Improved structure‐stability and packaging characters of crosslinked collagen fiber‐based film with casein, keratin and SPI
Background To improve the structure‐stability and packing characters of collagen fiber, we manufactured crosslinked collagen fiber (CColF)‐based edible films using transglutaminase (TGase). Then we made a comparison on structure‐stability and packing characteristics among the CColF‐based films loade...
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| Veröffentlicht in: | Journal of the science of food and agriculture 2019-08, Vol.99 (11), p.4942-4951 |
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| creator | Wu, Xiaomeng Luo, Yanghe Liu, Qi Jiang, Shujuan Mu, Guangqing |
| description | Background
To improve the structure‐stability and packing characters of collagen fiber, we manufactured crosslinked collagen fiber (CColF)‐based edible films using transglutaminase (TGase). Then we made a comparison on structure‐stability and packing characteristics among the CColF‐based films loaded with casein (CN), keratin (KRT) and soy protein isolate (SPI), respectively.
Results
Observed from scanning electron microscopy (SEM), the CColF loaded with CN, KRT and SPI showed some unique morphology of the additional proteins. The CColF–protein films performed better packing characteristics including barrier properties, mechanical properties and thermal‐stability properties, compared with CColF films. Importantly, with 500 g kg−1 CN (of CColF) addition, CColF‐based films possessed a greater thermal stability than the other films judged from differential scanning calorimetry (DSC). Meanwhile, the CColF loaded with 100 g kg−1 CN provided a higher value of tensile strength (TS) and the CColF loaded with 100 g kg−1 KRT showed a higher value in elongation‐at‐break (EAB) than the other films.
Conclusion
In conclusion, the collagen fiber‐based edible films with better structure‐stability and packing characteristics for food packaging was obtained which could be an advantage to promote the development of the application of collagen in packing products. © 2019 Society of Chemical Industry |
| doi_str_mv | 10.1002/jsfa.9726 |
| format | Article |
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To improve the structure‐stability and packing characters of collagen fiber, we manufactured crosslinked collagen fiber (CColF)‐based edible films using transglutaminase (TGase). Then we made a comparison on structure‐stability and packing characteristics among the CColF‐based films loaded with casein (CN), keratin (KRT) and soy protein isolate (SPI), respectively.
Results
Observed from scanning electron microscopy (SEM), the CColF loaded with CN, KRT and SPI showed some unique morphology of the additional proteins. The CColF–protein films performed better packing characteristics including barrier properties, mechanical properties and thermal‐stability properties, compared with CColF films. Importantly, with 500 g kg−1 CN (of CColF) addition, CColF‐based films possessed a greater thermal stability than the other films judged from differential scanning calorimetry (DSC). Meanwhile, the CColF loaded with 100 g kg−1 CN provided a higher value of tensile strength (TS) and the CColF loaded with 100 g kg−1 KRT showed a higher value in elongation‐at‐break (EAB) than the other films.
Conclusion
In conclusion, the collagen fiber‐based edible films with better structure‐stability and packing characteristics for food packaging was obtained which could be an advantage to promote the development of the application of collagen in packing products. © 2019 Society of Chemical Industry</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.9726</identifier><identifier>PMID: 30953342</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Calorimetry ; Calorimetry, Differential Scanning ; Casein ; Caseins - chemistry ; Caseins - metabolism ; Collagen ; Collagen - chemistry ; Cross-Linking Reagents - metabolism ; crosslinked collagen fiber ; Crosslinking ; Differential scanning calorimetry ; Drug Stability ; edible film ; Elongation ; Food packaging ; Food Packaging - instrumentation ; Food packaging industry ; Hot Temperature ; Keratin ; Keratins - chemistry ; Keratins - metabolism ; Mechanical Phenomena ; Mechanical properties ; Microscopy, Electron, Scanning ; Morphology ; Organic chemistry ; Packaging ; Packing ; packing characteristics ; Permeability ; Proteins ; Scanning electron microscopy ; Soybean Proteins - chemistry ; Soybean Proteins - metabolism ; Steam ; Tensile Strength ; Thermal stability ; transglutaminase ; Transglutaminases - metabolism ; X-Ray Diffraction</subject><ispartof>Journal of the science of food and agriculture, 2019-08, Vol.99 (11), p.4942-4951</ispartof><rights>2019 Society of Chemical Industry</rights><rights>2019 Society of Chemical Industry.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3536-333902cd4e3225adc533fea57442bab7f2581e07cd5fee26dd087c352fd6f8453</citedby><cites>FETCH-LOGICAL-c3536-333902cd4e3225adc533fea57442bab7f2581e07cd5fee26dd087c352fd6f8453</cites><orcidid>0000-0001-9356-753X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.9726$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.9726$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30953342$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wu, Xiaomeng</creatorcontrib><creatorcontrib>Luo, Yanghe</creatorcontrib><creatorcontrib>Liu, Qi</creatorcontrib><creatorcontrib>Jiang, Shujuan</creatorcontrib><creatorcontrib>Mu, Guangqing</creatorcontrib><title>Improved structure‐stability and packaging characters of crosslinked collagen fiber‐based film with casein, keratin and SPI</title><title>Journal of the science of food and agriculture</title><addtitle>J Sci Food Agric</addtitle><description>Background
To improve the structure‐stability and packing characters of collagen fiber, we manufactured crosslinked collagen fiber (CColF)‐based edible films using transglutaminase (TGase). Then we made a comparison on structure‐stability and packing characteristics among the CColF‐based films loaded with casein (CN), keratin (KRT) and soy protein isolate (SPI), respectively.
