Antioxidative properties of albumins in enzymatically catalyzed model systems

• Autorzy: Wolosiak R. , Klepacka M.
• Języki publikacji: EN

Abstrakty

EN

The activity of plant origin albumins (obtained from dark and light pea (Pisum sativum) seeds and from white and brown bean (Phaseolus vulgaris) seeds) and animal origin albumins (ovoalbumin, BSA and human) in 2 enzymatically catalyzed model systems as well as their aromatic hydrophobicity and sulfhydryl groups content were investigated. Pea and bean albumins were much more effective in decreasing the production of superoxide anion radicals in hypoxanthine/xanthine oxidase system (82-97%) than animal-derived preparations (6-26%), whereas no big differences in activity were found when oxidation of linoleic acid by lipoxydase was monitored. No unequivocal correlation between sulfhydryl groups content or aromatic hydrophobicity and the antioxidant properties of preparations was observed.

Słowa kluczowe

EN

enzymatic oxidation; legume albumin; albumin; lipoxydase; antioxidative property; Phaseolus vulgaris; brown bean; antioxidant; pea; superoxide anion radical; Pisum sativum; seed

• Wydawca: -
• Czasopismo: Electronic Journal of Polish Agricultural Universities. Series Food Science and Technology
• Rocznik: 2002
• Tom: 05
• Numer: 1
• Opis fizyczny: http://www.ejpau.media.pl

Twórcy

autor

Wolosiak R.

• Warsaw Agricultural University, Nowoursynowska 159c, 02-787 Warsaw, Poland

autor

Klepacka M.

Bibliografia

• Bressani, R., 1993. Grain quality of common bean. Food Rev. Int., 9, 237-297
• Chen, H-M., Muramoto, K., Yamauchi, F., Nokihara, K., 1996.: Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein. J. Agric. Food Chem., 44, 2619-2623
• Haskard, C., Li-Chan, E., 1998. Hydrophobicity of bovine serum albumin and ovoalbumin determined using uncharged (PRODAN) and anionic (ANS-) fluorescent probes. J. Agric. Food Chem., 46, 2617-2677
• Hayakawa, S., Nakai, S., 1985. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J. Food Sci., 50, 486-491
• Hayes, R.E., Bookwalter, G.N., Bagley E.B., 1977. Antioxidant activity of soybean flour and derivatives - a review. J. Food Sci., 42, 1527-1532
• Kato, A., Osako, Y., Matsudomi, N., Kobayashi, K., 1983. Changes in the emulsifying and foaming properties of proteins during heat denaturation. Agric. Biol. Chem., 47, 33-37
• Leterme, P., Monmart, T., Baudart E., 1990. Amino acid composition of pea (Pisum sativum) proteins and protein profile of pea flour. J. Sci. Food Agric., 53, 107-110
• Maniak, B., Targoński, Z., 1996. Przeciwutleniacze naturalne występujące w żywności. [Natural antioxidants occuring in foods] Przem. Ferment. Owoc-Warz., 40, 7-10 [in Polish]
• Martineau, A., Mercier, Y., Marinova, P., Tassy, C., Gatellier, P., Renerre, M., 1997. Comparison of oxidative processes on myofibrillar proteins from beef during maturation and by different model oxidation systems. J. Agric. Food Chem., 45, 2481-2487
• Larson, R.A., 1988. The antioxidants of higher plants. Phytochemistry, 27, 969-978
• Soyer, A., Hultin, H.O., 2000. Kinetics of oxidation of the lipids and proteins of Cod Sarkoplasmatic reticulum. J. Agric. Food Chem., 48, 2127-2134
• Wettasinghe, M., Shahidi, F., 1999. Evening primrose meal: a source of natural antioxidants and scavenger of hydrogen peroxide and oxygen-derived free radicals. J. Agric. Food Chem., 47, 1801-1812
• Yen, G-C., Chen, H-Y., 1995. Antioxidant activity of various tea extracts in relation to their antimutagenicity. J. Agric. Food Chem., 43, 27-32