Characteristics of myoglobin and haemoglobin-mediated lipid oxidation in washed mince from bighead carp (Hypophthalmichthys nobilis) |
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| Authors: | Yaowapa ThiansilakulSoottawat Benjakul Sung Yong ParkMark P. Richards |
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| Affiliation: | a Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla 90112, Thailand
b Meat Science and Muscle Biology Laboratory, Department of Animal Sciences, University of Wisconsin-Madison, 1805 Linden Drive West, Madison, WI 53706, USA |
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| Abstract: | 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 ∼16 kDa. Haemin loss from metHb was more rapid, compared to metMb (pH 6.0, 4 °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. |
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| Keywords: | Myoglobin Haemoglobin Lipid oxidation Haem degradation Haemin loss Blood |
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