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Functional Properties and Bioactivities of Protein Powder Prepared from Skipjack Tuna (Katsuwonus pelamis) Liver Using the pH Shift Process
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Department of Fishery Products, Faculty of Fisheries, Kasetsart University, 50 Ngam Wong Wan Rd, Ladyao, Chatuchak, Bangkok 10900, Thailand
Pramvadee Tepwong   

Department of Fishery Products, Faculty of Fisheries, Kasetsart University, 50 Ngam Wong Wan Rd, Ladyao, Chatuchak, 10900, Bangkok, Thailand
Submission date: 2022-06-01
Acceptance date: 2022-10-07
Online publication date: 2022-11-14
Publication date: 2022-11-14
Pol. J. Food Nutr. Sci. 2022;72(4):347–359
Skipjack tuna (Katsuwonus pelamis) liver (TL) contains high-quality proteins which can potentially serve as an excellent source of functional protein ingredients. Thus, this study was conceptualized to evaluate the physicochemical, functional, and biological properties of proteins from TL using the pH shift process. The pH shift process was conducted through solubilization of TL at pH from 1.5 to 12.5, and the solubilized proteins at pH 2.5, 3.5, 10.5 and 11.5 were precipitated at pH 5.5. Finally, the tuna liver protein powders after the processes at pH 2.5 and 11.5 (TLP 2.5 and TLP 11.5, respectively) were obtained by freeze-drying, i.e. those with the highest extraction and protein recovery yields under acidic and alkaline conditions. Protein and lipid contents of TLPs were higher and lower, respectively, compared to the TL powder (control). Glutamic acid, aspartic acid, and alanine were prominent amino acids found in both TLPs. Foaming properties and water/oil holding capacity were higher in TLP 11.5, while protein solubility and emulsion properties were greater in TLP 2.5 compared between groups. Additionally, the DPPH• and ABTS•+ scavenging activities, as well as the angiotensin I-converting enzyme inhibitory activity, were remarkably higher in TLP 11.5 than in TLP 2.5. On the other hand, significant ferrous-ion chelating activity was observed in TLP 2.5. In conclusion, TLP 11.5 could serve as an alternative functional protein ingredient that provides essential amino acids, functional properties, and bioactivities.
ABTS – 2,2’-Azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid; ABTS•+ – 2,2’-Azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid radical cation; ACE – Angiotensin I-converting enzyme; DDW – Deionized distilled water; DPPH – 2,2-Diphenyl-1-picrylhydrazyl; EAA – Essential amino acid; EAI – Emulsifying activity index; ESI – Emulsion stability index; EW – Egg white powder; FC – Foaming capacity; FS – Foaming stability; HAA – Hydrophobic amino acid; HPAA – Hydrophilic amino acid; OHC – Oil holding capacity; PUFAs – Polyunsaturated fatty acids; SP – Soy protein concentrate; TL – Tuna liver; TLP – Tuna liver protein powder; TLP 2.5 – Tuna liver protein powder from solubilization at pH 2.5; TLP 11.5 – Tuna liver protein powder from solubilization at pH 11.5; WHC – Water holding capacity
The research work was funded by Kasetsart University Research and Development Institute (KURDI), FF(KU)7.65 under the research program “Development of functional ingredients from by-products of canned tuna processing”.
The authors declare no conflict of interest.
Abdollahi, M., Undeland, I. (2019). Physicochemical and gel-forming properties of protein isolated from salmon, cod and herring by-products using the pH-shift method. Food Science and Technology, 101, 678–684.
AOAC. (2000). Official Methods of Analysis of AOAC International (17th ed.). Association of Official Analytical Chemists International.
Binsan, W., Benjakul, S., Visessanguan, W., Roytrakul, S., Tanaka, M., Kishimura, H. (2008). Antioxidative activity of Mungoong, an extract paste, from the cephalothorax of white shrimp (Litopenaeus vannamei). Food Chemistry, 106(1), 185–193.
Cha, J.W., Yoon, I.S., Lee, G.W., Kang, S.I., Park, S.Y., Kim, J.S., Heu, M.S. (2020). Food functionalities and bioactivities of protein isolates recovered from skipjack tuna roe by isoelectric solubilization and precipitation. Food Science & Nutrition, 8(4), 1874–1887.
