agricultural Technology, Universitas Gadjah Mada, Jl. Flora, Bulaksumur, Yogyakarta 55281, Indonesia
-
Retno Indrati
Department of Food and Agricultural Product Technology, Faculty of Agricultural Technology, Universitas Gadjah Mada, Jl. Flora, Bulaksumur, Yogyakarta 55281, Indonesia
DOI:
https://doi.org/10.3923/pjn.2019.324.332Keywords:
Acid-soluble collagen (ASC-SH), fish, haruan scale, pepsin-soluble collagen (PSC-SH), pepsin digestionAbstract
Background and Objective: The optimal use of haruan scales for preparing collagen is a promising method to increase value-added products and to protect the environment. The aim of this research was to characterize the acid- and pepsin-soluble collagens from haruan (Channa striatus) scales. Materials and Methods: The fish scales were subjected to an extraction with 0.5 M acetic acid and a digestion with 0.1% pepsin. The results are presented as the mean±standard deviation. Results: The yields of the acid-soluble collagen in the haruan scales (ASC-SH) and the pepsin-soluble collagen in the haruan scales (PSC-SH) were 1.44 and 2.94% (on a dry basis), respectively. ASC-SH and PSC-SH contained glycine as the major amino acid and had high imino acid contents (238 and 242 residues/1,000 residues, respectively). Based on the SDS-PAGE pattern, both ASC-SH and PSC-SH were identified as type I collagens containing α1 and α2 chains. β and γ components were also found in both collagens. The FTIR spectra indicated that both collagens had triple helical structures. The collagens were both soluble at acidic pH levels (1-4) and their solubility was low when the NaCl concentrations were above 3% (w/v). Conclusion: It was concluded that haruan scales could be an alternative source of collagen and that the characteristics of the collagens were slightly affected by the extraction process used in this study.
References
Morimura, S., H. Nagata, Y. Uemura, A. Fahmi, T. Shigematsu and K. Kida, 2002. Development of an effective process for utilization of collagen from livestock and fish waste. Process Biochem., 37: 1403-1412.
Lee, C.H., A. Singla and Y. Lee, 2001. Biomedical applications of collagen. Int. J. Pharm., 221: 1-22.
Liu, W., G. Li, Y. Miao and X. Wu, 2009. Preparation and characterization of pepsinâ€solubilized type I collagen from the scales of snakehead (Ophiocephalus argus). J. Food Biochem., 33: 20-37.
Liu, Q., B.H. Kong, Y.L. Xiong and X.F. Xia, 2010. Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis. Food Chem., 118: 403-410.
Ogawa, M., R.J. Portier, M.W. Moody, J. Bell, M.A. Schexnayder and J.N. Losso, 2004. Biochemical properties of bone and scale collagens isolated from the subtropical fish black drum (Pogonia cromis) and sheepshead seabream (Archosargus probatocephalus). Food Chem., 88: 495-501.
Zhang, J., R. Duan, C. Ye and K. Konno, 2010. Isolation and characterization of collagens from scale of silver carp (Hypophthalmichthys molitrix). J. Food Biochem., 34: 1343-1354.
Huang, C.Y., J.M. Kuo, S.J. Wu and H.T. Tsai, 2016. Isolation and characterization of fish scale collagen from tilapia (Oreochromis sp.) by a novel extrusion-hydro-extraction process. Food Chem., 190: 997-1006.
Chi, C.F., B. Wang, Z.R. Li, H.Y. Luo, G.F. Ding and C.W. Wu, 2014. Characterization of acidâ€soluble collagen from the skin of hammerhead shark (S phyrna lewini). J. Food Biochem., 38: 236-247.
Kittiphattanabawon, P., S. Benjakul, W. Visessanguan, T. Nagai and M. Tanaka, 2005. Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chem., 89: 363-372.
Pan, B.Q., W.J. Su, M.J. Cao, Q.F. Cai, W.Y. Weng and G.M. Liu, 2012. IgE reactivity to type I collagen and its subunits from tilapia (Tilapia zillii). Food Chem., 130: 127-133.
