Functionality and Biological Activity of Isolate Processed Water Generated During Protein Isolate Preparation of Fish Roes Using an Isoelectric Solubilization and Precipitation Process
![]() |
Lee, Gyoon-Woo
(Department of Food and Nutrition/Institute of Marine Industry, Gyeongsang National University)
Yoon, In Seong (Department of Food and Nutrition/Institute of Marine Industry, Gyeongsang National University) Kang, Sang In (Department of Seafood and Aquaculture Science/Institute of Marine Industry, Gyeongsang National University) Lee, Su Gwang (Department of Seafood and Aquaculture Science/Institute of Marine Industry, Gyeongsang National University) Kim, Jae-Il (Department of Food Science and Nutrition, Pukyong National University) Kim, Jin-Soo (Department of Seafood and Aquaculture Science/Institute of Marine Industry, Gyeongsang National University) Heu, Min Soo (Department of Food and Nutrition/Institute of Marine Industry, Gyeongsang National University) |
1 | Damodaran S. 1997. Protein-stabilised foams and emulsions. In: Food Proteins and Their Applications. Damodaran S, ed. Marcel Dekker, New York, U.S.A., 57-110. |
2 | Dickinson E, Lorient D. Emulsions. 1994. Food macromolecules and colloids. The Royal Society of Chemistry, Cambridge, London, U.K., 201-274. |
3 | Dumay J, Radier S, Barnathan G, Berge JP and Jaouen P. 2008. Recovery of valuable soluble compounds from washing waters generated during small fatty pelagic surimi process\-ing by membrane processes. Environ Technol 29, 451-461. http://dx.doi.org/10.1080/09593330801983912. DOI |
4 | Gomez-Ruiz JA, Lopez-Exposito I, Pihlanto A, Ramos M and Recio I. 2008. Antioxidant activity of ovine casein hydrolysates: identification of active peptides by HPLC-MS/ MS. Eur Food Res Technol 227, 1061-1067. http://dx.doi.org/10.1007/s00217-008-0820-3. DOI |
5 | Heu MS, Kim HS, Jung SC, Park CH, Park HJ, Yeum DM, Park HS, Kim CG and Kim JS. 2006. Food component characteristics of skipjack (Katsuwonus pelamis) and yellowfin tuna (Thunnus albacares) roes. J Kor Fish Soc 39, 1-8. |
6 | Himaya SWA, Ngo DH, Ryu B and Kim SK. 2012. An active peptide purified from gastrointestinal enzyme hydrolysate of Pacific cod skin gelatin attenuates angiotensin-1 converting enzyme (ACE) activity and cellular oxidative stress. Food Chem 132, 1872-1882. http://dx.doi.org/10.1016/j.foodchem.2011.12.020. DOI |
7 | Hultin HO and Kelleher SD. 1999. Process for isolating a protein composition from a muscle source and protein composition. Advanced Protein Technologies Inc., assignee. US Patent 6,005,073. |
8 | Iida K, Hase K, Shimomura K, Sudo S, Kadota S and Namba T. 1995. Potent inhibitors of tyrosinase activity and melanin biosynthesis from Rheum officinale. Planta Med 61, 425-428. http://dx.doi.org/10.1055/s-2006-958129. DOI |
9 | Park SH, Lee HJ, Yoon IS, Lee GW, Kim JS and Heu MS. 2016. Protein functionality of concentrates prepared from yellowfin tuna (Thunnus albacares) roe by cook-dried process. Food Sci Biotechnol 25, 1569-1575. http://dx.doi.org/10.1007/s10068-016-0242-0. DOI |
10 | Schurink M, van Berkel WJ, Wichers HJ and Boeriu CG. 2007. Novel peptides with tyrosinase inhibitory activity. Peptides 28, 485-495. http://dx.doi.org/10.1016/j.pep\-tides.2006.11.023. DOI |
11 | Tahergorabi R and Jaczynski J. 2012. Physicochemical changes in surimi with salt substitute. Food Chem 132, 1281-1286. . http://dx.doi.org/10.1016/j.foodchem.2011.11.104. DOI |
