Effect of salmon protamine on the physicochemical properties of porcine myofibril
Though salmon protamine (PRO) is known to exhibit strong antibacterial action, the effect of PRO on the physicochemical properties of porcine myofibril (Mf) are not yet fully understood. In this study, we investigated the effect of PRO on the rheological properties of Mf proteins. The viscosity of t...
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| Veröffentlicht in: | FOOD SCIENCE AND TECHNOLOGY RESEARCH 2021, Vol.27(6), pp.915-921 |
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| container_title | FOOD SCIENCE AND TECHNOLOGY RESEARCH |
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| creator | Miyaguchi, Yuji Sasaki, Shun Shibuya, Tomomi Ogawa, Yasuki |
| description | Though salmon protamine (PRO) is known to exhibit strong antibacterial action, the effect of PRO on the physicochemical properties of porcine myofibril (Mf) are not yet fully understood. In this study, we investigated the effect of PRO on the rheological properties of Mf proteins. The viscosity of the Mf homogenate decreased with increasing PRO in a concentration-dependent manner. The breaking stress of the thermal gel was reduced in the presence of PRO. Scanning electron microscopy examination showed that PRO had a 3-dimensional network structure with thread-like protein filaments. SDS-PAGE analysis demonstrated that myosin binding protein-C and myosin light chain 1 in Mf were solubilized by the addition of PRO. However, PRO inhibited the solubilization of α-actinin. These results showed that PRO had an adverse effect on the gelling properties of porcine Mf through the protein-protein interaction between PRO and Mf proteins. |
| doi_str_mv | 10.3136/fstr.27.915 |
| format | Article |
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In this study, we investigated the effect of PRO on the rheological properties of Mf proteins. The viscosity of the Mf homogenate decreased with increasing PRO in a concentration-dependent manner. The breaking stress of the thermal gel was reduced in the presence of PRO. Scanning electron microscopy examination showed that PRO had a 3-dimensional network structure with thread-like protein filaments. SDS-PAGE analysis demonstrated that myosin binding protein-C and myosin light chain 1 in Mf were solubilized by the addition of PRO. However, PRO inhibited the solubilization of α-actinin. These results showed that PRO had an adverse effect on the gelling properties of porcine Mf through the protein-protein interaction between PRO and Mf proteins.</description><identifier>ISSN: 1344-6606</identifier><identifier>EISSN: 1881-3984</identifier><identifier>DOI: 10.3136/fstr.27.915</identifier><language>eng ; jpn</language><publisher>Tsukuba: Japanese Society for Food Science and Technology</publisher><subject>Actinin ; Filaments ; Gel electrophoresis ; gelation ; Myosin ; Physicochemical properties ; porcine myofibril ; Protamine ; Protein interaction ; Protein structure ; Proteins ; Rheological properties ; Salmon ; Scanning electron microscopy ; Sodium lauryl sulfate ; Solubilization ; viscosity</subject><ispartof>Food Science and Technology Research, 2021, Vol.27(6), pp.915-921</ispartof><rights>2021 by Japanese Society for Food Science and Technology</rights><rights>Copyright Japan Science and Technology Agency 2021</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c391t-dc5b1a6b396844e7b60f03f9cba35fa40f096c8511df58ed7daa56d34dca2e0c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids></links><search><creatorcontrib>Miyaguchi, Yuji</creatorcontrib><creatorcontrib>Sasaki, Shun</creatorcontrib><creatorcontrib>Shibuya, Tomomi</creatorcontrib><creatorcontrib>Ogawa, Yasuki</creatorcontrib><creatorcontrib>Ibaraki University</creatorcontrib><creatorcontrib>College of Agriculture</creatorcontrib><title>Effect of salmon protamine on the physicochemical properties of porcine myofibril</title><title>FOOD SCIENCE AND TECHNOLOGY RESEARCH</title><addtitle>Food Science and Technology Research</addtitle><description>Though salmon protamine (PRO) is known to exhibit strong antibacterial action, the effect of PRO on the physicochemical properties of porcine myofibril (Mf) are not yet fully understood. In this study, we investigated the effect of PRO on the rheological properties of Mf proteins. The viscosity of the Mf homogenate decreased with increasing PRO in a concentration-dependent manner. The breaking stress of the thermal gel was reduced in the presence of PRO. Scanning electron microscopy examination showed that PRO had a 3-dimensional network structure with thread-like protein filaments. SDS-PAGE analysis demonstrated that myosin binding protein-C and myosin light chain 1 in Mf were solubilized by the addition of PRO. However, PRO inhibited the solubilization of α-actinin. These results showed that PRO had an adverse effect on the gelling properties of porcine Mf through the protein-protein interaction between PRO and Mf proteins.