Effects of dual-frequency ultrasound with different energy irradiation modes on the structural and emulsifying properties of soy protein isolate
[Display omitted] •Effects of ultrasonic pretreatments with different energy irradiation modes were compared.•ESI of SPI treated by EGU was higher than those of EDU and SU.•The influence of EGU on the structure of SPI was more significant than those of EDU and SU. The effects of dual-frequency ultra...
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| Veröffentlicht in: | Food and bioproducts processing 2020-09, Vol.123, p.419-426 |
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| creator | Huang, Liurong Zhang, Wenxue Ding, Xiaona Wu, Zhengfen Li, Yunliang |
| description | [Display omitted]
•Effects of ultrasonic pretreatments with different energy irradiation modes were compared.•ESI of SPI treated by EGU was higher than those of EDU and SU.•The influence of EGU on the structure of SPI was more significant than those of EDU and SU.
The effects of dual-frequency ultrasound pretreatments with different energy irradiation modes, including energy-gathered ultrasound (EGU), energy-divergent ultrasound (EDU) and slit ultrasound (SU) on the solubility and emulsifying properties of soy protein isolate (SPI) were investigated. The surface hydrophobicity, intrinsic fluorescence spectra, and circular dichroism spectra of SPI were determined. Results revealed that all ultrasonic pretreatments increased the solubility of SPI significantly (P ≤ 0.05). Ultrasonic pretreatments with EDU and SU could not improve the emulsifying activity (P > 0.05). The emulsion stability index of SPI treated by EGU was higher than those of EDU and SU with the same ultrasonic time and power density. Changes in surface hydrophobicity and intrinsic fluorescence showed the unfolding of protein and exposure of hydrophobic groups as a result of action of ultrasound. The CD spectra of SPI pretreated by optimal EGU, EDU and SU showed that dual-frequency ultrasound induced the decrease of β-sheet contents and increase of α-helix and random coil contents significantly (P ≤ 0.05). In conclusion, the influence of EGU on the structural and emulsifying properties of SPI was more significant than those of EDU and SU. |
| doi_str_mv | 10.1016/j.fbp.2020.07.021 |
| format | Article |
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•Effects of ultrasonic pretreatments with different energy irradiation modes were compared.•ESI of SPI treated by EGU was higher than those of EDU and SU.•The influence of EGU on the structure of SPI was more significant than those of EDU and SU.
The effects of dual-frequency ultrasound pretreatments with different energy irradiation modes, including energy-gathered ultrasound (EGU), energy-divergent ultrasound (EDU) and slit ultrasound (SU) on the solubility and emulsifying properties of soy protein isolate (SPI) were investigated. The surface hydrophobicity, intrinsic fluorescence spectra, and circular dichroism spectra of SPI were determined. Results revealed that all ultrasonic pretreatments increased the solubility of SPI significantly (P ≤ 0.05). Ultrasonic pretreatments with EDU and SU could not improve the emulsifying activity (P > 0.05). The emulsion stability index of SPI treated by EGU was higher than those of EDU and SU with the same ultrasonic time and power density. Changes in surface hydrophobicity and intrinsic fluorescence showed the unfolding of protein and exposure of hydrophobic groups as a result of action of ultrasound. The CD spectra of SPI pretreated by optimal EGU, EDU and SU showed that dual-frequency ultrasound induced the decrease of β-sheet contents and increase of α-helix and random coil contents significantly (P ≤ 0.05). In conclusion, the influence of EGU on the structural and emulsifying properties of SPI was more significant than those of EDU and SU.</description><identifier>ISSN: 0960-3085</identifier><identifier>EISSN: 1744-3571</identifier><identifier>DOI: 10.1016/j.fbp.2020.07.021</identifier><language>eng</language><publisher>Rugby: Elsevier B.V</publisher><subject>Circular dichroism ; Coils ; Dichroism ; Emulsifying properties ; Emulsions ; Energy ; Energy irradiation mode ; Fluorescence ; Hydrophobic surfaces ; Hydrophobicity ; Irradiation ; Mechanical properties ; Properties ; Properties (attributes) ; Protein folding ; Proteins ; Random coil ; Solubility ; Soy protein isolate ; Spectra ; Stability ; Structure ; Ultrasonic imaging ; Ultrasound</subject><ispartof>Food and bioproducts processing, 2020-09, Vol.123, p.419-426</ispartof><rights>2020 Institution of Chemical Engineers</rights><rights>Copyright Elsevier Science Ltd. Sep 2020</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c325t-d78e4708655e2dcd64d139dd54551bd4040e412284a43c898ead706580e192613</citedby><cites>FETCH-LOGICAL-c325t-d78e4708655e2dcd64d139dd54551bd4040e412284a43c898ead706580e192613</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.fbp.2020.07.021$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids></links><search><creatorcontrib>Huang, Liurong</creatorcontrib><creatorcontrib>Zhang, Wenxue</creatorcontrib><creatorcontrib>Ding, Xiaona</creatorcontrib><creatorcontrib>Wu, Zhengfen</creatorcontrib><creatorcontrib>Li, Yunliang</creatorcontrib><title>Effects of dual-frequency ultrasound with different energy irradiation modes on the structural and emulsifying properties of soy protein isolate</title><title>Food and bioproducts processing</title><description>[Display omitted]
•Effects of ultrasonic pretreatments with different energy irradiation modes were compared.•ESI of SPI treated by EGU was higher than those of EDU and SU.•The influence of EGU on the structure of SPI was more significant than those of EDU and SU.