Results
Observed from scanning electron microscopy (SEM), the CColF loaded with CN, KRT and SPI showed some unique morphology of the additional proteins. The CColF–protein films performed better packing characteristics including barrier properties, mechanical properties and thermal‐stability properties, compared with CColF films. Importantly, with 500 g kg−1 CN (of CColF) addition, CColF‐based films possessed a greater thermal stability than the other films judged from differential scanning calorimetry (DSC). Meanwhile, the CColF loaded with 100 g kg−1 CN provided a higher value of tensile strength (TS) and the CColF loaded with 100 g kg−1 KRT showed a higher value in elongation‐at‐break (EAB) than the other films.
Conclusion
In conclusion, the collagen fiber‐based edible films with better structure‐stability and packing characteristics for food packaging was obtained which could be an advantage to promote the development of the application of collagen in packing products. © 2019 Society of Chemical Industry</description><subject>Calorimetry</subject><subject>Calorimetry, Differential Scanning</subject><subject>Casein</subject><subject>Caseins - chemistry</subject><subject>Caseins - metabolism</subject><subject>Collagen</subject><subject>Collagen - chemistry</subject><subject>Cross-Linking Reagents - metabolism</subject><subject>crosslinked collagen fiber</subject><subject>Crosslinking</subject><subject>Differential scanning calorimetry</subject><subject>Drug Stability</subject><subject>edible film</subject><subject>Elongation</subject><subject>Food packaging</subject><subject>Food Packaging - instrumentation</subject><subject>Food packaging industry</subject><subject>Hot Temperature</subject><subject>Keratin</subject><subject>Keratins - chemistry</subject><subject>Keratins - metabolism</subject><subject>Mechanical Phenomena</subject><subject>Mechanical properties</subject><subject>Microscopy, Electron, Scanning</subject><subject>Morphology</subject><subject>Organic chemistry</subject><subject>Packaging</subject><subject>Packing</subject><subject>packing characteristics</subject><subject>Permeability</subject><subject>Proteins</subject><subject>Scanning electron microscopy</subject><subject>Soybean Proteins - chemistry</subject><subject>Soybean Proteins - metabolism</subject><subject>Steam</subject><subject>Tensile Strength</subject><subject>Thermal stability</subject><subject>transglutaminase</subject><subject>Transglutaminases - metabolism</subject><subject>X-Ray Diffraction</subject><issn>0022-5142</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kc1O3DAURi0EgillwQtUlthQqYEbO3aSJUKlTIVUJMo6cuzrwTP5mdoJaFbtI_QZ-yR4ZoBFJVaW7XOPPvsj5DiFsxSAnc-DVWdlzuQOmaRQ5glACrtkEu9YItKMHZAPIcwBoCyl3CcHHErBecYm5Pe0Xfr-EQ0Ngx_1MHr89-dvGFTtGjesqOoMXSq9UDPXzah-UF7pAX2gvaXa9yE0rlvEad03jZphR62r0UdFrUI8tq5p6ZMbHqiOe9d9oQv0anDdRnx3O_1I9qxqAh69rIfk_urrz8vr5ObHt-nlxU2iueAy4ZyXwLTJkDMmlNExvkUl8ixjtapzy0SRIuTaCIvIpDFQ5HGUWSNtkQl-SE633vjaXyOGoWpd0BhDd9iPoWIMMlnkUGQRPfkPnfej72K6SAkpQJawFn7eUptf8GirpXet8qsqhWrdSrVupVq3EtlPL8axbtG8ka81ROB8Czy5Blfvm6rvd1cXG-UzXpaaEg</recordid><startdate>20190830</startdate><enddate>20190830</enddate><creator>Wu, Xiaomeng</creator><creator>Luo, Yanghe</creator><creator>Liu, Qi</creator><creator>Jiang, Shujuan</creator><creator>Mu, Guangqing</creator><general>John Wiley & Sons, Ltd</general><general>John Wiley and Sons, Limited</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QL</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>SOI</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-9356-753X</orcidid></search><sort><creationdate>20190830</creationdate><title>Improved structure‐stability and packaging characters of crosslinked collagen fiber‐based film with casein, keratin and SPI</title><author>Wu, Xiaomeng ; Luo, Yanghe ; Liu, Qi ; Jiang, Shujuan ; Mu, Guangqing</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3536-333902cd4e3225adc533fea57442bab7f2581e07cd5fee26dd087c352fd6f8453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Calorimetry</topic><topic>Calorimetry, Differential Scanning</topic><topic>Casein</topic><topic>Caseins - chemistry</topic><topic>Caseins - metabolism</topic><topic>Collagen</topic><topic>Collagen - chemistry</topic><topic>Cross-Linking Reagents - metabolism</topic><topic>crosslinked collagen fiber</topic><topic>Crosslinking</topic><topic>Differential scanning calorimetry</topic><topic>Drug Stability</topic><topic>edible film</topic><topic>Elongation</topic><topic>Food