期刊
FOOD CHEMISTRY
卷 234, 期 -, 页码 230-235出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.04.182
关键词
Beef; oxyHb; oxyMb; Hemolysate; Lipid oxidation; SEC-purification
资金
- National Research Initiative from USDA National Institute of Food and Agriculture, Improving Food Quality [2014-67017-21648, A1361]
- NIFA [2014-67017-21648, 687612] Funding Source: Federal RePORTER
Bovine hemolysate was purified by size exclusion chromatography, and one high molecular weight protein was detected relative to the hemoglobin (Hb) fraction. Purified Hb promoted lipid oxidation in washed muscle slightly but significantly better than hemolysate, which may have been due to the absence of catalase and peroxiredoxin in the purified Hb. Purified Hb auto-oxidized to metHb more rapidly than Hb in the hemolysate (P < 0.05). OxyHb promoted lipid oxidation in washed muscle more effectively compared to oxyMb (P < 0.05). This was ascribed to hemin, released from metHb, promoting lipid oxidation more readily than oxidative forms of Mb that retain their protoporphyrin moiety. A 3:1 ratio of Mb:Hb promoted lipid oxidation similarly compared to adding a 1:1 ratio of Mb:Hb to washed muscle. Lipid oxidation products due to Hb-mediated lipid oxidation were elevated 60-fold at pH 6.3 compared to pH 6.7. (C) 2017 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据