Chanted, J., Panpipat, W., Cheong, L.Z., Chaijan, M. (2022). Recovery of functional proteins from pig brain using pH-shift processes. Foods, 11(5), art. no. 695.
Chomnawang, C., Yongsawatdigul, J. (2013). Protein recovery of tilapia frame by-products by pH-shift method. Journal of Aquatic Food Product Technology, 22(2), 112–120.
Department of Fisheries. (2022). The report of tuna can situation in Thailand during 2013-2021. Thailand: fisheries development policy and planning division. Retrieved from: [].
FAO. (2013). Dietary protein quality evaluation in human nutrition: report of an FAO Expert Consultation. Food and nutrition paper; 92. FAO: Rome. Food Labeling Guide.
Freitas, I.R., Gautério, G.V., Rios, D.G., Prentice, C. (2011). Functionality of protein isolates from argentine anchovy (Engraulis anchoita) residue obtained using pH shift processing. Journal of Food Science and Engineering, 1, 374–378.
Hamzeh, A., Rezaei, M., Khodabandeh, S., Motamedzadegan, A., Noruzinia, M. (2018). Antiproliferative and antioxidative activities of cuttlefish (Sepia pharaonis) protein hydrolysates as affected by degree of hydrolysis. Journal of Food Measurement and Characterization, 12(2), 721–727.
Han, J.R., Tang, Y., Li, Y., Shang, W.H., Yan, J.N., Du, Y.N., Wu, H.T., Zhu, B.W., Xiong, Y.L. (2019). Physiochemical properties and functional characteristics of protein isolates from the scallop (Patinopecten yessoensis) gonad. Journal of Food Science, 84(5), 1023-1034.
Jajić, I., Krstović, S., Glamočić, D., Jakšić, S., Abramović, B. (2013). Validation of an HPLC method for the determination of amino acids in feed. Journal of the Serbian Chemical Society, 78(6), 839–850.
Kang, T.K., Heu, M.S., Jee, S.J., Lee, J.H., Kim, H.S., Kim, J.S. (2007). Food component characteristics of tuna livers. Food Science and Biotechnology, 16(3), 367–373.
Kang, B., Myracle, A.D., Skonberg, D.I. (2018). Potential of recovered proteins from invasive green crabs (Carcinus maenas) as a functional food ingredient. Journal of the Science of Food and Agriculture, 99(4), 1748–1754.
Kasiwut, J., Youravong, W., Sirinupong, N. (2019). Angiotensin I‐converting enzyme inhibitory peptides produced from tuna cooking juice hydrolysate by continuous enzymatic membrane reactor. Journal of Food Biochemistry, 43(12), art. no. e13058.
Khumallambam, M., Rama, S., Karuppannan, R.R., Manjabhat, S.N. (2011). Antioxidant activity of protein isolate obtained by the pH shift technique from hydrolyzed and unhydrolyzed shrimp processing discards. Journal of Aquatic Food Product Technology, 20(2), 209–221.
Kim, H.J., Kang, S.G., Jaiswal, L., Li, J., Choi, J.H., Moon, S.M., Cho, J.Y., Ham, K.S. (2016). Identification of four new angiotensin I-converting enzyme inhibitory peptides from fermented anchovy sauce. Applied Biological Chemistry, 59, 25–31.
Kristinsson, H.G., Rasco, B.A. (2000). Fish protein hydrolysates: production, biochemical, and functional properties. Critical Reviews in Food Science and Nutrition, 40(1), 43–81.
Kristinsson, H.G., Theodore, A.E., Demir, N., Ingadottir, B. (2005). A comparative study between acid-and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle. Journal of Food Science, 70(4), 298–306.
Kristinsson, H.G., Liang, Y. (2006). Effect of pH-shift processing and surimi processing on atlantic croaker (Micropogonias undulates) muscle proteins. Journal of Food Science, 71(5), C304–C312.
Kristinsson, H.G., Lanier, T., Halldorsdottir, S.M., Geirsdóttir, M. (2013). Fish protein isolate by pH-shift. In J.W. Park (Ed.), Surimi and Surimi Seafood, CRC Press Inc., Boca Raton, Florida, USA, pp. 3–23.
Li, X., Xue, S., Zhao, X., Zhuang, X., Han, M., Xu, X., Zhou, G. (2017). Gelation properties of goose liver protein recovered by isoelectric solubilisation/precipitation process. International Journal of Food Science & Technology, 53(2), 356–364.
