Abstract
In this work, we investigated changes in protein structures in vacuum-packed pork during chill storage and its impact on the in vitro protein digestion. Longissimus dorsi muscles were vacuum packed and stored at 4°C for 3 days. Samples were subjected to Raman spectroscopy, in vitro digestion and nano LC-MS/MS. The 3 d samples had lower α-helix content, but higher β-sheet, β-turn, and random coil contents than the 0 d samples (P < 0.05). SDS-PAGE revealed significant protein degradation in the 3 d samples and the differences in digested products across the storage time. Proteome analysis indicated that the 3 d samples had the higher susceptibility to digestion. Increasing protein digestibility was mainly attributed to the degradation of myofibrillar proteins. Thus, exposure of more enzymatic sites in loose protein structure during chill storage could increase protein degradation in meat.
Highlights
Postmortem aging and its impact on eating quality of fresh meat has been widely concerned [1,2,3]
Protein oxidation may occur in fresh meat during chill storage [9], which may cause the formation of disulfide bonds, and a decrease in protein hydrophilicity and water holding capacity
We investigated the structural changes of meat proteins in pork during chill storage and their impacts on protein digestibility and the release of bioactive peptides
Summary
Postmortem aging and its impact on eating quality of fresh meat has been widely concerned [1,2,3]. Physicochemical and structural changes in meat proteins occurring in postmortem aging and processing may affect the protein digestion and nutritional value of meat [4,5,6]. Protein oxidation may occur in fresh meat during chill storage [9], which may cause the formation of disulfide bonds, and a decrease in protein hydrophilicity and water holding capacity. To avoid such changes, vacuum packaging and chill storage have been widely applied [10].
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