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Changes of structural and techno-functional properties of high hydrostatic pressure (HHP) treated whey protein isolate over refrigerated storage
This work assessed the effect of storage time on the structure and functionality of HHP-treated whey protein isolate (WPI). Different pressures (100–600 MPa) and treatment times (15–30 min) were applied to aqueous WPI dispersions (5% w/v). The induced degree of unfolding was evaluated to select opti...
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Published in: | Food science & technology 2021-02, Vol.137, p.110436, Article 110436 |
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description | This work assessed the effect of storage time on the structure and functionality of HHP-treated whey protein isolate (WPI). Different pressures (100–600 MPa) and treatment times (15–30 min) were applied to aqueous WPI dispersions (5% w/v). The induced degree of unfolding was evaluated to select optimal HHP treatment conditions of WPI before storage at 4 °C. Conformational and techno-functional properties of untreated and optimally HHP-treated WPI samples were determined by UV–Vis and IR spectroscopy, foaming capacity, and interfacial tension measurements, respectively. Further tests of HHP-assisted hydrolysis of WPI were performed by α-chymotrypsin, bromelain, or their mixture (1:1 w/w), with the degree of hydrolysis (DH%) and electrophoretic patterns analyzed.
The maximum unfolding degree was detected after a treatment of 400 MPa and 15 min and, at these processing conditions, no aggregation occurred. However, the structural changes achieved upon HHP were gradually lost during storage through a first-order refolding process (kREF. = 0.031 h−1), with restoring of native functionality.
Hydrolysis performances of selected enzymes towards WPI were significantly promoted by high-pressure. Interestingly, a clear synergistic effect of α-chymotrypsin and bromelain combination on the WPI hydrolysis yield was detected, which resulted in the highest protein rupture (DH = 17%).
•HHP treatment induced WPI unfolding and enhanced its interfacial properties.•WPI pre-treated by HHP under optimal conditions underwent refolding and loss of functionality during refrigerated storage.•HHP dramatically improved the enzymatic hydrolysis of WPI.•Combining α-chymotrypsin and bromelain resulted in a synergistic effect on the degree of hydrolysis of WPI. |
doi_str_mv | 10.1016/j.lwt.2020.110436 |
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The maximum unfolding degree was detected after a treatment of 400 MPa and 15 min and, at these processing conditions, no aggregation occurred. However, the structural changes achieved upon HHP were gradually lost during storage through a first-order refolding process (kREF. = 0.031 h−1), with restoring of native functionality.
Hydrolysis performances of selected enzymes towards WPI were significantly promoted by high-pressure. Interestingly, a clear synergistic effect of α-chymotrypsin and bromelain combination on the WPI hydrolysis yield was detected, which resulted in the highest protein rupture (DH = 17%).
•HHP treatment induced WPI unfolding and enhanced its interfacial properties.•WPI pre-treated by HHP under optimal conditions underwent refolding and loss of functionality during refrigerated storage.•HHP dramatically improved the enzymatic hydrolysis of WPI.•Combining α-chymotrypsin and bromelain resulted in a synergistic effect on the degree of hydrolysis of WPI.</description><identifier>ISSN: 0023-6438</identifier><identifier>EISSN: 1096-1127</identifier><identifier>DOI: 10.1016/j.lwt.2020.110436</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Denaturing gel electrophoresis (SDS-PAGE) ; High hydrostatic pressure (HHP) ; Refolding ; Techno-functional properties ; Whey protein isolate (WPI)</subject><ispartof>Food science & technology, 2021-02, Vol.137, p.110436, Article 110436</ispartof><rights>2020 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c340t-9b6817776e635f0c193d9f697ff76b9efbac07cd2df8965de7561d60df36da693</citedby><cites>FETCH-LOGICAL-c340t-9b6817776e635f0c193d9f697ff76b9efbac07cd2df8965de7561d60df36da693</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27907,27908</link.rule.ids></links><search><creatorcontrib>Carullo, D.</creatorcontrib><creatorcontrib>Barbosa-Cánovas, G.V.</creatorcontrib><creatorcontrib>Ferrari, G.</creatorcontrib><title>Changes of structural and techno-functional properties of high hydrostatic pressure (HHP) treated whey protein isolate over refrigerated storage</title><title>Food science & technology</title><description>This work assessed the effect of storage time on the structure and functionality of HHP-treated whey protein isolate (WPI). Different pressures (100–600 MPa) and treatment times (15–30 min) were applied to aqueous WPI dispersions (5% w/v). The induced degree of unfolding was evaluated to select optimal HHP treatment conditions of WPI before storage at 4 °C. Conformational and techno-functional properties of untreated and optimally HHP-treated WPI samples were determined by UV–Vis and IR spectroscopy, foaming capacity, and interfacial tension measurements, respectively. Further tests of HHP-assisted hydrolysis of WPI were performed by α-chymotrypsin, bromelain, or their mixture (1:1 w/w), with the degree of hydrolysis (DH%) and electrophoretic patterns analyzed.
The maximum unfolding degree was detected after a treatment of 400 MPa and 15 min and, at these processing conditions, no aggregation occurred. However, the structural changes achieved upon HHP were gradually lost during storage through a first-order refolding process (kREF. = 0.031 h−1), with restoring of native functionality.
