Effects of sodium chloride and sodium tripolyphosphate on the prooxidant properties of hemoglobin in washed turkey muscle system
This study examined the effects of sodium chloride (NaCl) and sodium tripolyphosphate (STPP) on lipid oxidation induced by oxyhemoglobin (oxyHb) in washed turkey muscle (WTM) model. To explore the reasons for observed effects, the pro-oxidant abilities of Hb derivatives (e.g., metHb, oxyHb, hemin, F...
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Format: | Article |
Language: | English |
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Elsevier
2022-12-01
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Series: | Food Chemistry: X |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157522002784 |
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author | Haizhou Wu Sung Yong Park Mark P. Richards |
author_facet | Haizhou Wu Sung Yong Park Mark P. Richards |
author_sort | Haizhou Wu |
collection | DOAJ |
description | This study examined the effects of sodium chloride (NaCl) and sodium tripolyphosphate (STPP) on lipid oxidation induced by oxyhemoglobin (oxyHb) in washed turkey muscle (WTM) model. To explore the reasons for observed effects, the pro-oxidant abilities of Hb derivatives (e.g., metHb, oxyHb, hemin, Fe2+, and Fe3+), pH change, and antioxidation of Hb in the presence of NaCl or STPP were also analyzed. The observed lipid oxidation capacity in WTM followed the order metHb > hemin > oxyHb > Fe2+ > Fe3+. Added Fe2+ accelerated auto-oxidation of oxyHb and oxyHb-mediated lipid oxidation. Hb auto-oxidation to metHb increased as the pH decreased from 6.6 to 5.0. NaCl promoted oxyHb-mediated lipid oxidation due to NaCl causing decreased pH value and increased formation of metHb. STPP inhibited oxyHb-mediated lipid oxidation and weakened the pro-oxidative effect of NaCl. This could be attributed to STPP increasing the pH, inactivating free iron, and inhibiting formation of metHb. |
first_indexed | 2024-04-11T19:53:33Z |
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id | doaj.art-40d34d0ff3ff42f2a16f2c4ba9dca6ac |
institution | Directory Open Access Journal |
issn | 2590-1575 |
language | English |
last_indexed | 2024-04-11T19:53:33Z |
publishDate | 2022-12-01 |
publisher | Elsevier |
record_format | Article |
series | Food Chemistry: X |
spelling | doaj.art-40d34d0ff3ff42f2a16f2c4ba9dca6ac2022-12-22T04:06:13ZengElsevierFood Chemistry: X2590-15752022-12-0116100480Effects of sodium chloride and sodium tripolyphosphate on the prooxidant properties of hemoglobin in washed turkey muscle systemHaizhou Wu0Sung Yong Park1Mark P. Richards2Department of Animal and Dairy Sciences, University of Wisconsin-Madison, Meat Science and Animal Biologics Discovery, 1933 Observatory Dr. Madison, WI 53706, United States; National Center of Meat Quality, Safety Control, Jiangsu Innovation Center of Meat Production, Processing, College of Food Science, Technology, Nanjing Agricultural University, Nanjing 210095, PR China; Department of Biology and Biological Engineering–Food and Nutrition Science, Chalmers University of Technology, SE 412 96 Gothenburg, Sweden; Corresponding author at: Department of Animal and Dairy Sciences, University of Wisconsin-Madison, Meat Science and Animal Biologics Discovery, 1933 Observatory Dr. Madison, WI 53706, United States.Department of Animal and Dairy Sciences, University of Wisconsin-Madison, Meat Science and Animal Biologics Discovery, 1933 Observatory Dr. Madison, WI 53706, United StatesDepartment of Animal and Dairy Sciences, University of Wisconsin-Madison, Meat Science and Animal Biologics Discovery, 1933 Observatory Dr. Madison, WI 53706, United StatesThis study examined the effects of sodium chloride (NaCl) and sodium tripolyphosphate (STPP) on lipid oxidation induced by oxyhemoglobin (oxyHb) in washed turkey muscle (WTM) model. To explore the reasons for observed effects, the pro-oxidant abilities of Hb derivatives (e.g., metHb, oxyHb, hemin, Fe2+, and Fe3+), pH change, and antioxidation of Hb in the presence of NaCl or STPP were also analyzed. The observed lipid oxidation capacity in WTM followed the order metHb > hemin > oxyHb > Fe2+ > Fe3+. Added Fe2+ accelerated auto-oxidation of oxyHb and oxyHb-mediated lipid oxidation. Hb auto-oxidation to metHb increased as the pH decreased from 6.6 to 5.0. NaCl promoted oxyHb-mediated lipid oxidation due to NaCl causing decreased pH value and increased formation of metHb. STPP inhibited oxyHb-mediated lipid oxidation and weakened the pro-oxidative effect of NaCl. This could be attributed to STPP increasing the pH, inactivating free iron, and inhibiting formation of metHb.http://www.sciencedirect.com/science/article/pii/S2590157522002784Heme proteinMeatNaClSTPPHeminAuto-oxidation |
spellingShingle | Haizhou Wu Sung Yong Park Mark P. Richards Effects of sodium chloride and sodium tripolyphosphate on the prooxidant properties of hemoglobin in washed turkey muscle system Food Chemistry: X Heme protein Meat NaCl STPP Hemin Auto-oxidation |
title | Effects of sodium chloride and sodium tripolyphosphate on the prooxidant properties of hemoglobin in washed turkey muscle system |
title_full | Effects of sodium chloride and sodium tripolyphosphate on the prooxidant properties of hemoglobin in washed turkey muscle system |
title_fullStr | Effects of sodium chloride and sodium tripolyphosphate on the prooxidant properties of hemoglobin in washed turkey muscle system |
title_full_unstemmed | Effects of sodium chloride and sodium tripolyphosphate on the prooxidant properties of hemoglobin in washed turkey muscle system |
title_short | Effects of sodium chloride and sodium tripolyphosphate on the prooxidant properties of hemoglobin in washed turkey muscle system |
title_sort | effects of sodium chloride and sodium tripolyphosphate on the prooxidant properties of hemoglobin in washed turkey muscle system |
topic | Heme protein Meat NaCl STPP Hemin Auto-oxidation |
url | http://www.sciencedirect.com/science/article/pii/S2590157522002784 |
work_keys_str_mv | AT haizhouwu effectsofsodiumchlorideandsodiumtripolyphosphateontheprooxidantpropertiesofhemoglobininwashedturkeymusclesystem AT sungyongpark effectsofsodiumchlorideandsodiumtripolyphosphateontheprooxidantpropertiesofhemoglobininwashedturkeymusclesystem AT markprichards effectsofsodiumchlorideandsodiumtripolyphosphateontheprooxidantpropertiesofhemoglobininwashedturkeymusclesystem |