Lone, D.A., Wani, N.A., Wani, I.A., Masoodi, F.A. (2015). Physicochemical and functional properties of rainbow trout fish protein isolate. International Food Research Journal, 22(3), 1112–1116.
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193(1), 265–275.
Marmon, S.K., Undeland, I. (2010). Protein isolation from gutted herring (Clupea harengus) using pH-shift processes. Journal of Agricultural and Food Chemistry, 58(19), 10480–10486.
Nakajima, K., Yoshie-Stark, Y., Ogushi, M. (2009). Comparison of ACE inhibitory and DPPH radical scavenging activities of fish muscle hydrolysates. Food Chemistry, 114(3), 844–851.
Nikoo, M., Benjakul, S., Yasemi, M., Gavlighi, H.A., Xu, X. (2019). Hydrolysates from rainbow trout (Oncorhynchus mykiss) processing by-product with different pretreatments: Antioxidant activity and their effect on lipid and protein oxidation of raw fish emulsion. LWT – Food Science and Technology, 108, 120–128.
Nolsøe, H., Undeland, I. (2009). The acid and alkaline solubilization process for the isolation of muscle proteins: state of the art. Food and Bioprocess Technology, 2(1), 1–27.
Panpipat, W., Chaijan, M. (2017). Functional properties of pH-shifted protein isolates from bigeye snapper (Priacanthus tayenus) head by-product. International Journal of Food Properties, 20(3), 596–610.
Pires, C., Costa, S., Batista, A.P., Nunes, M.C., Raymundo, A., Batista, I. (2012). Properties of protein powder prepared from Cape hake by-products. Journal of Food Engineering, 108(2), 268–275.
Sarojnalini, C., Hei, A. (2019). Fish as an important functional food for quality life. In Lagouri, V. (Ed.), Functional Foods, InTech Open E-Book, London, UK, pp. 1–19.
Shen, K., Mu, W., Xia, S., Chen, Y., Ren, H., Xie, X., Fang, Y., Huang, G. (2022). Preparation of protein powder from the liver of Yellowfin tuna (Thunnus albacores): a comparison of acid- and alkali-aided pH-shifting. Food Science and Technology (Campinas), 42, art. no. e40120.
Sun, X., Sarteshnizi, R.A., Boachie, T.T., Okagu, O.D., Abioye, R.O., Neves, R.P., Ohanenye, I.C., Udenigwe, C.C. (2020). Peptide–mineral complexes: understanding their chemical interactions, bioavailability, and potential application in mitigating micronutrient deficiency. Foods, 9(10), art. no. 1402.
Torres-Fuentes, C., Alaiz, M., Vioque, J. (2012). Iron-chelating activity of chickpea protein hydrolysate peptides. Food Chemistry, 134(3), 1585–1588.
Tseng, H.C., Lee, C.Y., Weng, W.L., Shiah, I.M. (2009). Solubilities of amino acids in water at various pH values under 298.15 K. Fluid Phase Equilibria, 285(1–2), 90–95.
Xiong, G., Gao, X., Wang, P., Xu, X., Zhou, G. (2016). Comparative study of extraction efficiency and composition of protein recovered from chicken liver by acid–alkaline treatment. Process Biochemistry, 51(10), 1629–1635.
Yen, G.C., Hsieh, P.P. (1995). Antioxidative activity and scavenging effects on active oxygen of xylose-lysine Maillard reaction products. Journal of the Science of Food and Agriculture, 67(3), 415–420.
Zhang, Y., Ma, L., Cai, L., Liu, Y., Li, J. (2017). Effect of combined ultrasonic and alkali pretreatment on enzymatic preparation of angiotensin converting enzyme (ACE) inhibitory peptides from native collagenous materials. Ultrasonics Sonochemistry, 36, 88–94.
Zhang, Y., Niu, F., Zhang, X., Lu, Z., Guo, Y., Wang, H. (2018). Controlled enzymatic hydrolysis on characteristic and antioxidant properties of soybean protein isolate-maltodextrin conjugates. International Journal of Food Properties, 21(1), 2239–2249.
Zhu, C.Z., Zhang, W.G., Kang, Z.L., Zhou, G.H., Xu, X.L. (2014). Stability of an antioxidant peptide extracted from Jinhua ham, Meat Science, 96(2), 783–789.