Browse > Article
http://dx.doi.org/10.5657/KFAS.2022.0397

Collagen and Texture Properties of Commonly Consumed Fish Species in Korea as Sliced Raw Fishes  

Park, Ji Hoon (Department of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University)
Lee, Chang Yong (Research Center for Industrial Development of Seafood, Gyeongsang National University)
Choe, Yu Ri (Department of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University)
Lee, Jung Suck (Department of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University)
Heu, Min Soo (Research Center for Industrial Development of Seafood, Gyeongsang National University)
Kim, Jin-Soo (Department of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University)
Publication Information
Korean Journal of Fisheries and Aquatic Sciences / v.55, no.4, 2022 , pp. 397-407 More about this Journal
Abstract
This study investigated the collagen and texture properties of commonly consumed sliced raw fish species (CC-SRF) [olive flounder (OF), red seabream (RS), Atlantic salmon (AS), coho salmon (CoS) and sockeye salmon (SS)] distributed in Korea as sliced raw fishes. The crude lipid contents of CC-SRF were 5.5% for OF, 6.8% for RS, 18.5% for AS, 16.1% for CoS, and 5.7% for SS. The collagen content and solubility from CC-SRF were 622 mg/100 g and 78.0%, respectively, in OF, 270 mg/100 g and 75.6%, respectively, in RS, 237 mg/100 g and 24.1%, respectively, in AS, 341 mg/100 g and 65.7%, respectively, in CoS, and 246 mg/100 g and 17.9%, respectively, in SS. The texture of CC-SRF was affected by the lipid content, collagen content, acid solubility, hydroxylation, and cross linkage degree. The highest hardness of CC-SRF was obtained from OF, followed by RS, SS, AS and CoS. There was, however, no difference (P>0.05) in hardness between OF and RS and between AS and CoS.
Keywords
Collagen; Oliver flounder; Sliced raw fish; Texture of fish;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Bella J, Brodsky B and Berman HM. 1995. Hydration structure of a collagen peptide. Structure 3, 893-906. https://doi.org/10.1016/S0969-2126(01)00224-6.   DOI
2 Ciarlo AS, Paredi ME and Fraga AN. 1997. Isolation of soluble collagen from hake skin (Merluccius hubbsi). J Aquat Food Prod Technol 6, 65-77. https://doi.org/10.1300/J030v06n01_06.   DOI
3 Feng H, Peng D, Liang XF, Chai F, Tang S and Li J. 2022. Effect of dietary hydroxyproline supplementation on Chinese perch (Siniperca chuatsi) fed with fish meal partially replaced by fermented soybean meal. Aquaculture 547, 737454. https://doi.org/10.1016/j.aquaculture.2021.737454.   DOI
4 Horowitz JM. 2002. 10 Foods that pack a wallop. Time 159, 76-81.
5 Jeevithan E, Wu W, Nanping W, Lan H and Bao B. 2014. Isolation, purification and characterization of pepsin soluble collagen isolated from silvertip shark (Carcharhinus albimarginatus) skeletal and head bone. Process Biochem 49, 1767-1777. https://doi.org/10.1016/j.procbio.2014.06.011.   DOI
6 Jianan S, Jingjing Z, Dandan Z, Changhu X, Zhen L and Xiangzhao M. 2019. Characterization of turbot (Scophthalmus maximus) skin and the extracted acid-soluble collagen. J Ocean Univ China 18, 687-692. https://doi.org/10.1007/s11802-019-3837-2.   DOI
7 Kim JS and Park JW. 2004. Characterization of acid-soluble collagen from Pacific whiting surimi processing byproducts. J Food Sci 69, C637-C642. https://doi.org/10.1111/j.1365-2621.2004.tb09912.x.   DOI
8 Kimura S, Zhu XP, Matsui R, Shijoh M and Takamizawa S. 1988. Characterization of fish muscle type I collagen. J Food Sci 53, 1315-1318. https://doi.org/10.1111/j.1365-2621.1988.tb09266.x.   DOI
9 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.   DOI
10 MFDS (Ministry of Food and Drug Safety). 2021. General Analytical Method in Food Code. Retrieved from http://www.foodsafetykorea.go.kr/foodcode/01_02.jsp?idx=263 on Sep 30, 2021.
11 Montero P, Borderias J, Turnay J and Leyzarbe MA. 1990. Characterization of hake (Merluccius merluccius L.) and trout (Salmo irideus Gibb) collagen. J Agric Food Chem 38, 604-609. https://doi.org/10.1021/jf00093a004.   DOI
12 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.   DOI
13 Ando M, Makino M, Tsukamasa Y, Makinodan Y and Miyosh M. 2001. Interdependence between heat solubility and pyridinoline contents of squid mantle collagen. J Food Sci 66, 265-269. https://doi.org/10.1111/j.1365-2621.2001.tb11329.x.   DOI
14 Doyle BB, Bendit EG and Blout ER. 1975. Infrared spectroscopy of collagen and collagen-like polypeptides. Biopolymers 14, 937-957. https://doi.org/10.1002/bip.1975.360140505.   DOI
15 Jakobsen RJ, Brown LL, Hutson TB, Fink DJ and Veis A. 1983. Intermolecular interactions in collagen self-assembly as revealed by Fourier transform infrared spectroscopy. Science 220, 1288-1290. https://doi.org/10.1126/science.6857249.   DOI
16 Sato K, Ohashi C, Ohtsuki K and Kawabata M. 1991. Type V collagen in trout (Salmo gairdneri) muscle and its solubility change during chilled storage of muscle. J Agric Food Chem 39, 1222-1225. https://doi.org/10.1021/jf00007a005.   DOI
17 Moreno HM, Montero MP, Gomez-Guillen MC, FernandezMartin F, Morkore T and Borderias J. 2012. Collagen characteristics of farmed Atlantic salmon with firm and soft fillet texture. Food Chem 134, 678-685. https://doi.org/10.1016/j.foodchem.2012.02.160.   DOI
18 Nagai T and Suzuki N. 2000. Isolation of collagen from fish waste material-skin, bone and fins. Food Chem 68, 277-281. https://doi.org/10.1016/S0308-8146(99)00188-0.   DOI
19 Park YH, Jang DS and Kim SB. 1995. Processing and Utilization of Seafood. Hyungseoul Publishing Co., Daegu, Korea, 76-151.
