4.7 Article

Attributes of lipid, oxidation due to bovine myoglobin, hemoglobin and hemolysate

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

  1. National Research Initiative from USDA National Institute of Food and Agriculture, Improving Food Quality [2014-67017-21648, A1361]
  2. NIFA [2014-67017-21648, 687612] Funding Source: Federal RePORTER

向作者/读者索取更多资源

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。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据