12 | Undeland I, Kelleher SD and Hultin HO. 2002. Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process. J Agric Food Chem 50, 7371-7379. http://dx.doi.org/10.1021/jf0404445. DOI |
13 | Watanabe H, Takai R, Sekigawa A and Hasegawa H. 1982. An estimation of the amount of protein lost in the effluent from frozen surimi manufacture. Bull Jpn Soc Sci Fish 48, 869-871. http://dx.doi.org/10.2331/suisan.48.869. DOI |
14 | Wiriyaphan C, Chitsomboon B and Yongsawadigul J. 2012. Antioxidant activity of protein hydrolysates derived from threadfin bream surimi byproducts. Food Chem 132, 104-111. http://dx.doi.org/10.1016/j.foodchem.2011.10.040. DOI |
15 | Yeo SG, Lee TG, Ahn CW, Kim IS, Gu YS, Park YH and Kim SB. 1998. Angiotensin converting enzyme inhibitory activ\-ity of skipjack/yellow tuna cooking broth. J Life Sci 8, 312-317. |
16 | Yoon IS, Lee GW, Kang SI, Park SY, Kim JS and Heu MS. 2017. Food functionality and biological activity of processed waters produced during the preparation of fish roe concentrates by cook-dried process. Korean J Fish Aquat Sci 50, 506-519. https://doi.org/10.5657/KFAS.2017.0506. |
17 | Intarasirisawat R, Benjakul S and Visessanguan W. 2012. Antioxidative and functional properties of protein hydrolysate from defatted skipjack (Katsuwonous pelamis) roe. Food Chem 135,3039-3048. http://dx.doi.org/10.1016/j.foodchem.2012.06.076. DOI |
18 | Intarasirisawat R, Benjakul S and Visessanguan W. 2011. Chemical compositions of the roes from skipjack, tongol and bonito. Food Chem 124, 1328-1334. http://dx.doi.org/10.1016/j.foodchem.2010.07.076. DOI |
19 | Intarasirisawat R, Benjakul S, Wu J and Visessanguan W. 2013. Isolation of antioxidative and ACE inhibitory peptides from protein hydrolysate of skipjack (Katsuwana pelamis) roe. J Funct Foods 5, 1854-1862. http://dx.doi.org/10.1016/j. jff.2013.09.006. DOI |
20 | Ji CI, Lee JH, Park DC, Gu YS, Kim IS, Lee TG and Kim SB. 2002. Angiotensin converting enzyme inhibitory activity in peptic hydrolysates of cooking discards from anchovy factory ship. Korean J Food Sci Technol 34, 529-532. |
21 | Jung W, Mendis E, Je J, Park P, Son BW, Kim HC, Choi YK and Kim S. 2006. Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hyperten\-sive rats. Food Chem 94, 26-32. http://dx.doi.org/10.1016/j.foodchem.2004.09.048. DOI |
22 | Joh Y and Hood LF. 1979. Preparation and properties of dehydrated clam flavor from clam processing wash water. J Food Sci 44, 1612-1614. |
23 | Kang KT, Heu MS and Kim JS. 2007. Improvement on the quality and functionality of red tanner crab cooking drip using commercial enzymes. J Korean Soc Food Sci Nutr 36, 1022-1030. DOI |
24 | Kim IS, Heu MS, Lee JS, Kim PH, Cho ML, Ahn HJ, Shim HD and Kim JS. 2001c. Quality stability of powdered soup using powder from oyster wash water. Appl Biol Chem 44, 224-229. |
25 | Kim JS and Heu MS. 2001a. Preparation of instant powdered soup using canned oyster processing waste water and its characteristics. J Korean Fish Soc 34, 285-290. |
26 | Afonso MD and Borquez R. 2002. Review of the treatment of seafood processing wastewaters and recovery of proteins therein by membrane separation processes- prospects of the ultrafiltration of wastewaters from the fish meal industry. Desalination 142, 29-45. http://dx.doi.org/10.1016/S0011-9164(01)00423-4. DOI |
