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Ultrasonic modification of whey protein isolate: Implications for the structural and functional properties
The present study aimed to investigate the implications of ultrasonic treatment on the conformational and functional properties of whey protein isolate (WPI). SDS-PAGE showed that ultrasonication did not change the molecular weight of WPI. FTIR spectroscopy demonstrated that sonication caused second...
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Published in: | Food science & technology 2021-12, Vol.152, p.112272, Article 112272 |
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creator | Meng, Yueyue Liang, Zhiqiang Zhang, Chenyi Hao, Siqi Han, Hongyang Du, Peng Li, Aili Shao, Hong Li, Chun Liu, Libo |
description | The present study aimed to investigate the implications of ultrasonic treatment on the conformational and functional properties of whey protein isolate (WPI). SDS-PAGE showed that ultrasonication did not change the molecular weight of WPI. FTIR spectroscopy demonstrated that sonication caused secondary structure alterations in WPI, with a reduction in α-helix and β-sheet, and an enhancement in β-turn, and random coil content. An increase in surface hydrophobicity was observed after ultrasound treatment, suggesting that modification in tertiary structure of WPI were induced by sonication. The sizes of aggregates in WPI were found reduced after sonication by the analysis of particle size distribution and scanning electron microscopy (SEM). Additionally, the foaming, emulsifying and antioxidant attributes of WPI were enhanced after treated with ultrasonication. These results suggest that ultrasonication can be used as a useful technology to modify the functional characteristics of whey proteins.
•Effects of sonication on properties of WPI was assessed.•Sonication did not change the molar masses of WPI.•Sonication caused conformational changes in WPI at secondary and tertiary structure.•Sonication reduced sizes of aggregates in WPI.•Sonication improved the foaming, emulsifying and antioxidant properties of WPI. |
doi_str_mv | 10.1016/j.lwt.2021.112272 |
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•Effects of sonication on properties of WPI was assessed.•Sonication did not change the molar masses of WPI.•Sonication caused conformational changes in WPI at secondary and tertiary structure.•Sonication reduced sizes of aggregates in WPI.•Sonication improved the foaming, emulsifying and antioxidant properties of WPI.</description><identifier>ISSN: 0023-6438</identifier><identifier>EISSN: 1096-1127</identifier><identifier>DOI: 10.1016/j.lwt.2021.112272</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Antioxidant activity ; Emulsifying property ; Foaming property ; Ultrasound ; Whey protein isolate</subject><ispartof>Food science & technology, 2021-12, Vol.152, p.112272, Article 112272</ispartof><rights>2021 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c297t-fbbde94305c5ad8175b4feb613cb3f1d3e46af6a8f10c415e47965ac58c035c13</citedby><cites>FETCH-LOGICAL-c297t-fbbde94305c5ad8175b4feb613cb3f1d3e46af6a8f10c415e47965ac58c035c13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Meng, Yueyue</creatorcontrib><creatorcontrib>Liang, Zhiqiang</creatorcontrib><creatorcontrib>Zhang, Chenyi</creatorcontrib><creatorcontrib>Hao, Siqi</creatorcontrib><creatorcontrib>Han, Hongyang</creatorcontrib><creatorcontrib>Du, Peng</creatorcontrib><creatorcontrib>Li, Aili</creatorcontrib><creatorcontrib>Shao, Hong</creatorcontrib><creatorcontrib>Li, Chun</creatorcontrib><creatorcontrib>Liu, Libo</creatorcontrib><title>Ultrasonic modification of whey protein isolate: Implications for the structural and functional properties</title><title>Food science & technology</title><description>The present study aimed to investigate the implications of ultrasonic treatment on the conformational and functional properties of whey protein isolate (WPI). SDS-PAGE showed that ultrasonication did not change the molecular weight of WPI. FTIR spectroscopy demonstrated that sonication caused secondary structure alterations in WPI, with a reduction in α-helix and β-sheet, and an enhancement in β-turn, and random coil content. An increase in surface hydrophobicity was observed after ultrasound treatment, suggesting that modification in tertiary structure of WPI were induced by sonication. The sizes of aggregates in WPI were found reduced after sonication by the analysis of particle size distribution and scanning electron microscopy (SEM). Additionally, the foaming, emulsifying and antioxidant attributes of WPI were enhanced after treated with ultrasonication. These results suggest that ultrasonication can be used as a useful technology to modify the functional characteristics of whey proteins.
