Matrix metalloproteinase- 9 may contribute to collagen structure modification during postmortem aging of beef
Matrix metalloproteinases (MMPs) are responsible for the turnover of intramuscular connective tissue in live animals. We hypothesize that MMPs may play a role in postmortem aging of beef muscles for the degradation of connective tissues. Four different experiments were performed to: 1) characterize...
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Veröffentlicht in: | Meat science 2023-11, Vol.205, p.109321-109321, Article 109321 |
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creator | Koulicoff, Larissa A. Heilman, Terra Vitanza, Lauren Welter, Amelia Jeneske, Haley O'Quinn, Travis G. Hansen, Stephanie Huff-Lonergan, Elisabeth Schulte, Matthew D. Chao, Michael D. |
description | Matrix metalloproteinases (MMPs) are responsible for the turnover of intramuscular connective tissue in live animals. We hypothesize that MMPs may play a role in postmortem aging of beef muscles for the degradation of connective tissues. Four different experiments were performed to: 1) characterize MMP activity during postmortem aging of beef; 2) determine if the native beef MMP can contribute to connective tissue degradation in a simulated standard industry postmortem aging condition; 3) explore approaches to improve the native beef MMP activity and 4) characterize MMP activity in beef from cattle supplemented with supranutritional level of Zn. In experiment 1, MMP was active throughout the entire aging periods (3, 21, 42 and 63 d) for beef muscles Longissimus lumborum, Gluteus medius and Gastrocnemius, and the unknown MMP responsible for the collagen degradation was identified as MMP-9 by Western Blot. In experiment 2 and 3, MMP-9 activity was noticeable in the gels after 42 d of storage in the cooler. Moreover, the addition of ZnCl₂ in the model system significantly increased MMP-9 activity when compared to the control (P < 0.01). In experiment 4, Longissimus thoracis from animals supplemented with a supranutritional Zn level had increased Zn availability and MMP-9 activity than those from animals fed with a control diet (P < 0.05). Further research is needed better understand MMP-9 mechanism during postmortem aging of meat. With a better understanding of MMP-9 in the aging process, the beef industry can provide better connective tissue management strategies for lower-quality beef cuts. |
doi_str_mv | 10.1016/j.meatsci.2023.109321 |
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We hypothesize that MMPs may play a role in postmortem aging of beef muscles for the degradation of connective tissues. Four different experiments were performed to: 1) characterize MMP activity during postmortem aging of beef; 2) determine if the native beef MMP can contribute to connective tissue degradation in a simulated standard industry postmortem aging condition; 3) explore approaches to improve the native beef MMP activity and 4) characterize MMP activity in beef from cattle supplemented with supranutritional level of Zn. In experiment 1, MMP was active throughout the entire aging periods (3, 21, 42 and 63 d) for beef muscles Longissimus lumborum, Gluteus medius and Gastrocnemius, and the unknown MMP responsible for the collagen degradation was identified as MMP-9 by Western Blot. In experiment 2 and 3, MMP-9 activity was noticeable in the gels after 42 d of storage in the cooler. Moreover, the addition of ZnCl₂ in the model system significantly increased MMP-9 activity when compared to the control (P < 0.01). In experiment 4, Longissimus thoracis from animals supplemented with a supranutritional Zn level had increased Zn availability and MMP-9 activity than those from animals fed with a control diet (P < 0.05). Further research is needed better understand MMP-9 mechanism during postmortem aging of meat. With a better understanding of MMP-9 in the aging process, the beef industry can provide better connective tissue management strategies for lower-quality beef cuts.