27 | Binsan W, Benjakul S, Visessanguan W, Roytrakul S, Tanaka M and Kishimura H. 2008. Antioxidative activity of Mungoong, an extract paste, from the cephalothorax of white shrimp (Litopenaeus vannamei). Food Chem 106, 185-193. http://dx.doi.org/10.1016/j.foodchem.2007.05.065. DOI |
28 | Bliois MS. 1958. Antioxidant determinations by the use of a stable free radical. Nature 181, 1199-1200. DOI |
29 | Bougatef A, Nedjar-Arroume N, Manni L, Ravallec R, Barkia A, Guillochon D and Nasri M. 2010. Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinella aurita) by-products proteins. Food Chem 118, 559-565. http://dx.doi.org/10.1016/j.foodchem.2009.05.021. DOI |
30 | Can Karaca A, Low N and Nickerson M. 2011. Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction. Food Res Int 44, 2742-2750. http://dx.doi.org/10.1016/j.foodres.2011.06.012. DOI |
31 | Chalamaiah M, Hemalatha MD, Jyothirmayi T, Diwan PV, Bhaskarachary K, Vajreswari A, Ramesh Kumar R and Dinesh Kumar B. 2015. Chemical composition and immunomodulatory effects of enzymatic protein hydrolysates from common carp (Cyprinus carpio) egg. Nutrition 31, 388-398. http://dx.doi.org/10.1016/j.nut.2014.08.006. DOI |
32 | Chalamaiah M, Jyothirmayi T, Bhaskarachary K, Vajreswari A, Hemalatha R and Dinesh Kumar B. 2013. Chemical composition, molecular mass distribution and antioxidant capacity of rohu (Labeo rohita) roe (egg) protein hydrolysates prepared by gastrointestinal proteases. Food Res Int 52, 221-229. http://dx.doi.org/10.1016/j.foodres.2013.03.020. DOI |
33 | Kim JS and Heu MS. 2001b. Preparation of instant powdered soup using oyster wash water and its characteristics. Korean J Food Sci Technol 33, 534-539. |
34 | Klomklao S and Benjakul S. 2016. Utilization of tuna processing byproducts: Protein hydrolysate from skipjack tuna (Katsuwonus pelamis) viscera. J Food Process Preserv 41, e12970. http://dx.doi.org/10.1111/jfpp.12970. |
35 | Klompong V, Benjakul S, Kantachote D and Shahidi F. 2007. Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chem 102, 1317-1327. http://dx.doi.org/10.1016/j.foodchem.2006.07.016. DOI |
36 | Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685. http://dx.doi.org/10.1038/227680a0. DOI |
37 | Lee HJ, Park SH, Yoon IS, Lee GW, Kim JS and Heu MS. 2016a. Chemical composition of protein concentrate prepared from yellowfin tuna Thunnus albacores roe by cook-dried process. Fish Aquat Sci 19:12. http://dx.doi.org/10.1186/s41240-016-0012-1. DOI |
38 | Lee HJ, Lee GW, Yoon IS, Park SH, Park SY, Kim JS, Heu MS. 2016b. Preparation and characterization of protein isolate from yellowfin tuna Thunnus albacares roe by isoelectric solubilization/precipitation process. Fish Aquat Sci 19, 14:1-10. http://dx.doi.org/10.1186/S41240-016-0014-Z. DOI |
39 | Li GH, Le G.W, Shi YH and Shrestha S. 2004. Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutr Res 24, 469-486. http://dx.doi.org/10.1016/j.nu\-tres.2003.10.014. DOI |
40 | Li X, Luo Y, Shen H and You J. 2012. Antioxidant activities and functional properties of grass carp (Ctenopharyngodon idellus) protein hydrolysates. J Sci Food Agric 92, 292-298. http://dx.doi.org/10.1002/jsfa.4574. DOI |
41 | Chen YC and Jaczynski J. 2007. Gelation of protein recovered from Antarctic krill (Euphausia superba) by isoelectric solubilization/precipitation as affected by function additives. J Agric Food Chem 55, 1814-1822. http://dx.doi.org/10.1021/jf0629944. DOI |
