Influence of salting process on the structure and in vitro digestibility of actomyosin
Salting process is widely used in the process of meat products, whereas few studies have revealed the digestibility of actomyosin after salting treatment, which is closely related with the nutrition of meat. This work reported effect of salting on the structural change and digestibility of actomyosi...
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| Veröffentlicht in: | Journal of food science and technology 2020-05, Vol.57 (5), p.1763-1773 |
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| creator | Zhao, Di He, Jing Zou, Xiaoyu Nian, Yingqun Xu, Xianglian Zhou, Guanghong Li, Chunbao |
| description | Salting process is widely used in the process of meat products, whereas few studies have revealed the digestibility of actomyosin after salting treatment, which is closely related with the nutrition of meat. This work reported effect of salting on the structural change and digestibility of actomyosin before and after heat treatment. Actomyosin in 0.4 M and 0.8 M of NaCl had higher content of disulfide bonds, and actomyosin in 0.4 M NaCl showed the largest particle sizes before and after heat treatment. In addition, actomyosin in 0.6 M and 0.8 M of NaCl was oxidized more severely after heat treatment. Based on peptidomics analysis by using liquid chromatography tandem mass spectrometry (LC–MS/MS), actomyosin in 0.6 M was digested more easily, which was followed by sample in 0.8 M and 0.4 M of NaCl in descending order. The lowest digestibility of actomyosin in 0.4 M NaCl was related with its higher content of disulfide bond and severer aggregation behavior. The lower digestibility of actomyosin in 0.8 M NaCl should be related with the higher content of disulfide bonds and surface oxidation. These results highlight the crucial role of salting process in affecting the digestibility of meat protein. |
| doi_str_mv | 10.1007/s13197-019-04210-w |
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This work reported effect of salting on the structural change and digestibility of actomyosin before and after heat treatment. Actomyosin in 0.4 M and 0.8 M of NaCl had higher content of disulfide bonds, and actomyosin in 0.4 M NaCl showed the largest particle sizes before and after heat treatment. In addition, actomyosin in 0.6 M and 0.8 M of NaCl was oxidized more severely after heat treatment. Based on peptidomics analysis by using liquid chromatography tandem mass spectrometry (LC–MS/MS), actomyosin in 0.6 M was digested more easily, which was followed by sample in 0.8 M and 0.4 M of NaCl in descending order. The lowest digestibility of actomyosin in 0.4 M NaCl was related with its higher content of disulfide bond and severer aggregation behavior. The lower digestibility of actomyosin in 0.8 M NaCl should be related with the higher content of disulfide bonds and surface oxidation. These results highlight the crucial role of salting process in affecting the digestibility of meat protein.</description><identifier>ISSN: 0022-1155</identifier><identifier>EISSN: 0975-8402</identifier><identifier>DOI: 10.1007/s13197-019-04210-w</identifier><identifier>PMID: 32327787</identifier><language>eng</language><publisher>New Delhi: Springer India</publisher><subject>Actomyosin ; Aggregation behavior ; Chemical bonds ; Chemistry ; Chemistry and Materials Science ; Chemistry/Food Science ; Digestibility ; Disulfide bonds ; Food Science ; Heat treatment ; Heat treatments ; Liquid chromatography ; Mass spectrometry ; Mass spectroscopy ; Meat ; Meat products ; Nutrition ; Original ; Original Article ; Oxidation ; Salting ; Sodium chloride</subject><ispartof>Journal of food science and technology, 2020-05, Vol.57 (5), p.1763-1773</ispartof><rights>Association of Food Scientists & Technologists (India) 2019</rights><rights>Association of Food Scientists & Technologists (India) 2019.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-cca9e5393e8fd9a8e8044381c57e0d3e5e127c4ae6e058944c1ce27a3350d4223</citedby><cites>FETCH-LOGICAL-c474t-cca9e5393e8fd9a8e8044381c57e0d3e5e127c4ae6e058944c1ce27a3350d4223</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7171045/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7171045/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,41487,42556,51318,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32327787$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Di</creatorcontrib><creatorcontrib>He, Jing</creatorcontrib><creatorcontrib>Zou, Xiaoyu</creatorcontrib><creatorcontrib>Nian, Yingqun</creatorcontrib><creatorcontrib>Xu, Xianglian</creatorcontrib><creatorcontrib>Zhou, Guanghong</creatorcontrib><creatorcontrib>Li, Chunbao</creatorcontrib><title>Influence of salting process on the structure and in vitro digestibility of actomyosin</title><title>Journal of food science and technology</title><addtitle>J Food Sci Technol</addtitle><addtitle>J Food Sci Technol</addtitle><description>Salting process is widely used in the process of meat products, whereas few studies have