•Effects of sonication on properties of WPI was assessed.•Sonication did not change the molar masses of WPI.•Sonication caused conformational changes in WPI at secondary and tertiary structure.•Sonication reduced sizes of aggregates in WPI.•Sonication improved the foaming, emulsifying and antioxidant properties of WPI.</description><subject>Antioxidant activity</subject><subject>Emulsifying property</subject><subject>Foaming property</subject><subject>Ultrasound</subject><subject>Whey protein isolate</subject><issn>0023-6438</issn><issn>1096-1127</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp9kMtqwzAQRUVpoWnaD-hOP2BXDz_bVQl9BALdNGshj0dExrGMpDTk76uQrjub4cI9w3AIeeQs54xXT0M-HmMumOA550LU4oosOGurLKX6miwYEzKrCtnckrsQBpamEM2CDNsxeh3cZIHuXW-NBR2tm6gz9LjDE529i2gnaoMbdcRnut7P418pUOM8jTukIfoDxIPXI9VTT81hgnMhxcTP6KPFcE9ujB4DPvztJdm-v32vPrPN18d69brJQLR1zEzX9dgWkpVQ6r7hddkVBruKS-ik4b3EotKm0o3hDApeYlG3VamhbIDJErhcEn65C96F4NGo2du99ifFmTrLUoNKstRZlrrISszLhcH02I9FrwJYnAB76xGi6p39h_4FfV51ig</recordid><startdate>202112</startdate><enddate>202112</enddate><creator>Meng, Yueyue</creator><creator>Liang, Zhiqiang</creator><creator>Zhang, Chenyi</creator><creator>Hao, Siqi</creator><creator>Han, Hongyang</creator><creator>Du, Peng</creator><creator>Li, Aili</creator><creator>Shao, Hong</creator><creator>Li, Chun</creator><creator>Liu, Libo</creator><general>Elsevier Ltd</general><scope>6I.</scope><scope>AAFTH</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>202112</creationdate><title>Ultrasonic modification of whey protein isolate: Implications for the structural and functional properties</title><author>Meng, Yueyue ; Liang, Zhiqiang ; Zhang, Chenyi ; Hao, Siqi ; Han, Hongyang ; Du, Peng ; Li, Aili ; Shao, Hong ; Li, Chun ; Liu, Libo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c297t-fbbde94305c5ad8175b4feb613cb3f1d3e46af6a8f10c415e47965ac58c035c13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Antioxidant activity</topic><topic>Emulsifying property</topic><topic>Foaming property</topic><topic>Ultrasound</topic><topic>Whey protein isolate</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meng, Yueyue</creatorcontrib><creatorcontrib>Liang, Zhiqiang</creatorcontrib><creatorcontrib>Zhang, Chenyi</creatorcontrib><creatorcontrib>Hao, Siqi</creatorcontrib><creatorcontrib>Han, Hongyang</creatorcontrib><creatorcontrib>Du, Peng</creatorcontrib><creatorcontrib>Li, Aili</creatorcontrib><creatorcontrib>Shao, Hong</creatorcontrib><creatorcontrib>Li, Chun</creatorcontrib><creatorcontrib>Liu, Libo</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>CrossRef</collection><jtitle>Food science & technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meng, Yueyue</au><au>Liang, Zhiqiang</au><au>Zhang, Chenyi</au><au>Hao, Siqi</au><au>Han, Hongyang</au><au>Du, Peng</au><au>Li, Aili</au><au>Shao, Hong</au><au>Li, Chun</au><au>Liu, Libo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ultrasonic modification of whey protein isolate: Implications for the structural and functional properties</atitle><jtitle>Food science & technology</jtitle><date>2021-12</date><risdate>2021</risdate><volume>152</volume><spage>112272</spage><pages>112272-</pages><artnum>112272</artnum><issn>0023-6438</issn><eissn>1096-1127</eissn><abstract>The present study aimed to investigate the implications of ultrasonic treatment on the conformational and functional properties of whey protein isolate (WPI). SDS-PAGE showed that ultrasonication did not change the molecular weight of WPI. FTIR spectroscopy demonstrated that sonication caused secondary structure alterations in WPI, with a reduction in α-helix and β-sheet, and an enhancement in β-turn, and random coil content. An increase in surface hydrophobicity was observed after ultrasound treatment, suggesting that modification in tertiary structure of WPI were induced by sonication. The sizes of aggregates in WPI were found reduced after sonication by the analysis of particle size distribution and scanning electron microscopy (SEM). Additionally, the foaming, emulsifying and antioxidant attributes of WPI were enhanced after treated with ultrasonication. These results suggest that ultrasonication can be used as a useful technology to modify the functional characteristics of whey proteins.
•Effects of sonication on properties of WPI was assessed.•Sonication did not change the molar masses of WPI.•Sonication caused conformational changes in WPI at secondary and tertiary structure.•Sonication reduced sizes of aggregates in WPI.•Sonication improved the foaming, emulsifying and antioxidant properties of WPI.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.lwt.2021.112272</doi><oa>free_for_read</oa></addata></record> |
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subjects | Antioxidant activity Emulsifying property Foaming property Ultrasound Whey protein isolate |
title | Ultrasonic modification of whey protein isolate: Implications for the structural and functional properties |
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