42 | Chlapanidas T, Farago S, Lucconi G, Perteghella S, Galuzzi M, Mantelli M and Torre ML. 2013. Sericins exhibit ROS-scavenging, anti-tyrosinase, anti-elastase, and in vitro immunomodulatory activities. Int J Biol Macromol 58, 47-56. http://dx.doi.org/10.1016/j.ijbiomac.2013.03.054. DOI |
43 | Cho SY, Joo DS, Park SH, Kang HJ and Jeon JK. 2000. Change of taurine content in squid meat during squid processing and taurine content in the squid processing waste water. Korean J Fish Aquat Sci 33, 51-54. |
44 | Chobert JM, Bertrand-Harb C and Nicolus MG. 1988. Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin. J Agric Food Chem 36, 883-892. http://dx.doi.org/10.1021/jf00083a002. DOI |
45 | Choi JI, Kim JH and Lee JW. 2011. Physiological properties of tuna cooking drip hydrolysate prepared with gamma irradiation. Process Biochem 46, 1875-1878. http://dx.doi.org/10.1016/j.procbio.2011.06.005. DOI |
46 | Choi JS, Jang DB, Moon HE, Roh MK, Kim YD, Cho KK and Choi IS. 2017. Physiological properties of Engraulis japonicus muscle protein hydrolysates prepared by subcritical water hydrolysis. J Eviron Biol 38, 283-289. |
47 | Chung IK, Kim HS, Kang KT, Choi YJ, Choi JD, Kim JS and Heu MS. 2006. Preparation and functional properties of enzymatic oyster hydrolysates. J Korean Soc Food Sci Nutr 35, 919-925. DOI |
48 | Mahmoodani F, Ghassem M, Babji AS, Yusop SM and Khosrokhavar R. 2014. ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate. J Food Sci Technol 51, 1847-1856. http://dx.doi.org/10.1007/s13197-012-0742-8. DOI |
49 | Cushman DW and Cheung HS. 1971. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem Pharm 20, 1637-1648. http://dx.doi.org/10.1016/0006-2952(71)90292-9. DOI |
50 | Mahmoud KA, Linder M, Fanni J and Parmentier M. 2008. Characterisation of the lipid fractions obtained by proteolytic and chemical extractions from rainbow trout (Oncorhyn\-chus mykiss) roe. Process Biochem 43, 376-383. http://dx.doi.org/10.1016/j.procbio.2008.01.011. DOI |
51 | Marklund S and Marklund G. 1974. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. The FEBS Journal 47, 469-474. http://dx.doi.org/10.1111/j.1432-1033.1974.tb03714.x. |
52 | Masaki H. 2010. Role of antioxidants in the skin: Anti-aging effects. J Dermatol Sci 58, 85-90. DOI |
53 | Mohan M, Ramachandran D, Sankar TV and Anandan R. 2007. Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus). Process Biochem 42, 1056-1062. http://dx.doi.org/10.1016/j.procbio.2007.04.005. DOI |
54 | Narsing Rao. 2014. Physico-chemical, functional and antioxidant properties of roe protein concentrates from Cyprinus carpio and Epinephelus tauvina. J Food Pharm Sci 15, 22. http://dx.doi.org/10.14499/jfps. |
55 | Oh HS, Kang KT, Kim HS, Lee JH, Jee SJ, Ha JH, Kim JS and Heu MS. 2007. Food component characteristics of seafood cooking drips. J Korean Soc Food Sci Nutr 36, 595-602. DOI |
56 | Oyaizu N, Yasumizu R, Miyama-Inaba M, Nomura S, Yoshida H, Miyawaki S, Shibata Y, Mitsuoka S, Yasunaga K and Morii S. 1988. (NZW x BXSB) F1 mouse. A new animal model of idiopathic thrombocytopenic purpura. J Exp Med. 167, 2017-2022. DOI |
57 | Lowry OH, Rosebrough NJ, Farr AL and Randall RJ. 1951. Protein measurement with the Folin phenol reagent. J Biol Chem 193, 265-275. |
![]() |