packaging</topic><topic>Food Packaging - instrumentation</topic><topic>Food packaging industry</topic><topic>Hot Temperature</topic><topic>Keratin</topic><topic>Keratins - chemistry</topic><topic>Keratins - metabolism</topic><topic>Mechanical Phenomena</topic><topic>Mechanical properties</topic><topic>Microscopy, Electron, Scanning</topic><topic>Morphology</topic><topic>Organic chemistry</topic><topic>Packaging</topic><topic>Packing</topic><topic>packing characteristics</topic><topic>Permeability</topic><topic>Proteins</topic><topic>Scanning electron microscopy</topic><topic>Soybean Proteins - chemistry</topic><topic>Soybean Proteins - metabolism</topic><topic>Steam</topic><topic>Tensile Strength</topic><topic>Thermal stability</topic><topic>transglutaminase</topic><topic>Transglutaminases - metabolism</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wu, Xiaomeng</creatorcontrib><creatorcontrib>Luo, Yanghe</creatorcontrib><creatorcontrib>Liu, Qi</creatorcontrib><creatorcontrib>Jiang, Shujuan</creatorcontrib><creatorcontrib>Mu, Guangqing</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</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>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the science of food and agriculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, Xiaomeng</au><au>Luo, Yanghe</au><au>Liu, Qi</au><au>Jiang, Shujuan</au><au>Mu, Guangqing</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Improved structure‐stability and packaging characters of crosslinked collagen fiber‐based film with casein, keratin and SPI</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J Sci Food Agric</addtitle><date>2019-08-30</date><risdate>2019</risdate><volume>99</volume><issue>11</issue><spage>4942</spage><epage>4951</epage><pages>4942-4951</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><abstract>Background
To improve the structure‐stability and packing characters of collagen fiber, we manufactured crosslinked collagen fiber (CColF)‐based edible films using transglutaminase (TGase). Then we made a comparison on structure‐stability and packing characteristics among the CColF‐based films loaded with casein (CN), keratin (KRT) and soy protein isolate (SPI), respectively.
Results
Observed from scanning electron microscopy (SEM), the CColF loaded with CN, KRT and SPI showed some unique morphology of the additional proteins. The CColF–protein films performed better packing characteristics including barrier properties, mechanical properties and thermal‐stability properties, compared with CColF films. Importantly, with 500 g kg−1 CN (of CColF) addition, CColF‐based films possessed a greater thermal stability than the other films judged from differential scanning calorimetry (DSC). Meanwhile, the CColF loaded with 100 g kg−1 CN provided a higher value of tensile strength (TS) and the CColF loaded with 100 g kg−1 KRT showed a higher value in elongation‐at‐break (EAB) than the other films.
Conclusion
In conclusion, the collagen fiber‐based edible films with better structure‐stability and packing characteristics for food packaging was obtained which could be an advantage to promote the development of the application of collagen in packing products. © 2019 Society of Chemical Industry</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>30953342</pmid><doi>10.1002/jsfa.9726</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-9356-753X</orcidid></addata></record> |
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| subjects | Calorimetry Calorimetry, Differential Scanning Casein Caseins - chemistry Caseins - metabolism Collagen Collagen - chemistry Cross-Linking Reagents - metabolism crosslinked collagen fiber Crosslinking Differential scanning calorimetry Drug Stability edible film Elongation Food packaging Food Packaging - instrumentation Food packaging industry Hot Temperature Keratin Keratins - chemistry Keratins - metabolism Mechanical Phenomena Mechanical properties Microscopy, Electron, Scanning Morphology Organic chemistry Packaging Packing packing characteristics Permeability Proteins Scanning electron microscopy Soybean Proteins - chemistry Soybean Proteins - metabolism Steam Tensile Strength Thermal stability transglutaminase Transglutaminases - metabolism X-Ray Diffraction |
| title | Improved structure‐stability and packaging characters of crosslinked collagen fiber‐based film with casein, keratin and SPI |
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