This study was designed to investigate the effect of cooking on in vitro digestibility and peptide profiling of pork protein. We simulated gastrointestinal digestion of cooked pork that was treated with pepsin alone or followed by trypsin treatment. Digested products were identified using matrix-assisted laser desorption/ionization–time-of-flight mass spectrometry and liquid chromatography–mass spectrometry analyses. Cooking led to a reduction (p < 0.05) in digestibility and band intensities on sodium dodecyl sulfate–polyacrylamide gel electrophoresis gels. Peptide profiling and identification analyses also showed significant difference (p < 0.05) in the m/z ranges and number of peptides from the pepsin-digested products between raw (4 °C) and very well done samples (100 °C). Peptides sequenced from pepsin-digested samples under lower degrees of doneness disappeared as the temperature increased. Meanwhile, the trypsin cleavages appeared more consistent among different degrees of cooking. Further work may be needed to evaluate the bioavailability of the digested products under different cooking temperatures.
In vitro digestion products of proteins were compared among beef, pork, chicken, and fish. Gastric and jejunal contents from the rats fed these meat proteins were also compared. Cooked pork, beef, chicken, and fish were homogenized and incubated with pepsin alone or followed by trypsin. The digestion products with molecular weights of less than 3000 Da were identified with MALDI‐TOF‐MS and nano‐LC‐MS/MS. Gastric and jejunal contents obtained from the rats fed the four meat proteins for 7 days were also analyzed. After pepsin digestion, pork, and beef samples had a greater number of fragments in similarity than chicken and fish samples, but the in vitro digestibility was the greatest (p < 0.05) for pork and the smallest for beef samples. After trypsin digestion, the species differences were less pronounced (p > 0.05). A total of 822 and 659 peptides were identified from the in vitro and in vivo digestion products, respectively. Our results could interpret for the differences in physiological functions after the ingestion of different species of meat.
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