Abstract：
: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 result in aggregates formation, 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.
journal_name
Food Chemjournal_title
Food chemistryauthors
Zhao X,Xing T,Xu X,Zhou Gdoi
10.1016/j.foodchem.2020.126574subject
Has Abstractpub_date
2020-07-30 00:00:00pages
126574eissn
0308-8146issn
1873-7072pii
S0308-8146(20)30436-2journal_volume
319pub_type
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