Evaluation of occasional nonresponse of a washed cod mince model to hemoglobin (Hb)-mediated oxidation

An emerging model to test antioxidants for application in seafoods is washed cod mince fortified with hemoglobin (Hb) as a catalyst. This system has been used to test the antioxidative activity of certain muscle extracts and some pure compounds such as BHA, BHT, TBHQ, and propyl gallate during ice storage. However, the washed cod mince model has occasionally been resistant to Hb-mediated oxidation. This has been in cases when the moisture of the model has been minimized by washes at the protein isoelectric point (pH approximately 5.5) to allow for large additions of potentially antioxidative solutions. In this paper, noncontrollable and controllable factors for this intriguing occasional oxidation resistance were studied. Compositional analyses (lipid content, alpha-tocopherol, and lipid hydroperoxides) and structural analysis of a "normal" oxidizing model and a stable model were done to identify any differences among them. Some controllable factors related to the model preparation that were studied included different washing pH values (5.5-6.6), Hb concentrations (7.2 and 13.5 microM), final model moisture contents (75, 81, and 90%), and light exposure during ice storage (0 h, 3-4 h, or 24 h of light/day). Results revealed a 2-fold higher alpha-tocopherol content in the stable model than in the oxidizing model. Electron microscopy images showed a more and less disrupted myofibrillar structure in the stable and the oxidizing cod model, respectively. This indicated that "cold setting" (i.e., pre-gelation) of the stable model may have occurred and prevented Hb from diffusing freely in the model. Controllable factors that reduced lipid oxidation in the models were less Hb and lower moisture.