Hydrolysis performances of selected enzymes towards WPI were significantly promoted by high-pressure. Interestingly, a clear synergistic effect of α-chymotrypsin and bromelain combination on the WPI hydrolysis yield was detected, which resulted in the highest protein rupture (DH = 17%).
•HHP treatment induced WPI unfolding and enhanced its interfacial properties.•WPI pre-treated by HHP under optimal conditions underwent refolding and loss of functionality during refrigerated storage.•HHP dramatically improved the enzymatic hydrolysis of WPI.•Combining α-chymotrypsin and bromelain resulted in a synergistic effect on the degree of hydrolysis of WPI.</description><subject>Denaturing gel electrophoresis (SDS-PAGE)</subject><subject>High hydrostatic pressure (HHP)</subject><subject>Refolding</subject><subject>Techno-functional properties</subject><subject>Whey protein isolate (WPI)</subject><issn>0023-6438</issn><issn>1096-1127</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp9kLFOwzAQhi0EEqXwAGweYUix49SpxYQqoEiVYIDZcu1z4irEle0U9S14ZFzCzC2n----068foWtKZpRQfreddV9pVpIyz5RUjJ-gCSWCF5SW9SmaEFKygldscY4uYtySXFW5mKDvZav6BiL2FscUBp2GoDqseoMT6Lb3hR16nZzvs7oLfgchufG8dU2L24MJPiaVnM5riHEIgG9Wq7dbnAKoBAZ_tXA4oglcj130XVax30PAAWxwDYTfs5h8UA1cojOrughXf32KPp4e35erYv36_LJ8WBeaVSQVYsMXtK5rDpzNLdFUMCMsF7W1Nd8IsBulSa1NaexC8LmBes6p4cRYxo3igk0RHf_q7D9mJ3IX3KcKB0mJPEYqtzJHKo-RyjHSzNyPDGRjewdBRu2g12BcAJ2k8e4f-gfXMIMh</recordid><startdate>202102</startdate><enddate>202102</enddate><creator>Carullo, D.</creator><creator>Barbosa-Cánovas, G.V.</creator><creator>Ferrari, G.</creator><general>Elsevier Ltd</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>202102</creationdate><title>Changes of structural and techno-functional properties of high hydrostatic pressure (HHP) treated whey protein isolate over refrigerated storage</title><author>Carullo, D. ; Barbosa-Cánovas, G.V. ; Ferrari, G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-9b6817776e635f0c193d9f697ff76b9efbac07cd2df8965de7561d60df36da693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Denaturing gel electrophoresis (SDS-PAGE)</topic><topic>High hydrostatic pressure (HHP)</topic><topic>Refolding</topic><topic>Techno-functional properties</topic><topic>Whey protein isolate (WPI)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carullo, D.</creatorcontrib><creatorcontrib>Barbosa-Cánovas, G.V.</creatorcontrib><creatorcontrib>Ferrari, G.</creatorcontrib><collection>CrossRef</collection><jtitle>Food science & technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Carullo, D.</au><au>Barbosa-Cánovas, G.V.</au><au>Ferrari, G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Changes of structural and techno-functional properties of high hydrostatic pressure (HHP) treated whey protein isolate over refrigerated storage</atitle><jtitle>Food science & technology</jtitle><date>2021-02</date><risdate>2021</risdate><volume>137</volume><spage>110436</spage><pages>110436-</pages><artnum>110436</artnum><issn>0023-6438</issn><eissn>1096-1127</eissn><abstract>This work assessed the effect of storage time on the structure and functionality of HHP-treated whey protein isolate (WPI). Different pressures (100–600 MPa) and treatment times (15–30 min) were applied to aqueous WPI dispersions (5% w/v). The induced degree of unfolding was evaluated to select optimal HHP treatment conditions of WPI before storage at 4 °C. Conformational and techno-functional properties of untreated and optimally HHP-treated WPI samples were determined by UV–Vis and IR spectroscopy, foaming capacity, and interfacial tension measurements, respectively. Further tests of HHP-assisted hydrolysis of WPI were performed by α-chymotrypsin, bromelain, or their mixture (1:1 w/w), with the degree of hydrolysis (DH%) and electrophoretic patterns analyzed.
The maximum unfolding degree was detected after a treatment of 400 MPa and 15 min and, at these processing conditions, no aggregation occurred. However, the structural changes achieved upon HHP were gradually lost during storage through a first-order refolding process (kREF. = 0.031 h−1), with restoring of native functionality.
Hydrolysis performances of selected enzymes towards WPI were significantly promoted by high-pressure. Interestingly, a clear synergistic effect of α-chymotrypsin and bromelain combination on the WPI hydrolysis yield was detected, which resulted in the highest protein rupture (DH = 17%).
•HHP treatment induced WPI unfolding and enhanced its interfacial properties.•WPI pre-treated by HHP under optimal conditions underwent refolding and loss of functionality during refrigerated storage.•HHP dramatically improved the enzymatic hydrolysis of WPI.•Combining α-chymotrypsin and bromelain resulted in a synergistic effect on the degree of hydrolysis of WPI.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.lwt.2020.110436</doi><oa>free_for_read</oa></addata></record> |
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subjects | Denaturing gel electrophoresis (SDS-PAGE) High hydrostatic pressure (HHP) Refolding Techno-functional properties Whey protein isolate (WPI) |
title | Changes of structural and techno-functional properties of high hydrostatic pressure (HHP) treated whey protein isolate over refrigerated storage |
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