최소 단어 이상 선택하여야 합니다.
최대 10 단어까지만 선택 가능합니다.
다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기한국수산과학회지 = Korean journal of fisheries and aquatic sciences, v.55 no.4, 2022년, pp.397 - 407
박지훈 (경상국립대학교 해양식품공학과) , 이창영 (경상국립대학교 수산식품산업화 기술지원센터) , 최유리 (경상국립대학교 해양식품공학과) , 이정석 (경상국립대학교 해양식품공학과) , 허민수 (경상국립대학교 수산식품산업화 기술지원센터) , 김진수 (경상국립대학교 해양식품공학과)
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 we...
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.
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.
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.
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.
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.
Horowitz JM. 2002. 10 Foods that pack a wallop. Time 159, 76-81.
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.
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.
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.
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.
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.
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.
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.
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.
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?idx263 on Sep 30, 2021.
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.
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.
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.
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.
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.
Park YH, Jang DS and Kim SB. 1995. Processing and Utilization of Seafood. Hyungseoul Publishing Co., Daegu, Korea, 76-151.
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.
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.
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.
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.
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.
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.
Song KW and Jang PS. 1993. Animal Food Processing. Moonundang Publishing Co., Seoul, Korea, 12-13.
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.
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.
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.
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.
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.
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
오픈액세스 학술지에 출판된 논문
※ AI-Helper는 부적절한 답변을 할 수 있습니다.