Discrimination of in vitro and in vivo digestion products of meat proteins from pork,beef, chicken,and fish |
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| Authors: | Siying Wen Guanghong Zhou Shangxin Song Xinglian Xu Josef Voglmeir Li Liu Fan Zhao Mengjie Li Li Li Xiaobo Yu Yun Bai Chunbao Li |
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| Affiliation: | 1. Key Laboratory of Meat Processing and Quality Control, MOE, Synergetic Innovation Center of Food Safety and Nutrition, Jiangsu Innovation Center of Meat Production and Processing, Key Laboratory of Animal Products Processing, MOA, Synergetic Innovation Center of Meat Processing and Quality Control, Nanjing Agricultural University, Nanjing, P. R. China;2. Glycomics and Glycan Bioengineering Research Center, College of Food Science and Technology, Nanjing Agricultural University, Nanjing, P. R. China |
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| Abstract: | 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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| Keywords: | Animal proteomics Digestibility Meat protein Peptide sequence Peptidomics |
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