The mechanisms of the unfolding and aggregation of PSE-like chicken meat protein at extreme alkaline pHs (pH 11.0, 11.5 and 12.0) were studied and related to the physical properties of edible films. Results of asymmetrical flow field-flow fractionation coupled with various detectors showed that pH 12.0 leads to a certain degree of protein aggregation, which could also be observed in atomic force microscopy (AFM) images. Higher levels of protein denaturation and unfolding, as proved by the circular dichroism spectrum, could induce this aggregation, whereas all pH-adjusted groups exhibited similar flow behavior. The pH 11.0 sample exhibited films with higher water resistance compared to others.Comparatively, solubilizing PSE-like meat protein at pH 11.5 could result in better edible films with greater mechanical properties, water resistance and transparency. Our results elucidated the effects of the PSE-like chicken meat protein unfolding and aggregation on edible film properties under various extreme alkaline pH conditions.

Protein unfolding and aggregation of PSE-like chicken meat protein at an extreme alkaline pH: Influence on edible film-forming properties

2019 Fall National Meeting

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