</description><identifier>ISSN: 0309-1740</identifier><identifier>EISSN: 1873-4138</identifier><identifier>DOI: 10.1016/j.meatsci.2023.109321</identifier><language>eng</language><subject>beef ; beef industry ; cattle ; collagen ; diet ; longissimus muscle ; meat science ; metalloproteinases ; Western blotting</subject><ispartof>Meat science, 2023-11, Vol.205, p.109321-109321, Article 109321</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c319t-f08a714225a7ecf92802132f56202d91f7243a5977b03a02ecacc4ad8e54ee5d3</citedby><cites>FETCH-LOGICAL-c319t-f08a714225a7ecf92802132f56202d91f7243a5977b03a02ecacc4ad8e54ee5d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids></links><search><creatorcontrib>Koulicoff, Larissa A.</creatorcontrib><creatorcontrib>Heilman, Terra</creatorcontrib><creatorcontrib>Vitanza, Lauren</creatorcontrib><creatorcontrib>Welter, Amelia</creatorcontrib><creatorcontrib>Jeneske, Haley</creatorcontrib><creatorcontrib>O'Quinn, Travis G.</creatorcontrib><creatorcontrib>Hansen, Stephanie</creatorcontrib><creatorcontrib>Huff-Lonergan, Elisabeth</creatorcontrib><creatorcontrib>Schulte, Matthew D.</creatorcontrib><creatorcontrib>Chao, Michael D.</creatorcontrib><title>Matrix metalloproteinase- 9 may contribute to collagen structure modification during postmortem aging of beef</title><title>Meat science</title><description>Matrix metalloproteinases (MMPs) are responsible for the turnover of intramuscular connective tissue in live animals. We hypothesize that MMPs may play a role in postmortem aging of beef muscles for the degradation of connective tissues. Four different experiments were performed to: 1) characterize MMP activity during postmortem aging of beef; 2) determine if the native beef MMP can contribute to connective tissue degradation in a simulated standard industry postmortem aging condition; 3) explore approaches to improve the native beef MMP activity and 4) characterize MMP activity in beef from cattle supplemented with supranutritional level of Zn. In experiment 1, MMP was active throughout the entire aging periods (3, 21, 42 and 63 d) for beef muscles Longissimus lumborum, Gluteus medius and Gastrocnemius, and the unknown MMP responsible for the collagen degradation was identified as MMP-9 by Western Blot. In experiment 2 and 3, MMP-9 activity was noticeable in the gels after 42 d of storage in the cooler. Moreover, the addition of ZnCl₂ in the model system significantly increased MMP-9 activity when compared to the control (P < 0.01). In experiment 4, Longissimus thoracis from animals supplemented with a supranutritional Zn level had increased Zn availability and MMP-9 activity than those from animals fed with a control diet (P < 0.05). Further research is needed better understand MMP-9 mechanism during postmortem aging of meat. With a better understanding of MMP-9 in the aging process, the beef industry can provide better connective tissue management strategies for lower-quality beef cuts.</description><subject>beef</subject><subject>beef industry</subject><subject>cattle</subject><subject>collagen</subject><subject>diet</subject><subject>longissimus muscle</subject><subject>meat science</subject><subject>metalloproteinases</subject><subject>Western blotting</subject><issn>0309-1740</issn><issn>1873-4138</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNqFkU1LAzEQhoMoWKs_QcjRy9Z8bJrkKMUvqHjRc0izk5Ky2dQkC_bfu6W9exrm5WF4hwehe0oWlNDl424RwdbiwoIRxqdMc0Yv0IwqyZuWcnWJZoQT3VDZkmt0U8qOEEI5UzMUP2zN4RdHqLbv0z6nCmGwBRqscbQH7NIwAZuxAq5p2vrebmHApebR1TEDjqkLPjhbQxpwN-YwbPE-lRpTrhCx3R6D5PEGwN-iK2_7AnfnOUffL89fq7dm_fn6vnpaN45TXRtPlJW0ZUxYCc5rpgib6nqxnB7sNPWStdwKLeWGcEsYOOtcazsFogUQHZ-jh9Pd6Z-fEUo1MRQHU_cB0lgMp6KlS0rI8l-UKaG0klSwCRUn1OVUSgZv9jlEmw-GEnM0YXbmbMIcTZiTCf4HPF6ARA</recordid><startdate>20231101</startdate><enddate>20231101</enddate><creator>Koulicoff, Larissa A.</creator><creator>Heilman, Terra</creator><creator>Vitanza, Lauren</creator><creator>Welter, Amelia</creator><creator>Jeneske, Haley</creator><creator>O'Quinn, Travis G.</creator><creator>Hansen, Stephanie</creator><creator>Huff-Lonergan, Elisabeth</creator><creator>Schulte, Matthew D.</creator><creator>Chao, Michael D.