DETERMINATION OF PROTEIN OXIDATION IN AQUACULTURE FEED
Abstract
This research aimed to develop a reliable, easy-to-perform and cheap method for measuring protein oxidation in complex samples such as aquaculture feed within various protein sources. For that purpose modified 2,4-dinitrophenylhydrazine (DNPH)-based method for quantification of protein carbonyls was employed whilst the modification of the method consisted of using different solutions for the extraction (distilled water and different concentrations of KCl and NaCl solutions), time of protein extraction (after homogenization and over the night) and concentration of trichloracetic acid (10 and 25% TCA) for protein precipitation. Extraction during the night, higher TCA concentration and the use of 0.5 M KCl extraction solution resulted in the highest protein amount measured by the Lowry method and 280 nm protein estimation. On the other hand, the lowest protein yield was obtained by using distilled water for the extraction. Furthermore, the lowest amount of protein carbonyls was in the case when extraction was performed with distilled water (DW), while the highest content of protein carbonyls was reached with 0.15 M KCl and 0.5 M KCl extraction solutions. It was observed that the amount of protein-bound carbonyls compounds was increasing during storage under accelerated conditions and, in comparison to the original method, the modified method for measuring protein oxidation resulted in a higher amount of carbonyls during all points of storage.
References
Armenteros, M., Heinonen, M., Ollilainen, V., Toldrá, F., & Estevez, M. (2009). Analysis of protein carbonyls in meat products by using the DNPH-method, fluorescence spectroscopy and liquid chromatography–electrospray ionisation–mass spectrometry (LC–ESI–MS). Meat Science, 83(1), 104-112. https://doi.org/10.1016/j.meatsci.2009.04.007
Ayadi, F. Y., Rosentrater, K, A., & Muthukumarappan, K. (2012). Alternative protein sources for aquaculture feeds. Journal of Aquaculture Feed Science and Nutrition, 4(1), 1-26.
Boyd, C. E., & Polioudakis, M. (2006, April 1). Land use for aquaculture production. Retrieved from Global Aquaculture Advocate, https://www.aquaculturealliance.org/advocate/land-use-for-aquaculture-production
Chen, N., Zhao, M., Chassenieux, C., & Nicolai, T. (2016). Data on the characterization of native soy globulin by SDS-Page, light scattering and titration. Data in Brief, 9, 749-752. http://dx.doi.org/10.1016/j.foodhyd.2015.12.028
Chookird, D., Tantikitti, C., Pongdara, A., & Srichanun, M. (2010). Effect of hemoglobin powder substituted for fishmeal on growth performance, protein digestibility, and trypsin gene expression in Litopenaeusvannamei. Songklanakarin Journal of Science & Technology, 32(2), 119-127. http://rdo.psu.ac.th/sjst/journal/32-2/0125-3395-32-2-119-127.pdf
Davis, D. A. (2015). Feed and feeding practices in aquaculture (1st ed., pp 128-150). Cambridge, UK: Woodhead Publishing.
Decker, E. A., Faustman, C., & Lopez-Bote, C. J. (2000). Antioxidants in muscle foods: nutritional strategies to improve quality (1st edition ). New York, USA: John Wiley & Sons.
Estévez, M., Ventanas, S., & Heinonen, M. (2011). Formation of Strecker aldehydes between protein carbonyls–α-aminoadipic and γ-glutamic semialdehydes–and leucine and isoleucine. Food Chemistry, 128(4), 1051-1057. https://doi.org/10.1016/j.foodchem.2011.04.012
Eymard, S., Baron, C. P., & Jacobsen, C. (2009). Oxidation of lipid and protein in horse mackerel (Trachurustrachurus) mince and washed minces during processing and storage. Food Chemistry, 114(1), 57-65. https://doi.org/10.1016/j.foodchem.2008.09.030
(FAO) Food and Agricultural Organization. (2012). State of Food and Agriculture 2012: Investing in Agriculture for a Better Future. https://www.fao.org/publications/sofa/2012/en/
Guyon, C., Meynier, A., & de Lamballerie, M. (2016). Protein and lipid oxidation in meat: A review with emphasis on high-pressure treatments. Trends in Food Science & Technology, 50, 131-143. https://doi.org/10.1016/j.tifs.2016.01.026
Hu, X. Z., Cheng, Y. Q., Fan, J. F., Lu, Z. H., Yamaki, K., & Li, L. T. (2010). Effects of drying method on physicochemical and functional properties of soy protein isolates. Journal of Food Processing and Preservation, 34(3), 520-540. https://doi.org/10.1111/j.1745-4549.2008.00357.x
Huntington, T. C., & Hasan, M. R. (2009). Fish as feed inputs for aquaculture–practices, sustainability and implications: a global synthesis. FAO Fisheries and Aquaculture Technical Paper, 518, 1-61. http://www.fao.org/3/i1140e/i1140e01.pdf
Jin, D. X., Liu, X. L., Zheng, X. Q., Wang, X. J., & He, J. F. (2016). Preparation of antioxidative corn protein hydrolysates, purification and evaluation of three novel corn antioxidant peptides. Food Chemistry, 204, 427-436. https://doi.org/10.1016/j.foodchem.2016.02.119
Jobling, M. (2012). National Research Council (NRC): Nutrient requirements of fish and shrimp. Aquaculture International, 20, 601–602. https://doi.org/10.1007/s10499-011-9480-6.
Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature, 227, 680-685. https://doi.org/10.1038/227680a0
Levine, R. L., Garland, D., Oliver, C. N., Amici, A., Climent, I., Lenz, A., Ahn, B., Shaltiel, S., & Stadtman, E. R. (1990). Determination of carbonyl content in oxidatively modified proteins. Methods Enzymology, 186, 464-478. https://doi.org/10.1016/0076-6879(90)86141-H
Levine, R. L., & Stadtman, E. R. (2001).Oxidative modification of proteins during aging. Experimental Gerontology, 36(9), 1495-1502. https://doi.org/10.1016/S0531-5565(01)00135-8
Levine, R. L., Williams, J. A., Stadtman, E. P., & Shacter, E. (1994). Carbonyl assays for determination of oxidatively modified proteins. Methods in Enzymology, 233, 346-357. https://doi.org/10.1016/S0076-6879(94)33040-9
Lowry, O., Rosenbrough, N., Fair, A., & Randall, R. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193, 265-275. https://www.cabdirect.org/cabdirect/abstract/19511404458
Lund, M. N., Lametsch, R., Hviid, M. S., Jensen, O. N., & Skibsted, L. H. (2007). High-oxygen packaging atmosphere influences protein oxidation and tenderness of porcine longissimus dorsi during chill storage. Meat Science, 77(3), 295-303. https://doi.org/10.1016/j.meatsci.2007.03.016
Mandal, S., & Mandal, R. K. (2000). Seed storage proteins and approaches for improvement of their nutritional quality by genetic engineering. Current Science, 79(5), 576-587. https://www.jstor.org/stable/24105073
Mæhre, H. K., Dalheim, L., Edvinsen, G. K., Elvevoll, E. O., & Jensen, I. J. (2018). Protein determination—method matters. Foods, 7(1), 5. https://doi.org/10.3390/foods7010005
Mitra, B., Lametsch, R., Akcan, T., & Ruiz-Carrascal, J. (2018). Pork proteins oxidative modifications under the influence of varied time-temperature thermal treatments: A chemical and redox proteomics assessment. Meat Science, 140, 134-144. https://doi.org/10.1016/j.meatsci.2018.03.011
Papastergiadis, A., Mubiru, E., Van Langenhove, H., & De Meulenaer, B. (2012). Malondialdehyde measurement in oxidized foods: evaluation of the spectrophotometric thiobarbituric acid reactive substances (TBARS) test in various food. Journal of Agriculture and Food Chemistry, 60, 9589-9594.https://doi.org/10.1021/jf302451c
Phillips, G. O., & Williams, P. A. (Eds.).(2011). Handbook of food proteins. Cambridge, UK: Woodhead Publishing.
Popović, Lj., Stolić, Ž., Čakarević, J., Torbica, A., Tomić, J., & Šijački, M. (2017). Biologically active digests from pumpkin oil cake protein: effect of cross-linking by transglutaminase. Journal of the American Oil Chemists Society, 94, 1245-1251. https://doi.org/10.1007/s11746-017-3041-8
Porzio, M. A., & Pearson, A. M. (1977). Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochimica et Biophysica Acta (BBA)-Protein Structure, 490(1), 27-34. https://doi.org/10.1016/0005-2795(77)90102-7
Rakita, S., Čolović, D., Levart, A., Banjac, V., Čolović, R., Dragojlović, D., & Đuragić, O. (2020). A rapid spectrophotometric method for determination of thiobarbituric acid reactive substances in rainbow trout feed. Food and Feed Research, 47(1), 43-54. http://scindeks.ceon.rs/article.aspx?artid=2217-53692001043R
Recreational Fisheries FAO (2012). Technical Guidelines for Responsible Fisheries 13. Food and Agriculture Organization of the United Nations. Rome, Italy. http://www.fao.org/docrep/016/i2708e/i2708e00.htm
Reeg, S., & Grune, T. (2015). Protein oxidation in aging: does it play a role in aging progression? Antioxidants & Redox Signaling, 23(3), 239-255. https://doi.org/10.1089/ars.2014.6062
Requena, J. R., Levine, R. L., & Stadtman, E. R. (2003). Recent advances in the analysis of oxidized proteins. Amino Acids, 25(3-4), 221-226. https://doi.org/10.1007/s00726-003-0012-1
Soglia, F., Petracci, M., & Ertbjerg, P. (2016). Novel DNPH-based method for determination of protein carbonylation in muscle and meat. Food Chemistry, 197, 670-675. https://doi.org/10.1016/j.foodchem.2015.11.038
Stadman, E. R., & Levine, R. L. (2000). Protein oxidation. Annals New York Academy of Sciences, 899(1), 191-208. https://doi.org/10.1111/j.1749-6632.2000.tb06187.x
Traore, S., Aubry, L., Gatellier, P., Przybylski, W., Jaworska, D., Kajak-Siemaszko, K., & Santé-Lhoutellier, V. (2012). Effect of heat treatment on protein oxidation in pig meat. Meat Science, 91(1), 14-21. https://doi.org/10.1016/j.meatsci.2011.11.037
Weingärtner, H., Cabrele, C., & Herrmann, C. (2012). How ionic liquids can help to stabilize native proteins. Physical Chemistry Chemical Physics, 14(2), 415-426 https://doi.org/10.1007/s00726-003-0012-1