ODREĐIVANJE OKSIDACIJE PROTEINA U HRANI ZA RIBE

  • Danka Dragojlović University of Novi Sad, Institute of Food Technology
Ključne reči: ekstrakcija proteina, karbonilna jedinjenja, globulini, 2,4-dinitrofenilhidrazin

Sažetak


Cilj ovog istraživanja bilo je razvijanje pouzdane, jednostavnije, jeftinije metode za merenje oksidacije proteina u složenim uzorcima, kao što je hrana za ribe, koja u svom sastavu sadrži različite izvore proteina. U tu svrhu korišćena je modifikovana metoda za kvantifikaciju proteinskih karbonila, koja je zasnovanana 2,4- dinitrofenilhidrazin (DNPH)-metodi. Modifikacija metode se sastojala u promeni rastvarača (destilovana voda različite koncentracije rastvora NaCliKCl) i vremenu ekstrakcije (nakon homogenizacije i preko noći), kao i koncentracije trihlor sirćetne kiseline (TCA, 10 i 25%) za precipitaciju proteina. Uočeno je da produženo vreme ekstrakcije (tokom noći), veća koncetracijaTCA (25%) i 0,5 M rastvor KCl-a dovodi do povećanja koncentracije proteina. S druge strane, najmanja količina proteina dobijena je ekstrakcijom pomoću destilovane vode. U pogledu količine proteinskih karbonila, pokazano je da je najveći sadržaj postignut ekstrakcijom pomoću 0,15 M i 0,5 M KCl. Tokom skladištenja uzoraka, pod ekstremnim uslovima, uočeno je da se količina karbonilnih jedinjenja povećava. A u poređenju sa originalnom metodom, modifikovanom metodom za merenje oksidacije proteina izmerena je veća količina karbonilnih jedinjenja u svakoj fazi skladištenja.

Reference

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

Objavljeno
2021/12/08
Broj časopisa
Rubrika
Originalni naučni rad