Consequences of superfine grinding treatment on structure, physicochemical and rheological properties of transglutaminase-crosslinked whey protein isolate
•Superfine grinding promoted formation of transglutaminase-treated whey protein.•Emulsifying ability of all the samples increased after superfine grinding treatment.•Transglutaminase-treated micronized whey protein showed high apparent viscosity. Impacts of superfine grinding treatment (0, 2, 4, 6,...
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| Veröffentlicht in: | Food chemistry 2020-03, Vol.309, p.125757-125757, Article 125757 |
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| creator | Wang, Chunyan Li, Tianqi Ma, Ling Li, Tong Yu, Haiying Hou, Juncai Jiang, Zhanmei |
| description | •Superfine grinding promoted formation of transglutaminase-treated whey protein.•Emulsifying ability of all the samples increased after superfine grinding treatment.•Transglutaminase-treated micronized whey protein showed high apparent viscosity.
Impacts of superfine grinding treatment (0, 2, 4, 6, 8 or 10 h) on structure, physicochemical and rheological properties of transglutaminase (TGase)-crosslinked whey protein isolate (WPI) were investigated. Size exclusion chromatography showed that high molecular weight polymers were formed in TGase-treated sWPI (WPI treated with superfine grinding), whereas its consumption of free amino groups reached the maximum at grinding 8 h and 10 h. With the milling time extended from 0 to 10 h, particle size of the TGase-crosslinked sWPI gradually increased. Emission spectrum shifted from 338.6 nm to 340.6 nm after sWPI treated with TGase. Meanwhile, TGase-crosslinked sWPI had higher apparent viscosity, emulsifying properties than TGase-crosslinked WPI, but the solubility of TGase-crosslinked sWPI was lower than sWPI. Superfine grinding treatment remarkably increased β-sheet and random compositions in TGase-crosslinked sWPI. These findings indicated that superfine grinding treatment could enhance the TGase cross-linking degree, and improve rheological properties in TGase-crosslinked WPI. |
| doi_str_mv | 10.1016/j.foodchem.2019.125757 |
| format | Article |
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Impacts of superfine grinding treatment (0, 2, 4, 6, 8 or 10 h) on structure, physicochemical and rheological properties of transglutaminase (TGase)-crosslinked whey protein isolate (WPI) were investigated. Size exclusion chromatography showed that high molecular weight polymers were formed in TGase-treated sWPI (WPI treated with superfine grinding), whereas its consumption of free amino groups reached the maximum at grinding 8 h and 10 h. With the milling time extended from 0 to 10 h, particle size of the TGase-crosslinked sWPI gradually increased. Emission spectrum shifted from 338.6 nm to 340.6 nm after sWPI treated with TGase. Meanwhile, TGase-crosslinked sWPI had higher apparent viscosity, emulsifying properties than TGase-crosslinked WPI, but the solubility of TGase-crosslinked sWPI was lower than sWPI. Superfine grinding treatment remarkably increased β-sheet and random compositions in TGase-crosslinked sWPI. These findings indicated that superfine grinding treatment could enhance the TGase cross-linking degree, and improve rheological properties in TGase-crosslinked WPI.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2019.125757</identifier><identifier>PMID: 31699562</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Emulsions - chemistry ; Molecular Weight ; Particle Size ; Physicochemical properties ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Rheological property ; Rheology ; Solubility ; Spectroscopy, Fourier Transform Infrared ; Superfine grinding ; Transglutaminase ; Transglutaminases - metabolism ; Viscosity ; Whey protein isolate ; Whey Proteins - chemistry ; Whey Proteins - metabolism</subject><ispartof>Food chemistry, 2020-03, Vol.309, p.125757-125757, Article 125757</ispartof><rights>2019 Elsevier Ltd</rights><rights>Copyright © 2019 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-e0cd8e2a0f8cda615bbd2b44d066189ce0af4aee5a836a659240d859d5b733823</citedby><cites>FETCH-LOGICAL-c368t-e0cd8e2a0f8cda615bbd2b44d066189ce0af4aee5a836a659240d859d5b733823</cites><orcidid>0000-0002-7296-658X ; 0000-0003-2943-3398</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.foodchem.2019.125757$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31699562$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Chunyan</creatorcontrib><creatorcontrib>Li, Tianqi</creatorcontrib><creatorcontrib>Ma, Ling</creatorcontrib><creatorcontrib>Li, Tong</creatorcontrib><creatorcontrib>Yu, Haiying</creatorcontrib><creatorcontrib>Hou, Juncai</creatorcontrib><creatorcontrib>Jiang, Zhanmei</creatorcontrib><title>Consequences of superfine grinding treatment on structure, physicochemical and rheological properties of transglutaminase-crosslinked whey protein isolate</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>•Superfine grinding promoted formation of transglutaminase-treated whey protein.•Emulsifying ability of all the samples increased after superfine grinding treatment.•Transglutaminase-treated micronized whey protein showed high apparent viscosity.
