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Discrimination of in vitro and in vivo digestion products of meat proteins from pork, beef, chicken, and fish
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 digestio...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5049642/ https://www.ncbi.nlm.nih.gov/pubmed/26227428 http://dx.doi.org/10.1002/pmic.201500179 |
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author | Wen, Siying Zhou, Guanghong Song, Shangxin Xu, Xinglian Voglmeir, Josef Liu, Li Zhao, Fan Li, Mengjie Li, Li Yu, Xiaobo Bai, Yun Li, Chunbao |
author_facet | Wen, Siying Zhou, Guanghong Song, Shangxin Xu, Xinglian Voglmeir, Josef Liu, Li Zhao, Fan Li, Mengjie Li, Li Yu, Xiaobo Bai, Yun Li, Chunbao |
author_sort | Wen, Siying |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5049642 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-50496422016-10-06 Discrimination of in vitro and in vivo digestion products of meat proteins from pork, beef, chicken, and fish Wen, Siying Zhou, Guanghong Song, Shangxin Xu, Xinglian Voglmeir, Josef Liu, Li Zhao, Fan Li, Mengjie Li, Li Yu, Xiaobo Bai, Yun Li, Chunbao Proteomics Animal Proteomics 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. John Wiley and Sons Inc. 2015-09-10 2015-11 /pmc/articles/PMC5049642/ /pubmed/26227428 http://dx.doi.org/10.1002/pmic.201500179 Text en © 2015 The Authors. PROTEOMICS Published by Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License (http://creativecommons.org/licenses/by-nc-nd/4.0/) , which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Animal Proteomics Wen, Siying Zhou, Guanghong Song, Shangxin Xu, Xinglian Voglmeir, Josef Liu, Li Zhao, Fan Li, Mengjie Li, Li Yu, Xiaobo Bai, Yun Li, Chunbao Discrimination of in vitro and in vivo digestion products of meat proteins from pork, beef, chicken, and fish |
title | Discrimination of in vitro and in vivo digestion products of meat proteins from pork, beef, chicken, and fish |
title_full | Discrimination of in vitro and in vivo digestion products of meat proteins from pork, beef, chicken, and fish |
title_fullStr | Discrimination of in vitro and in vivo digestion products of meat proteins from pork, beef, chicken, and fish |
title_full_unstemmed | Discrimination of in vitro and in vivo digestion products of meat proteins from pork, beef, chicken, and fish |
title_short | Discrimination of in vitro and in vivo digestion products of meat proteins from pork, beef, chicken, and fish |
title_sort | discrimination of in vitro and in vivo digestion products of meat proteins from pork, beef, chicken, and fish |
topic | Animal Proteomics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5049642/ https://www.ncbi.nlm.nih.gov/pubmed/26227428 http://dx.doi.org/10.1002/pmic.201500179 |
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