Dispersible and Thermal Stable Nanofibrils Derived from Glycated Whey Protein
Formation of nanofibrils by heating proteins at pH 2.0 has been studied extensively because of the potential as novel biomaterials. However, nanofibrils of whey proteins have poor dispersibility and heat stability, limiting their application in fluidic and transparent products. We report, for the fi...
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| Veröffentlicht in: | Biomacromolecules 2013-07, Vol.14 (7), p.2146-2153 |
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| creator | Liu, Gang Zhong, Qixin |
| description | Formation of nanofibrils by heating proteins at pH 2.0 has been studied extensively because of the potential as novel biomaterials. However, nanofibrils of whey proteins have poor dispersibility and heat stability, limiting their application in fluidic and transparent products. We report, for the first time, the formation of nanofibrils from whey protein isolate (WPI) glycated with lactose (WPI-g-L) that were highly dispersible and remained transparent after heating at pH 3.0–7.0 and 0–150 mM NaCl. The WPI-g-L followed similar nanofibril formation mechanism as WPI based on reducing protein electrophoresis, analytical ultracentrifugation, and circular dichroism spectroscopy. The rate of nanofibril formation from WPI-g-L was similar to that of WPI, but the yield was lower based on thioflavin-T fluorescence spectroscopy. The presence of the glycated lactose on nanofibril surface provided steric hindrance enabling the dispersibility and thermal stability and supplying functions such as viscosity in various fluidic, transparent consumer products. |
| doi_str_mv | 10.1021/bm400521b |
| format | Article |
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However, nanofibrils of whey proteins have poor dispersibility and heat stability, limiting their application in fluidic and transparent products. We report, for the first time, the formation of nanofibrils from whey protein isolate (WPI) glycated with lactose (WPI-g-L) that were highly dispersible and remained transparent after heating at pH 3.0–7.0 and 0–150 mM NaCl. The WPI-g-L followed similar nanofibril formation mechanism as WPI based on reducing protein electrophoresis, analytical ultracentrifugation, and circular dichroism spectroscopy. The rate of nanofibril formation from WPI-g-L was similar to that of WPI, but the yield was lower based on thioflavin-T fluorescence spectroscopy. The presence of the glycated lactose on nanofibril surface provided steric hindrance enabling the dispersibility and thermal stability and supplying functions such as viscosity in various fluidic, transparent consumer products.</description><identifier>ISSN: 1525-7797</identifier><identifier>EISSN: 1526-4602</identifier><identifier>DOI: 10.1021/bm400521b</identifier><identifier>PMID: 23750817</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Applied sciences ; Biological and medical sciences ; Exact sciences and technology ; Fundamental and applied biological sciences. Psychology ; Glycosylation ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Lactose - chemistry ; Microscopy, Atomic Force ; Microscopy, Electron, Transmission ; Milk Proteins - chemistry ; Miscellaneous ; Nanofibers - chemistry ; Natural polymers ; Physicochemistry of polymers ; Proteins ; Spectrometry, Fluorescence ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Viscosity ; Whey Proteins</subject><ispartof>Biomacromolecules, 2013-07, Vol.14 (7), p.2146-2153</ispartof><rights>Copyright © 2013 American Chemical Society</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a378t-ed9ce7e8bfaeb7928f59b9c64e622c14dae60ba8e93c05296af51c5c28e492233</citedby><cites>FETCH-LOGICAL-a378t-ed9ce7e8bfaeb7928f59b9c64e622c14dae60ba8e93c05296af51c5c28e492233</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bm400521b$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bm400521b$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=27584484$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23750817$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Gang</creatorcontrib><creatorcontrib>Zhong, Qixin</creatorcontrib><title>Dispersible and Thermal Stable Nanofibrils Derived from Glycated Whey Protein</title><title>Biomacromolecules</title><addtitle>Biomacromolecules</addtitle><description>Formation of nanofibrils by heating proteins at pH 2.0 has been studied extensively because of the potential as novel biomaterials. However, nanofibrils of whey proteins have poor dispersibility and heat stability, limiting their application in fluidic and transparent products. We report, for the first time, the formation of nanofibrils from whey protein isolate (WPI) glycated with lactose (WPI-g-L) that were highly dispersible and remained transparent after heating at pH 3.0–7.0 and 0–150 mM NaCl. The WPI-g-L followed similar nanofibril formation mechanism as WPI based on reducing protein electrophoresis, analytical ultracentrifugation, and circular dichroism spectroscopy. The rate of nanofibril formation from WPI-g-L was similar to that of WPI, but the yield was lower based on thioflavin-T fluorescence spectroscopy. The presence of the glycated lactose on nanofibril surface provided steric hindrance enabling the dispersibility and thermal stability and supplying functions such as viscosity in various fluidic, transparent consumer products.