The effects of dual-frequency ultrasound pretreatments with different energy irradiation modes, including energy-gathered ultrasound (EGU), energy-divergent ultrasound (EDU) and slit ultrasound (SU) on the solubility and emulsifying properties of soy protein isolate (SPI) were investigated. The surface hydrophobicity, intrinsic fluorescence spectra, and circular dichroism spectra of SPI were determined. Results revealed that all ultrasonic pretreatments increased the solubility of SPI significantly (P ≤ 0.05). Ultrasonic pretreatments with EDU and SU could not improve the emulsifying activity (P > 0.05). The emulsion stability index of SPI treated by EGU was higher than those of EDU and SU with the same ultrasonic time and power density. Changes in surface hydrophobicity and intrinsic fluorescence showed the unfolding of protein and exposure of hydrophobic groups as a result of action of ultrasound. The CD spectra of SPI pretreated by optimal EGU, EDU and SU showed that dual-frequency ultrasound induced the decrease of β-sheet contents and increase of α-helix and random coil contents significantly (P ≤ 0.05). In conclusion, the influence of EGU on the structural and emulsifying properties of SPI was more significant than those of EDU and SU.</description><subject>Circular dichroism</subject><subject>Coils</subject><subject>Dichroism</subject><subject>Emulsifying properties</subject><subject>Emulsions</subject><subject>Energy</subject><subject>Energy irradiation mode</subject><subject>Fluorescence</subject><subject>Hydrophobic surfaces</subject><subject>Hydrophobicity</subject><subject>Irradiation</subject><subject>Mechanical properties</subject><subject>Properties</subject><subject>Properties (attributes)</subject><subject>Protein folding</subject><subject>Proteins</subject><subject>Random coil</subject><subject>Solubility</subject><subject>Soy protein isolate</subject><subject>Spectra</subject><subject>Stability</subject><subject>Structure</subject><subject>Ultrasonic imaging</subject><subject>Ultrasound</subject><issn>0960-3085</issn><issn>1744-3571</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp9kM1O3DAQxy3USmxpH6A3Sz0nHTt2PtQTQkCRkLjA2TLxBLzK2svYaZW34JHxspw5jTT6f8z8GPspoBYg2t_benrc1xIk1NDVIMUJ24hOqarRnfjCNjC0UDXQ61P2LaUtAIhe6A17vZwmHHPiceJusXM1Eb4sGMaVL3Mmm-ISHP_v8zN3vkgJQ-YYkJ5W7oms8zb7GPguOiwhgedn5CnTMuaF7MxtceNumZOfVh-e-J7iHil7fG9McT1sMvrAfYqzzfidfZ3snPDHxzxjD1eX9xd_q9u765uL89tqbKTOlet6VB30rdYo3eha5UQzOKeV1uLRKVCASkjZK6uasR96tK6DVveAYpCtaM7Yr2Nu6S8Pp2y2caFQKo1UGrpBDUNbVOKoGimmRDiZPfmdpdUIMAfwZmsKeHMAb6AzBXzx_Dl6sJz_zyOZNPpCFJ2ngtq46D9xvwHrzo4j</recordid><startdate>202009</startdate><enddate>202009</enddate><creator>Huang, Liurong</creator><creator>Zhang, Wenxue</creator><creator>Ding, Xiaona</creator><creator>Wu, Zhengfen</creator><creator>Li, Yunliang</creator><general>Elsevier B.V</general><general>Elsevier Science Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7ST</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H98</scope><scope>L.G</scope><scope>P64</scope><scope>SOI</scope></search><sort><creationdate>202009</creationdate><title>Effects of dual-frequency ultrasound with different energy irradiation modes on the structural and emulsifying properties of soy protein isolate</title><author>Huang, Liurong ; Zhang, Wenxue ; Ding, Xiaona ; Wu, Zhengfen ; Li, Yunliang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c325t-d78e4708655e2dcd64d139dd54551bd4040e412284a43c898ead706580e192613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Circular dichroism</topic><topic>Coils</topic><topic>Dichroism</topic><topic>Emulsifying properties</topic><topic>Emulsions</topic><topic>Energy</topic><topic>Energy irradiation mode</topic><topic>Fluorescence</topic><topic>Hydrophobic