Wang, B., Y.M. Wang, C.F. Chi, H.Y. Luo, S.G. Deng and J.Y. Ma, 2013. Isolation and characterization of collagen and antioxidant collagen peptides from scales of croceine croaker (Pseudosciaena crocea). Mar. Drugs, 11: 4641-4661.
Chuaychan, S., S. Benjakul and H. Kishimura, 2015. Characteristics of acid-and pepsin-soluble collagens from scale of seabass (Lates calcarifer). LWT-Food Sci. Technol., 63: 71-76.
Anonymous, 2015. Statistical data of aquaculture fishery in 2009-2013. Ministry of Marine and Fishery of Indonesia, Indonesia
AOAC., 2005. Official Method of Analysis of the Association of Official Analytical of Chemist. Association of Official Analytical Chemist, Arlington, VA., USA.
Reddy, K. and C.S. Enwemeka, 1996. A simplified method for the analysis of hydroxyproline in biological tissues. Clin. Biochem., 29: 225-229.
Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
Lowry, O.H., N.J. Rosebrough, A.L. Farr and R.J. Randall, 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem., 193: 265-275.
Montero, P., F. Jimenezâ€Colmenero and J. Borderìas, 1991. Effect of pH and the presence of NaCl on some hydration properties of collagenous material from trout (Salmo irideus Gibb) muscle and skin. J. Sci. Food Agric., 54: 137-146.
Zhang, Y., W. Liu, G. Li, B. Shi, Y. Miao and X. Wu, 2007. Isolation and partial characterization of pepsin-soluble collagen from the skin of grass carp (Ctenopharyngodon idella). Food Chem., 103: 906-912.
Galea, C. A., B.P. Dalrymple, R. Kuypers and R. Blakeley, 2000. Modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin. Prot. Sci., 9: 1947-1959.
Sato, K., T. Ebihara, E. Adachi, S. Kawashima, S. Hattori and S. Irie, 2000. Possible involvement of aminotelopeptide in self-assembly and thermal stability of collagen I as revealed by its removal with proteases. J. Biol. Chem., 275: 25870-25875.
Jongjareonrak, A., S. Benjakul, W. Visessanguan and M. Tanaka, 2005. Isolation and characterization of collagen from bigeye snapper (Priacanthus macracanthus) skin. J. Sci. Food Agric., 85: 1203-1210.
Nomura, Y., H. Sakai, Y. Ishii and K. Shirai, 1996. Preparation and some properties of type I collagen from fish scales. Biosci. Biotechnol. Biochem., 60: 2092-2094.
Regenstein, J.M. and P. Zhou, 2007. Collagen and Gelatin from Marine by-Products. In: Maximising The Value of Marine By-Products, Shahidi, F. (Ed.)., Woodhead Publishing Limited, UK., pp: 279-303.
McCormick, R.J., 2009. Collagen. In: Applied Muscle Biology and Meat Science, Du, M. and R.J. McCormic (Eds.)., Taylor and Francis, USA., pp: 129-148.
Muyonga, J.H., C.G.B. Cole and K.G. Duodu, 2004. Characterisation of acid soluble collagen from skins of young and adult Nile perch (Lates niloticus). Food Chem., 85: 81-89.
Foegeding, E.A., T.C. Lanier and H.O. Hultin, 1996. Characteristics of Edible Muscle Tissues. In: Food Chemistry, Fennema, O.R. (Eds.). 3rd Edn., Marcel Dekker, New York, pp: 902-906.
Matmaroh, K., S. Benjakul, T. Prodpran, A.B. Encarnacion and H. Kishimura, 2011. Characteristics of acid soluble collagen and pepsin soluble collagen from scale of spotted golden goatfish (Parupeneus heptacanthus). Food Chem., 129: 1179-1186.
Yu, D., C.F. Chi, B. Wang, G.F. Ding and Z.R. Li, 2014. Characterization of acid-and pepsin-soluble collagens from spines and skulls of skipjack tuna (Katsuwonus pelamis). Chinese J. Natural Med., 12: 712-720.
Huang, Y.R., C.Y. Shiau, H.H. Chen and B.C. Huang, 2011. Isolation and characterization of acid and pepsin-solubilized collagens from the skin of balloon fish (Diodon holocanthus). Food Hydrocolloids, 25: 1507-1513.