20 Sato K, Yoshinaka R, Sato M and Shimizu Y. 1986. Collagen content in the muscle of fishes in association with their swimming movement and meat texture. Nippon Suisan Gakkaishi 52, 1595-1600. https://doi.org/10.2331/suisan.52.1595.   DOI
21 Shen J, Yu D, Gao P, Xu Y, Jiang Q and Xia W. 2021. Relevance of collagen solubility and gelatinolytic proteinase activity for texture softening in chilled grass carp (Ctenopharyngodon idellus) fillets. Int J Food Sci Technol 56, 1801-1808. https://doi.org/10.1111/ijfs.14805.   DOI
22 Potaros T, Raksakulthai N, Runglerdkreangkrai J and Worawattanamateekul W. 2009. Characteristics of collagen from Nile tilapia (Oreochromis niloticus) skin isolated by two different methods. Kasetsart J Nat Sci 43, 584-593.
23 Ko JY, Kang N, Lee JH, Kim JS, Kim WS, Park SJ, Kim YT and Jeon YJ. 2016. Angiotensin I-converting enzyme inhibitory peptides from an enzymatic hydrolysate of flounder fish (Paralichthys olivaceus) muscle as a potent antihypertensive agent. Process Biochem 51, 535-541. https://doi.org/10.1016/j.procbio.2016.01.009.   DOI
24 MOF (Ministry of Oceans and Fisheries). 2022. Major Statistics of Oceans and Fisheries. Retrieved from https://www.fips.go.kr/p/S020304/ on Feb 28, 2022.
25 Muyonga JH, Cole CGB and Duodu KG. 2004. Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus). Food Chem 86, 325-332. https://doi.org/10.1016/j.foodchem.2003.09.038.   DOI
26 Seo YJ, Gil BJ, Kyoung JS, Yoo BS, Chang YH, Yu SY and Lee YS. 2014. Effect of environmentally-friendly red clayprocessed materials on quality characteristics of eel. J Korean Soc Food Sci Nutr 43, 287-292. https://doi.org/10.3746/jkfn.2014.43.2.287.   DOI
27 Silva RSG, Bandeira SF and Pinto LAA. 2014. Characteristics and chemical composition of skins gelatin from cobia (Rachycentron canadum). LWT-Food Sci Technol 57, 580-585. https://doi.org/10.1016/j.lwt.2014.02.026.   DOI
28 Vacha F, Stejskal V, Vejsada P, Kouril J and Hlavac D. 2013. Texture profile analyses in tench (Tinca tinca L., 1758) from extensive and intensive culture. Acta Vet Brno 82, 421-425. https://doi.org/10.2754/avb201382040421.   DOI
29 Song KW and Jang PS. 1993. Animal Food Processing. Moonundang Publishing Co., Seoul, Korea, 12-13.
30 Sigurgisladottir S, Hafsteinsson H, Jonsson A, Lie O, Nortvedt R, Thomassen M and Torrissen O. 1999. Textural properties of raw salmon fillets as related to sampling method. J Food Sci 64, 99-104. https://doi.org/10.1111/j.1365-2621.1999.tb09869.x.   DOI
31 Yan M, Li B, Zhao X, Ren G, Zhuang Y, Hou H, Zhang X, Chen L and Fan Y. 2008. Characterization of acid-soluble collagen from the skin of walleye pollock (Theragra chalcogramma). Food Chem 107, 1581-1586. https://doi.org/10.1016/j.food-chem.2007.10.027.   DOI
32 Takahashi K, Suzuki A and Wada K. 1989. Gelatinization of pig bone insoluble collagen. Nippon Shokuhin Kogyo Gakkaishi 36, 538-542. https://doi.org/10.3136/nskkk1962.36.7_538.   DOI
33 Veeruraj A, Arumugam M and Balasubramanian T. 2013. Isolation and characterization of thermostable collagen from the marine eel-fish (Evenchelys macrura). Process Biochem 48, 1592-1602. https://doi.org/10.1016/j.procbio.2013.07.011.   DOI
34 Xu C, Wang C, Cai QF, Zhang Q, Weng L, Liu GM, Su WJ and Cao MJ. 2015. Matrix metalloproteinase 2 (MMP-2) plays a critical role in the softening of common carp muscle during chilled storage by degradation of type I and V collagens. J Agric Food Chem 63, 10948-10956. https://doi.org/10.1021/acs.jafc.5b03893.   DOI