</creator><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope></search><sort><creationdate>20231101</creationdate><title>Matrix metalloproteinase- 9 may contribute to collagen structure modification during postmortem aging of beef</title><author>Koulicoff, Larissa A. ; Heilman, Terra ; Vitanza, Lauren ; Welter, Amelia ; Jeneske, Haley ; O'Quinn, Travis G. ; Hansen, Stephanie ; Huff-Lonergan, Elisabeth ; Schulte, Matthew D. ; Chao, Michael D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c319t-f08a714225a7ecf92802132f56202d91f7243a5977b03a02ecacc4ad8e54ee5d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>beef</topic><topic>beef industry</topic><topic>cattle</topic><topic>collagen</topic><topic>diet</topic><topic>longissimus muscle</topic><topic>meat science</topic><topic>metalloproteinases</topic><topic>Western blotting</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koulicoff, Larissa A.</creatorcontrib><creatorcontrib>Heilman, Terra</creatorcontrib><creatorcontrib>Vitanza, Lauren</creatorcontrib><creatorcontrib>Welter, Amelia</creatorcontrib><creatorcontrib>Jeneske, Haley</creatorcontrib><creatorcontrib>O'Quinn, Travis G.</creatorcontrib><creatorcontrib>Hansen, Stephanie</creatorcontrib><creatorcontrib>Huff-Lonergan, Elisabeth</creatorcontrib><creatorcontrib>Schulte, Matthew D.</creatorcontrib><creatorcontrib>Chao, Michael D.</creatorcontrib><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Meat science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koulicoff, Larissa A.</au><au>Heilman, Terra</au><au>Vitanza, Lauren</au><au>Welter, Amelia</au><au>Jeneske, Haley</au><au>O'Quinn, Travis G.</au><au>Hansen, Stephanie</au><au>Huff-Lonergan, Elisabeth</au><au>Schulte, Matthew D.</au><au>Chao, Michael D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Matrix metalloproteinase- 9 may contribute to collagen structure modification during postmortem aging of beef</atitle><jtitle>Meat science</jtitle><date>2023-11-01</date><risdate>2023</risdate><volume>205</volume><spage>109321</spage><epage>109321</epage><pages>109321-109321</pages><artnum>109321</artnum><issn>0309-1740</issn><eissn>1873-4138</eissn><abstract>Matrix metalloproteinases (MMPs) are responsible for the turnover of intramuscular connective tissue in live animals. We hypothesize that MMPs may play a role in postmortem aging of beef muscles for the degradation of connective tissues. Four different experiments were performed to: 1) characterize MMP activity during postmortem aging of beef; 2) determine if the native beef MMP can contribute to connective tissue degradation in a simulated standard industry postmortem aging condition; 3) explore approaches to improve the native beef MMP activity and 4) characterize MMP activity in beef from cattle supplemented with supranutritional level of Zn. In experiment 1, MMP was active throughout the entire aging periods (3, 21, 42 and 63 d) for beef muscles Longissimus lumborum, Gluteus medius and Gastrocnemius, and the unknown MMP responsible for the collagen degradation was identified as MMP-9 by Western Blot. In experiment 2 and 3, MMP-9 activity was noticeable in the gels after 42 d of storage in the cooler. Moreover, the addition of ZnCl₂ in the model system significantly increased MMP-9 activity when compared to the control (P < 0.01). In experiment 4, Longissimus thoracis from animals supplemented with a supranutritional Zn level had increased Zn availability and MMP-9 activity than those from animals fed with a control diet (P < 0.05). Further research is needed better understand MMP-9 mechanism during postmortem aging of meat. With a better understanding of MMP-9 in the aging process, the beef industry can provide better connective tissue management strategies for lower-quality beef cuts.</abstract><doi>10.1016/j.meatsci.2023.109321</doi><tpages>1</tpages></addata></record> |
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subjects | beef beef industry cattle collagen diet longissimus muscle meat science metalloproteinases Western blotting |
title | Matrix metalloproteinase- 9 may contribute to collagen structure modification during postmortem aging of beef |
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