ABSTRACTThe effect of heat treatment on a model protein, sperm whale myoglobin, at various water contents has been investigated at neutral pH. Samples ranging from solid preparations of 3 water content to dilute solutions of 99.6 water content have been examined. Differential scanning calorimetry (DSC) has been used for the heat treatments as well as for analyzing the effect of the heat treatments on the protein samples. At water contents below 30 only a certain fraction of the heat‐treated protein sample underwent irreversible transitions. This fraction of the protein sample increased linearly with the amount of water present during the heat treatment. Above 30 water content the entire protein sample underwent irreversible transitions. The heating rate was shown to influence the transition temperature as well as the apparent transition heat. Possible applications in food technology and food processing of the DSC technique used are discusse
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