Impacts of superfine grinding treatment (0, 2, 4, 6, 8 or 10 h) on structure, physicochemical and rheological properties of transglutaminase (TGase)-crosslinked whey protein isolate (WPI) were investigated. Size exclusion chromatography showed that high molecular weight polymers were formed in TGase-treated sWPI (WPI treated with superfine grinding), whereas its consumption of free amino groups reached the maximum at grinding 8 h and 10 h. With the milling time extended from 0 to 10 h, particle size of the TGase-crosslinked sWPI gradually increased. Emission spectrum shifted from 338.6 nm to 340.6 nm after sWPI treated with TGase. Meanwhile, TGase-crosslinked sWPI had higher apparent viscosity, emulsifying properties than TGase-crosslinked WPI, but the solubility of TGase-crosslinked sWPI was lower than sWPI. Superfine grinding treatment remarkably increased β-sheet and random compositions in TGase-crosslinked sWPI. These findings indicated that superfine grinding treatment could enhance the TGase cross-linking degree, and improve rheological properties in TGase-crosslinked WPI.</description><subject>Emulsions - chemistry</subject><subject>Molecular Weight</subject><subject>Particle Size</subject><subject>Physicochemical properties</subject><subject>Protein Conformation, alpha-Helical</subject><subject>Protein Conformation, beta-Strand</subject><subject>Rheological property</subject><subject>Rheology</subject><subject>Solubility</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Superfine grinding</subject><subject>Transglutaminase</subject><subject>Transglutaminases - metabolism</subject><subject>Viscosity</subject><subject>Whey protein isolate</subject><subject>Whey Proteins - chemistry</subject><subject>Whey Proteins - metabolism</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAURi1ERaeFV6i8ZEEG_8SOswONKFSqxKasLce-mfGQ2IPtgOZVeNomTcuWlWXp3O-79kHohpItJVR-PG77GJ09wLhlhLZbykQjmldoQ1XDq4Y07DXaEE5UpWgtL9FVzkdCyMyqN-iSU9m2QrIN-ruLIcOvCYKFjGOP83SC1PsAeJ98cD7scUlgygih4BhwLmmyZUrwAZ8O5-xtXJbw1gzYBIfTAeIQ90_3U4pzVvFrcEkm5P0wFTP6YDJUNsWcBx9-gsN_DnBe-AI-YJ_jYAq8RRe9GTK8ez6v0Y_bLw-7b9X99693u8_3leVSlQqIdQqYIb2yzkgqus6xrq4dkZKq1gIxfW0AhFFcGilaVhOnROtE13CuGL9G79fcuX_-iFz06LOFYTAB4pQ145RzIYlcULmiT7sn6PUp-dGks6ZEL170Ub940YsXvXqZB2-eO6ZuBPdv7EXEDHxaAZhf-ttD0tn6RYrzCWzRLvr_dTwCf3-n-g</recordid><startdate>20200330</startdate><enddate>20200330</enddate><creator>Wang, Chunyan</creator><creator>Li, Tianqi</creator><creator>Ma, Ling</creator><creator>Li, Tong</creator><creator>Yu, Haiying</creator><creator>Hou, Juncai</creator><creator>Jiang, Zhanmei</creator><general>Elsevier Ltd</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>7X8</scope><orcidid>https://orcid.org/0000-0002-7296-658X</orcidid><orcidid>https://orcid.org/0000-0003-2943-3398</orcidid></search><sort><creationdate>20200330</creationdate><title>Consequences of superfine grinding treatment on structure, physicochemical and rheological properties of transglutaminase-crosslinked whey protein isolate</title><author>Wang, Chunyan ; Li, Tianqi ; Ma, Ling ; Li, Tong ; Yu, Haiying ; Hou, Juncai ; Jiang, Zhanmei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-e0cd8e2a0f8cda615bbd2b44d066189ce0af4aee5a836a659240d859d5b733823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Emulsions - chemistry</topic><topic>Molecular Weight</topic><topic>Particle Size</topic><topic>Physicochemical properties</topic><topic>Protein Conformation, alpha-Helical</topic><topic>Protein Conformation, beta-Strand</topic><topic>Rheological