Impact of food structure on the compatibility of heated WPI-pectin-complexes in meat dispersions
Process-stable complexes composed of whey protein isolate (WPI) and sugar beet pectin have great potential as structuring agents or fat replacers in foods. The current study investigates the compatibility of heated WPI : pectin complexes in different meat matrices. Spreadable raw-fermented sausages...
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Veröffentlicht in: | Food & function 2018-03, Vol.9 (3), p.1647-1656 |
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description | Process-stable complexes composed of whey protein isolate (WPI) and sugar beet pectin have great potential as structuring agents or fat replacers in foods. The current study investigates the compatibility of heated WPI : pectin complexes in different meat matrices. Spreadable raw-fermented sausages and sliceable emulsion-type sausages were therefore manufactured containing biopolymer complexes with various WPI : pectin ratios
r
(2 : 1, 8 : 1). Macro- and microstructural properties of the meat dispersions were analyzed in terms of colour, texture, rheometry, sensory, and confocal laser scanning microscopy (CLSM) measurements. Textural and sensorial results demonstrated that the meat products became increasingly soft and yellowish as the biopolymer ratio
r
was increased regardless of the meat matrix, whereas pH and water activity values were not affected. CLSM images revealed that the meat protein network became disrupted and loose in the presence of pectin, which was attributed to a thermodynamic incompatibility effect. The results obtained from this study highlight that biopolymer complexes might be suitable fat mimetics, particularly for spreadable meat products.
Process-stable complexes composed of whey protein isolate (WPI) and sugar beet pectin have great potential as structuring agents or fat replacers in meat dispersions. |
doi_str_mv | 10.1039/c7fo01577a |
format | Article |
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r
(2 : 1, 8 : 1). Macro- and microstructural properties of the meat dispersions were analyzed in terms of colour, texture, rheometry, sensory, and confocal laser scanning microscopy (CLSM) measurements. Textural and sensorial results demonstrated that the meat products became increasingly soft and yellowish as the biopolymer ratio
r
was increased regardless of the meat matrix, whereas pH and water activity values were not affected. CLSM images revealed that the meat protein network became disrupted and loose in the presence of pectin, which was attributed to a thermodynamic incompatibility effect. The results obtained from this study highlight that biopolymer complexes might be suitable fat mimetics, particularly for spreadable meat products.
Process-stable complexes composed of whey protein isolate (WPI) and sugar beet pectin have great potential as structuring agents or fat replacers in meat dispersions.</description><identifier>ISSN: 2042-6496</identifier><identifier>EISSN: 2042-650X</identifier><identifier>DOI: 10.1039/c7fo01577a</identifier><identifier>PMID: 29469137</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Biopolymers ; Compatibility ; Confocal microscopy ; Dispersions ; Fermented food ; Food ; Incompatibility ; Lasers ; Meat ; Meat products ; Microscopy ; Pectin ; Rheometry ; Sausages ; Scanning microscopy ; Water activity ; Whey ; Whey protein</subject><ispartof>Food & function, 2018-03, Vol.9 (3), p.1647-1656</ispartof><rights>Copyright Royal Society of Chemistry 2018</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c337t-71bae6c2a6e069e69aee017cee8931ee90af3eda53ba5d9db071f5f53741129c3</citedby><cites>FETCH-LOGICAL-c337t-71bae6c2a6e069e69aee017cee8931ee90af3eda53ba5d9db071f5f53741129c3</cites><orcidid>0000-0003-3171-7082</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29469137$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zeeb, Benjamin</creatorcontrib><creatorcontrib>Schöck, Vanessa</creatorcontrib><creatorcontrib>Schmid, Nicole</creatorcontrib><creatorcontrib>Majer, Lisa</creatorcontrib><creatorcontrib>Herrmann, Kurt</creatorcontrib><creatorcontrib>Hinrichs, Jörg</creatorcontrib><creatorcontrib>Weiss, Jochen</creatorcontrib><title>Impact of food structure on the compatibility of heated WPI-pectin-complexes in meat dispersions</title><title>Food & function</title><addtitle>Food Funct</addtitle><description>Process-stable complexes composed of whey protein isolate (WPI) and sugar beet pectin have great potential as structuring agents or fat replacers in foods. The current study investigates the compatibility of heated WPI : pectin complexes in different meat matrices. Spreadable raw-fermented sausages and sliceable emulsion-type sausages were therefore manufactured containing biopolymer complexes with various WPI : pectin ratios
r
(2 : 1, 8 : 1). Macro- and microstructural properties of the meat dispersions were analyzed in terms of colour, texture, rheometry, sensory, and confocal laser scanning microscopy (CLSM) measurements. Textural and sensorial results demonstrated that the meat products became increasingly soft and yellowish as the biopolymer ratio
r
was increased regardless of the meat matrix, whereas pH and water activity values were not affected. CLSM images revealed that the meat protein network became disrupted and loose in the presence of pectin, which was attributed to a thermodynamic incompatibility effect. The results obtained from this study highlight that biopolymer complexes might be suitable fat mimetics, particularly for spreadable meat products.
