Characteristics of myoglobin and haemoglobin-mediated lipid oxidation in washed mince from bighead carp (Hypophthalmichthys nobilis)

被引：31
|
作者：
Thiansilakul, Yaowapa [1 ]
Benjakul, Soottawat [1 ]
Park, Sung Yong [2 ]
Richards, Mark P. [2 ]
机构：
[1] Prince Songkla Univ, Fac Agroind, Dept Food Technol, Hat Yai 90112, Songkhla, Thailand
[2] Univ Wisconsin, Dept Anim Sci, Meat Sci & Muscle Biol Lab, Madison, WI 53706 USA
来源：
FOOD CHEMISTRY | 2012年 / 132卷 / 02期
关键词：
Myoglobin; Haemoglobin; Lipid oxidation; Haem degradation; Haemin loss; Blood; HEME; FISH; LIPOXYGENASE; STABILITY; EASTERN; MUSCLE; ACID; PH;
D O I：
10.1016/j.foodchem.2011.11.060
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
Myoglobin (Mb) and haemoglobin (Hb) accounted for 61% and 39% of the total haem-protein in bighead carp (Hypophthalmichthys nobilis) dark muscle, respectively. Molecular weight of Mb and monomeric-Hb was similar to 16 kDa. Haemin loss from metHb was more rapid, compared to metMb (pH 6.0, 4 degrees C). Pro-oxidative activities of oxyMb/Hb and metMb/Hb were examined in washed mince during 9 days of iced storage (pH 6.0). Soret measurements suggested the existence of holoMb throughout storage. For Hb, weakening of haem-globin linkage was observed, especially for metHb which had undetectable Soret after 3 days of storage. Loss of redness was more rapid and extensive in washed mince containing Hb, compared to Mb. During storage, Hb induced larger amounts of peroxides, thiobarbituric acid-reactive substances and hexanal than did Mb (p < 0.05), especially for met-form. Thus, Hb had lower haemin affinity and was a stronger pro-oxidant than Mb. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码：892 / 900
页数：9
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