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Factors affecting the binding of trout HbI and HbIV to washed cod mince model system and their influence on lipid oxidation

Thippeswamy Sannaveerappa (Institutionen för kemi- och bioteknik, Livsmedelsvetenskap) ; He Cai ; Mark Richards ; Ingrid Undeland (Institutionen för kemi- och bioteknik, Livsmedelsvetenskap)
Food Chemistry (0308-8146). Vol. 143 (2014), p. 392-397.
[Artikel, refereegranskad vetenskaplig]

Electrostatic interactions between haemoglobin (Hb) and muscle components of fish may be an initial step of Hb-mediated lipid oxidation. This mechanism was investigated by examining the interaction of anionic HbIV and cationic Hbl with insoluble components of washed cod mince under different pH and salt conditions. Lipid oxidation was monitored in parallel using the thiobarbituric acid reactive substances (TBARS) test. Higher binding of Hbl to washed cod mince occurred compared to HbIV, yet HbIV better promoted lipid oxidation. An increase in pH from 5.7 to 6.3 and further to 7.0 lowered both Hb-binding and TBARS development. Addition of NaCl decreased Hb-binding but still did not influence Hb-mediated lipid oxidation. Thus, Hb binding had no consistent effect on lipid oxidation of washed cod mince. Rapid haemin release from the anionic Hb appeared to be a primary facilitator of lipid oxidation, overshadowing the greater binding ability of the cationic Hb. (C) 2013 Elsevier Ltd. All rights reserved.

Nyckelord: Haemoglobin; Lipid oxidation; Hb binding; TBARS; Trout Hb-type electrostatic interaction

Denna post skapades 2013-11-26. Senast ändrad 2017-02-03.
CPL Pubid: 187468


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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Livsmedelsvetenskap (2005-2014)



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