Process-stable complexes composed of whey protein isolate (WPI) and sugar beet pectin have great potential as structuring agents or fat replacers in meat dispersions.</description><subject>Biopolymers</subject><subject>Compatibility</subject><subject>Confocal microscopy</subject><subject>Dispersions</subject><subject>Fermented food</subject><subject>Food</subject><subject>Incompatibility</subject><subject>Lasers</subject><subject>Meat</subject><subject>Meat products</subject><subject>Microscopy</subject><subject>Pectin</subject><subject>Rheometry</subject><subject>Sausages</subject><subject>Scanning microscopy</subject><subject>Water activity</subject><subject>Whey</subject><subject>Whey protein</subject><issn>2042-6496</issn><issn>2042-650X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNpd0UtLxDAQB_Agisq6F-9KwIsI1TzaZnOUxceCsB4UvdU0nbBZ2qYmKei3t-s-BHOZwPwYhv8gdErJNSVc3mhhHKGZEGoPHTOSsiTPyPv-9p_K_AiNQ1iS4XEpJ3JyiI6YTHNJuThGH7OmUzpiZ7BxrsIh-l7H3gN2LY4LwNoNINrS1jZ-r9gCVIQKvz3Pkg50tG2yIjV8QcC2xc3QxpUNHfhgXRtO0IFRdYDxpo7Q6_3dy_QxeZo_zKa3T4nmXMRE0FJBrpnKgeQScqkACBUaYCI5BZBEGQ6VynipskpWJRHUZCbjIqWUSc1H6HI9t_Pus4cQi8YGDXWtWnB9KBghImWpEPlAL_7Rpet9O2w3KJpNGCN8pa7WSnsXggdTdN42yn8XlBSr6IupuJ__Rn874PPNyL5soNrRbdADOFsDH_Su-3c7_gN3bYin</recordid><startdate>20180301</startdate><enddate>20180301</enddate><creator>Zeeb, Benjamin</creator><creator>Schöck, Vanessa</creator><creator>Schmid, Nicole</creator><creator>Majer, Lisa</creator><creator>Herrmann, Kurt</creator><creator>Hinrichs, Jörg</creator><creator>Weiss, Jochen</creator><general>Royal Society of Chemistry</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>7T7</scope><scope>7TO</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-3171-7082</orcidid></search><sort><creationdate>20180301</creationdate><title>Impact of food structure on the compatibility of heated WPI-pectin-complexes in meat dispersions</title><author>Zeeb, Benjamin ; Schöck, Vanessa ; Schmid, Nicole ; Majer, Lisa ; Herrmann, Kurt ; Hinrichs, Jörg ; Weiss, Jochen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c337t-71bae6c2a6e069e69aee017cee8931ee90af3eda53ba5d9db071f5f53741129c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Biopolymers</topic><topic>Compatibility</topic><topic>Confocal microscopy</topic><topic>Dispersions</topic><topic>Fermented food</topic><topic>Food</topic><topic>Incompatibility</topic><topic>Lasers</topic><topic>Meat</topic><topic>Meat products</topic><topic>Microscopy</topic><topic>Pectin</topic><topic>Rheometry</topic><topic>Sausages</topic><topic>Scanning microscopy</topic><topic>Water activity</topic><topic>Whey</topic><topic>Whey protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zeeb, Benjamin</creatorcontrib><creatorcontrib>Schöck, Vanessa</creatorcontrib><creatorcontrib>Schmid, Nicole</creatorcontrib><creatorcontrib>Majer, Lisa</creatorcontrib><creatorcontrib>Herrmann, Kurt</creatorcontrib><creatorcontrib>Hinrichs, Jörg</creatorcontrib><creatorcontrib>Weiss, Jochen</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Food & function</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zeeb, Benjamin</au><au>Schöck, Vanessa</au><au>Schmid, Nicole</au><au>Majer, Lisa</au><au>Herrmann, Kurt</au><au>Hinrichs, Jörg</au><au>Weiss, Jochen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Impact of food structure on the compatibility of heated WPI-pectin-complexes in meat dispersions</atitle><jtitle>Food & function</jtitle><addtitle>Food Funct</addtitle><date>2018-03-01</date><risdate>2018</risdate><volume>9</volume><issue>3</issue><spage>1647</spage><epage>1656</epage><pages>1647-1656</pages><issn>2042-6496</issn><eissn>2042-650X</eissn><abstract>Process-stable complexes composed of whey protein isolate (WPI) and sugar beet pectin have great potential as structuring agents or fat replacers in foods. The current study investigates the compatibility of heated WPI : pectin complexes in different meat matrices. Spreadable raw-fermented sausages and sliceable emulsion-type sausages were therefore manufactured containing biopolymer complexes with various WPI : pectin ratios
r
(2 : 1, 8 : 1). Macro- and microstructural properties of the meat dispersions were analyzed in terms of colour, texture, rheometry, sensory, and confocal laser scanning microscopy (CLSM) measurements. Textural and sensorial results demonstrated that the meat products became increasingly soft and yellowish as the biopolymer ratio
r
was increased regardless of the meat matrix, whereas pH and water activity values were not affected. CLSM images revealed that the meat protein network became disrupted and loose in the presence of pectin, which was attributed to a thermodynamic incompatibility effect. The results obtained from this study highlight that biopolymer complexes might be suitable fat mimetics, particularly for spreadable meat products.
Process-stable complexes composed of whey protein isolate (WPI) and sugar beet pectin have great potential as structuring agents or fat replacers in meat dispersions.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>29469137</pmid><doi>10.1039/c7fo01577a</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0003-3171-7082</orcidid></addata></record> |
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source | Royal Society Of Chemistry Journals 2008- |
subjects | Biopolymers Compatibility Confocal microscopy Dispersions Fermented food Food Incompatibility Lasers Meat Meat products Microscopy Pectin Rheometry Sausages Scanning microscopy Water activity Whey Whey protein |
title | Impact of food structure on the compatibility of heated WPI-pectin-complexes in meat dispersions |
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