revealed the digestibility of actomyosin after salting treatment, which is closely related with the nutrition of meat. This work reported effect of salting on the structural change and digestibility of actomyosin before and after heat treatment. Actomyosin in 0.4 M and 0.8 M of NaCl had higher content of disulfide bonds, and actomyosin in 0.4 M NaCl showed the largest particle sizes before and after heat treatment. In addition, actomyosin in 0.6 M and 0.8 M of NaCl was oxidized more severely after heat treatment. Based on peptidomics analysis by using liquid chromatography tandem mass spectrometry (LC–MS/MS), actomyosin in 0.6 M was digested more easily, which was followed by sample in 0.8 M and 0.4 M of NaCl in descending order. The lowest digestibility of actomyosin in 0.4 M NaCl was related with its higher content of disulfide bond and severer aggregation behavior. The lower digestibility of actomyosin in 0.8 M NaCl should be related with the higher content of disulfide bonds and surface oxidation. These results highlight the crucial role of salting process in affecting the digestibility of meat protein.</description><subject>Actomyosin</subject><subject>Aggregation behavior</subject><subject>Chemical bonds</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry/Food Science</subject><subject>Digestibility</subject><subject>Disulfide bonds</subject><subject>Food Science</subject><subject>Heat treatment</subject><subject>Heat treatments</subject><subject>Liquid chromatography</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Meat</subject><subject>Meat products</subject><subject>Nutrition</subject><subject>Original</subject><subject>Original Article</subject><subject>Oxidation</subject><subject>Salting</subject><subject>Sodium 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of salting process on the structure and in vitro digestibility of actomyosin</title><author>Zhao, Di ; He, Jing ; Zou, Xiaoyu ; Nian, Yingqun ; Xu, Xianglian ; Zhou, Guanghong ; Li, Chunbao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-cca9e5393e8fd9a8e8044381c57e0d3e5e127c4ae6e058944c1ce27a3350d4223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Actomyosin</topic><topic>Aggregation behavior</topic><topic>Chemical bonds</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chemistry/Food Science</topic><topic>Digestibility</topic><topic>Disulfide bonds</topic><topic>Food Science</topic><topic>Heat treatment</topic><topic>Heat treatments</topic><topic>Liquid chromatography</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Meat</topic><topic>Meat 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Xiaoyu</au><au>Nian, Yingqun</au><au>Xu, Xianglian</au><au>Zhou, Guanghong</au><au>Li, Chunbao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Influence of salting process on the structure and in vitro digestibility of actomyosin</atitle><jtitle>Journal of food science and technology</jtitle><stitle>J Food Sci Technol</stitle><addtitle>J Food Sci Technol</addtitle><date>2020-05-01</date><risdate>2020</risdate><volume>57</volume><issue>5</issue><spage>1763</spage><epage>1773</epage><pages>1763-1773</pages><issn>0022-1155</issn><eissn>0975-8402</eissn><abstract>Salting process is widely used in the process of meat products, whereas few studies have revealed the digestibility of actomyosin after salting treatment, which is closely related with the nutrition of meat. This work reported effect of salting on the structural change and digestibility of actomyosin before and after heat treatment. Actomyosin in 0.4 M and 0.8 M of NaCl had higher content of disulfide bonds, and actomyosin in 0.4 M NaCl showed the largest particle sizes before and after heat treatment. In addition, actomyosin in 0.6 M and 0.8 M of NaCl was oxidized more severely after heat treatment. Based on peptidomics analysis by using liquid chromatography tandem mass spectrometry (LC–MS/MS), actomyosin in 0.6 M was digested more easily, which was followed by sample in 0.8 M and 0.4 M of NaCl in descending order. The lowest digestibility of actomyosin in 0.4 M NaCl was related with its higher content of disulfide bond and severer aggregation behavior. The lower digestibility of actomyosin in 0.8 M NaCl should be related with the higher content of disulfide bonds and surface oxidation. These results highlight the crucial role of salting process in affecting the digestibility of meat protein.</abstract><cop>New Delhi</cop><pub>Springer India</pub><pmid>32327787</pmid><doi>10.1007/s13197-019-04210-w</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Actomyosin Aggregation behavior Chemical bonds Chemistry Chemistry and Materials Science Chemistry/Food Science Digestibility Disulfide bonds Food Science Heat treatment Heat treatments Liquid chromatography Mass spectrometry Mass spectroscopy Meat Meat products Nutrition Original Original Article Oxidation Salting Sodium chloride |
| title | Influence of salting process on the structure and in vitro digestibility of actomyosin |
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