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Applied sciences</subject><subject>Biological and medical sciences</subject><subject>Exact sciences and technology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycosylation</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Lactose - chemistry</subject><subject>Microscopy, Atomic Force</subject><subject>Microscopy, Electron, Transmission</subject><subject>Milk Proteins - chemistry</subject><subject>Miscellaneous</subject><subject>Nanofibers - chemistry</subject><subject>Natural polymers</subject><subject>Physicochemistry of polymers</subject><subject>Proteins</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Viscosity</subject><subject>Whey Proteins</subject><issn>1525-7797</issn><issn>1526-4602</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0EtLxDAQB_Agio_Vg19AehH0UM2zaY6y6ir4Alc8lkk6xUgfa9IV9tvb1VUvHjxlMvyYYf6E7DN6wihnp7aRlCrO7BrZZopnqcwoX_-sVaq10VtkJ8ZXSqkRUm2SLS60ojnT2-T23McZhuhtjQm0ZTJ9wdBAnTz2sGzdQdtV3gZfx-Qcg3_HMqlC1ySTeuGgH37PL7hIHkLXo293yUYFdcS91TsiT5cX0_FVenM_uR6f3aQgdN6nWBqHGnNbAVpteF4pY43LJGacOyZLwIxayNEIN9xlMqgUc8rxHKXhXIgROfqaOwvd2xxjXzQ-OqxraLGbx2I4XAqjtPoHFcZQlRnNBnr8RV3oYgxYFbPgGwiLgtFiGXTxE_RgD1Zj57bB8kd-JzuAwxWA6KCuArTOx1-nVS5lLn8duFi8dvPQDsH9sfADdOGQcg</recordid><startdate>20130708</startdate><enddate>20130708</enddate><creator>Liu, Gang</creator><creator>Zhong, Qixin</creator><general>American Chemical Society</general><scope>IQODW</scope><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>7X8</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20130708</creationdate><title>Dispersible and Thermal Stable Nanofibrils Derived from Glycated Whey Protein</title><author>Liu, Gang ; Zhong, Qixin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a378t-ed9ce7e8bfaeb7928f59b9c64e622c14dae60ba8e93c05296af51c5c28e492233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Applied sciences</topic><topic>Biological and medical sciences</topic><topic>Exact sciences and technology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycosylation</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Lactose - chemistry</topic><topic>Microscopy, Atomic Force</topic><topic>Microscopy, Electron, Transmission</topic><topic>Milk Proteins - chemistry</topic><topic>Miscellaneous</topic><topic>Nanofibers - chemistry</topic><topic>Natural polymers</topic><topic>Physicochemistry of polymers</topic><topic>Proteins</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Viscosity</topic><topic>Whey Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Gang</creatorcontrib><creatorcontrib>Zhong, Qixin</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biomacromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Gang</au><au>Zhong, Qixin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dispersible and Thermal Stable Nanofibrils Derived from Glycated Whey Protein</atitle><jtitle>Biomacromolecules</jtitle><addtitle>Biomacromolecules</addtitle><date>2013-07-08</date><risdate>2013</risdate><volume>14</volume><issue>7</issue><spage>2146</spage><epage>2153</epage><pages>2146-2153</pages><issn>1525-7797</issn><eissn>1526-4602</eissn><abstract>Formation of nanofibrils by heating proteins at pH 2.0 has been studied extensively because of the potential as novel biomaterials. However, nanofibrils of whey proteins have poor dispersibility and heat stability, limiting their application in fluidic and transparent products. We report, for the first time, the formation of nanofibrils from whey protein isolate (WPI) glycated with lactose (WPI-g-L) that were highly dispersible and remained transparent after heating at pH 3.0–7.0 and 0–150 mM NaCl. The WPI-g-L followed similar nanofibril formation mechanism as WPI based on reducing protein electrophoresis, analytical ultracentrifugation, and circular dichroism spectroscopy. The rate of nanofibril formation from WPI-g-L was similar to that of WPI, but the yield was lower based on thioflavin-T fluorescence spectroscopy. The presence of the glycated lactose on nanofibril surface provided steric hindrance enabling the dispersibility and thermal stability and supplying functions such as viscosity in various fluidic, transparent consumer products.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>23750817</pmid><doi>10.1021/bm400521b</doi><tpages>8</tpages></addata></record> |
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| subjects | Analytical, structural and metabolic biochemistry Applied sciences Biological and medical sciences Exact sciences and technology Fundamental and applied biological sciences. Psychology Glycosylation Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Lactose - chemistry Microscopy, Atomic Force Microscopy, Electron, Transmission Milk Proteins - chemistry Miscellaneous Nanofibers - chemistry Natural polymers Physicochemistry of polymers Proteins Spectrometry, Fluorescence Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Viscosity Whey Proteins |
| title | Dispersible and Thermal Stable Nanofibrils Derived from Glycated Whey Protein |
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