property</topic><topic>Rheology</topic><topic>Solubility</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>Superfine grinding</topic><topic>Transglutaminase</topic><topic>Transglutaminases - metabolism</topic><topic>Viscosity</topic><topic>Whey protein isolate</topic><topic>Whey Proteins - chemistry</topic><topic>Whey Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Chunyan</creatorcontrib><creatorcontrib>Li, Tianqi</creatorcontrib><creatorcontrib>Ma, Ling</creatorcontrib><creatorcontrib>Li, Tong</creatorcontrib><creatorcontrib>Yu, Haiying</creatorcontrib><creatorcontrib>Hou, Juncai</creatorcontrib><creatorcontrib>Jiang, Zhanmei</creatorcontrib><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><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Chunyan</au><au>Li, Tianqi</au><au>Ma, Ling</au><au>Li, Tong</au><au>Yu, Haiying</au><au>Hou, Juncai</au><au>Jiang, Zhanmei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Consequences of superfine grinding treatment on structure, physicochemical and rheological properties of transglutaminase-crosslinked whey protein isolate</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2020-03-30</date><risdate>2020</risdate><volume>309</volume><spage>125757</spage><epage>125757</epage><pages>125757-125757</pages><artnum>125757</artnum><issn>0308-8146</issn><eissn>1873-7072</eissn><abstract>•Superfine grinding promoted formation of transglutaminase-treated whey protein.•Emulsifying ability of all the samples increased after superfine grinding treatment.•Transglutaminase-treated micronized whey protein showed high apparent viscosity.
Impacts of superfine grinding treatment (0, 2, 4, 6, 8 or 10 h) on structure, physicochemical and rheological properties of transglutaminase (TGase)-crosslinked whey protein isolate (WPI) were investigated. Size exclusion chromatography showed that high molecular weight polymers were formed in TGase-treated sWPI (WPI treated with superfine grinding), whereas its consumption of free amino groups reached the maximum at grinding 8 h and 10 h. With the milling time extended from 0 to 10 h, particle size of the TGase-crosslinked sWPI gradually increased. Emission spectrum shifted from 338.6 nm to 340.6 nm after sWPI treated with TGase. Meanwhile, TGase-crosslinked sWPI had higher apparent viscosity, emulsifying properties than TGase-crosslinked WPI, but the solubility of TGase-crosslinked sWPI was lower than sWPI. Superfine grinding treatment remarkably increased β-sheet and random compositions in TGase-crosslinked sWPI. These findings indicated that superfine grinding treatment could enhance the TGase cross-linking degree, and improve rheological properties in TGase-crosslinked WPI.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>31699562</pmid><doi>10.1016/j.foodchem.2019.125757</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-7296-658X</orcidid><orcidid>https://orcid.org/0000-0003-2943-3398</orcidid></addata></record> |
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| subjects | Emulsions - chemistry Molecular Weight Particle Size Physicochemical properties Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Rheological property Rheology Solubility Spectroscopy, Fourier Transform Infrared Superfine grinding Transglutaminase Transglutaminases - metabolism Viscosity Whey protein isolate Whey Proteins - chemistry Whey Proteins - metabolism |
| title | Consequences of superfine grinding treatment on structure, physicochemical and rheological properties of transglutaminase-crosslinked whey protein isolate |
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