Jamilah, B., M.U. Hartina, D.M. Hashim and A.Q. Sazili, 2013. Properties of collagen from barramundi (Lates calcarifer) skin. Int. Food Res. J., 20: 835-842.
Zhang, F., A. Wang, Z. Li, S. He and L. Shao, 2011. Preparation and characterisation of collagen from freshwater fish scales. Food Nutr. Sci., 2: 818-823.
El-Rashidy, A.A., A. Gad, A.E.H.G. Abu-Hussein, S.I. Habib, N.A. Badr and A.A. Hashem, 2015. Chemical and biological evaluation of Egyptian Nile Tilapia (Oreochromis niloticas) fish scale collagen. Int. J. Biol. Macromol., 79: 618-626.
Liu, D., L. Liang, J.M. Regenstein and P. Zhou, 2012. Extraction and characterisation of pepsin-solubilised collagen from fins, scales, skins, bones and swim bladders of bighead carp (Hypophthalmichthys nobilis). Food Chem., 133: 1441-1448.
Wang, B., L. Li, C.F. Chi, J.H. Ma, H.Y. Luo and Y.F. Xu, 2013. Purification and characterisation of a novel antioxidant peptide derived from blue mussel (Mytilus edulis) protein hydrolysate. Food Chem., 138: 1713-1719.
Chen, S., H. Chen, Q. Xie, B. Hong and J. Chen et al., 2016. Rapid isolation of high purity pepsin-soluble type I collagen from scales of red drum fish (Sciaenops ocellatus). Food Hydrocolloids, 52: 468-477.
Zeng, S., J. Yin, C. Zhang, Z. Jiang, W. Wu and X. Zhao, 2016. Physicochemical properties of pepsin-solubilized collagen extracted from Nile Tilapia (Oreochromis niloticus) scale. J. Aquat. Food Prod. Technol., 25: 656-665.
Okazaki, E. and K. Osako, 2014. Isolation and characterization of acid-soluble collagen from the scales of marine fishes from Japan and Vietnam. Food Chem., 149: 264-270.
Ogawa, M., M.W. Moody, R.J. Portier, J. Bell, M.A. Schexnayder and J.N. Losso, 2003. Biochemical properties of black drum and sheepshead seabream skin collagen. J. Agric. Food Chem., 512-513: 8088-8092.
Zhang, F., Z. Wang and S. Xu, 2009. Macroporous resin purification of grass carp fish (Ctenopharyngodon idella) scale peptides with in vitro angiotensin-I converting enzyme (ACE) inhibitory ability. Food Chem., 117: 387-392.
Singh, P., S. Benjakul, S. Maqsood and H. Kishimura, 2011. Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chem., 124: 97-105.
Sai, K.P. and M. Babu, 2001. Studies on Rana tigerina skin collagen. Comparat. Biochem. Physiol. Part B, 128: 81-90.
Doyle, B.B., E.G. Bendit and E.R. Blout, 1975. Infrared spectroscopy of collagen and collagenâ€like polypeptides. Biopolymers, 14: 937-957.
Abe, Y. and S. Krimm, 1972. Normal vibrations of crystalline polyglycine I. Biopolymers, 11: 1817-1839.
Payne, K.J. and A. Veis, 1988. Fourier transform ir spectroscopy of collagen and gelatin solutions: Deconvolution of the amide I band for conformational studies. Biopolymers, 27: 1749-1760.
Barth, A. and C. Zscherp, 2002. What vibrations tell about proteins. Quart. Rev. Biophys., 35: 369-430.
Nalinanon, S., S. Benjakul, W. Visessanguan and H. Kishimura, 2007. Use of pepsin for collagen extraction from the skin of bigeye snapper (Priacanthus tayenus). Food Chem., 104: 593-601.
De Guzzi Plepis, A.M., G. Goissis and D.K. Dasâ€Gupta, 1996. Dielectric and pyroelectric characterization of anionic and native collagen. Polym. Eng. Sci., 36: 2932-2938.
Bae, I., K. Osatomi, A. Yoshida, K. Osako, A. Yamaguchi and K. Hara, 2008. Biochemical properties of acid-soluble collagens extracted from the skins of underutilised fishes. Food Chem., 108: 49-54.
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