surfaces</topic><topic>Hydrophobicity</topic><topic>Irradiation</topic><topic>Mechanical properties</topic><topic>Properties</topic><topic>Properties (attributes)</topic><topic>Protein folding</topic><topic>Proteins</topic><topic>Random coil</topic><topic>Solubility</topic><topic>Soy protein isolate</topic><topic>Spectra</topic><topic>Stability</topic><topic>Structure</topic><topic>Ultrasonic imaging</topic><topic>Ultrasound</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huang, Liurong</creatorcontrib><creatorcontrib>Zhang, Wenxue</creatorcontrib><creatorcontrib>Ding, Xiaona</creatorcontrib><creatorcontrib>Wu, Zhengfen</creatorcontrib><creatorcontrib>Li, Yunliang</creatorcontrib><collection>CrossRef</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Aquaculture Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><jtitle>Food and bioproducts processing</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huang, Liurong</au><au>Zhang, Wenxue</au><au>Ding, Xiaona</au><au>Wu, Zhengfen</au><au>Li, Yunliang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of dual-frequency ultrasound with different energy irradiation modes on the structural and emulsifying properties of soy protein isolate</atitle><jtitle>Food and bioproducts processing</jtitle><date>2020-09</date><risdate>2020</risdate><volume>123</volume><spage>419</spage><epage>426</epage><pages>419-426</pages><issn>0960-3085</issn><eissn>1744-3571</eissn><abstract>[Display omitted]
•Effects of ultrasonic pretreatments with different energy irradiation modes were compared.•ESI of SPI treated by EGU was higher than those of EDU and SU.•The influence of EGU on the structure of SPI was more significant than those of EDU and SU.
The effects of dual-frequency ultrasound pretreatments with different energy irradiation modes, including energy-gathered ultrasound (EGU), energy-divergent ultrasound (EDU) and slit ultrasound (SU) on the solubility and emulsifying properties of soy protein isolate (SPI) were investigated. The surface hydrophobicity, intrinsic fluorescence spectra, and circular dichroism spectra of SPI were determined. Results revealed that all ultrasonic pretreatments increased the solubility of SPI significantly (P ≤ 0.05). Ultrasonic pretreatments with EDU and SU could not improve the emulsifying activity (P > 0.05). The emulsion stability index of SPI treated by EGU was higher than those of EDU and SU with the same ultrasonic time and power density. Changes in surface hydrophobicity and intrinsic fluorescence showed the unfolding of protein and exposure of hydrophobic groups as a result of action of ultrasound. The CD spectra of SPI pretreated by optimal EGU, EDU and SU showed that dual-frequency ultrasound induced the decrease of β-sheet contents and increase of α-helix and random coil contents significantly (P ≤ 0.05). In conclusion, the influence of EGU on the structural and emulsifying properties of SPI was more significant than those of EDU and SU.</abstract><cop>Rugby</cop><pub>Elsevier B.V</pub><doi>10.1016/j.fbp.2020.07.021</doi><tpages>8</tpages></addata></record> |
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| subjects | Circular dichroism Coils Dichroism Emulsifying properties Emulsions Energy Energy irradiation mode Fluorescence Hydrophobic surfaces Hydrophobicity Irradiation Mechanical properties Properties Properties (attributes) Protein folding Proteins Random coil Solubility Soy protein isolate Spectra Stability Structure Ultrasonic imaging Ultrasound |
| title | Effects of dual-frequency ultrasound with different energy irradiation modes on the structural and emulsifying properties of soy protein isolate |
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