</description><subject>Actinin</subject><subject>Filaments</subject><subject>Gel electrophoresis</subject><subject>gelation</subject><subject>Myosin</subject><subject>Physicochemical properties</subject><subject>porcine myofibril</subject><subject>Protamine</subject><subject>Protein interaction</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Rheological properties</subject><subject>Salmon</subject><subject>Scanning electron microscopy</subject><subject>Sodium lauryl sulfate</subject><subject>Solubilization</subject><subject>viscosity</subject><issn>1344-6606</issn><issn>1881-3984</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNpFkF1LwzAUhoMoOKdX_oGCl9KZr6bpjSBjTmEggl6HNB-2o21qkl3s35vSMW-SHPKc9z3nBeAewRVBhD3ZEP0Kl6sKFRdggThHOak4vUxvQmnOGGTX4CaEPYSoqDhegM-NtUbFzNksyK53QzZ6F2XfDiZLRWxMNjbH0CqnGtO3SnYTMBofWxOmrtF5NcH90dm29m13C66s7IK5O91L8P26-Vq_5buP7fv6ZZcrUqGYa1XUSLKaVIxTasqaQQuJrVQtSWElTVXFFC8Q0rbgRpdayoJpQrWS2EBFluBh1k3z_B5MiGLvDn5IlgIzWBBMMOWJepwp5V0I3lgx-raX_igQFFNmYspM4FKkzBK9nene6GlXN3Rpt39h21PrnE4OECMBIS4hEzApwdSdDozSbpxzmpSeZ6V9iPLHnF1lCk515uzKTtbnD9VIL8xA_gCKy46F</recordid><startdate>20210101</startdate><enddate>20210101</enddate><creator>Miyaguchi, Yuji</creator><creator>Sasaki, Shun</creator><creator>Shibuya, Tomomi</creator><creator>Ogawa, Yasuki</creator><general>Japanese Society for Food Science and Technology</general><general>The Japanese Society for Food Science and Technology</general><general>Japan Science and Technology Agency</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7QR</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope></search><sort><creationdate>20210101</creationdate><title>Effect of salmon protamine on the physicochemical properties of porcine myofibril</title><author>Miyaguchi, Yuji ; Sasaki, Shun ; Shibuya, Tomomi ; Ogawa, Yasuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-dc5b1a6b396844e7b60f03f9cba35fa40f096c8511df58ed7daa56d34dca2e0c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng ; jpn</language><creationdate>2021</creationdate><topic>Actinin</topic><topic>Filaments</topic><topic>Gel electrophoresis</topic><topic>gelation</topic><topic>Myosin</topic><topic>Physicochemical properties</topic><topic>porcine myofibril</topic><topic>Protamine</topic><topic>Protein interaction</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>Rheological properties</topic><topic>Salmon</topic><topic>Scanning electron microscopy</topic><topic>Sodium lauryl sulfate</topic><topic>Solubilization</topic><topic>viscosity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miyaguchi, Yuji</creatorcontrib><creatorcontrib>Sasaki, Shun</creatorcontrib><creatorcontrib>Shibuya, Tomomi</creatorcontrib><creatorcontrib>Ogawa, Yasuki</creatorcontrib><creatorcontrib>Ibaraki University</creatorcontrib><creatorcontrib>College of Agriculture</creatorcontrib><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>FOOD SCIENCE AND TECHNOLOGY RESEARCH</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miyaguchi, Yuji</au><au>Sasaki, Shun</au><au>Shibuya, Tomomi</au><au>Ogawa, Yasuki</au><aucorp>Ibaraki University</aucorp><aucorp>College of Agriculture</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of salmon protamine on the physicochemical properties of porcine myofibril</atitle><jtitle>FOOD SCIENCE AND TECHNOLOGY RESEARCH</jtitle><addtitle>Food Science and Technology Research</addtitle><date>2021-01-01</date><risdate>2021</risdate><volume>27</volume><issue>6</issue><spage>915</spage><epage>921</epage><pages>915-921</pages><issn>1344-6606</issn><eissn>1881-3984</eissn><abstract>Though salmon protamine (PRO) is known to exhibit strong antibacterial action, the effect of PRO on the physicochemical properties of porcine myofibril (Mf) are not yet fully understood. In this study, we investigated the effect of PRO on the rheological properties of Mf proteins. The viscosity of the Mf homogenate decreased with increasing PRO in a concentration-dependent manner. The breaking stress of the thermal gel was reduced in the presence of PRO. Scanning electron microscopy examination showed that PRO had a 3-dimensional network structure with thread-like protein filaments. SDS-PAGE analysis demonstrated that myosin binding protein-C and myosin light chain 1 in Mf were solubilized by the addition of PRO. However, PRO inhibited the solubilization of α-actinin. These results showed that PRO had an adverse effect on the gelling properties of porcine Mf through the protein-protein interaction between PRO and Mf proteins.</abstract><cop>Tsukuba</cop><pub>Japanese Society for Food Science and Technology</pub><doi>10.3136/fstr.27.915</doi><tpages>7</tpages></addata></record> |
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| subjects | Actinin Filaments Gel electrophoresis gelation Myosin Physicochemical properties porcine myofibril Protamine Protein interaction Protein structure Proteins Rheological properties Salmon Scanning electron microscopy Sodium lauryl sulfate Solubilization viscosity |
| title | Effect of salmon protamine on the physicochemical properties of porcine myofibril |
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