Thermal properties of milk fat, xanthine oxidase, caseins and whey proteins in pulsed electric field-treated bovine whole milk
•Pulsed electric field treatment did not alter fat melting temperature.•Electric field treatment induced less protein denaturation than thermal treatment.•Protein surface hydrophobicity increased with the intensity of the electric field.•Pulsed electric field treatment has lower impact on milk funct...
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Veröffentlicht in: | Food chemistry 2016-09, Vol.207, p.34-42 |
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description | •Pulsed electric field treatment did not alter fat melting temperature.•Electric field treatment induced less protein denaturation than thermal treatment.•Protein surface hydrophobicity increased with the intensity of the electric field.•Pulsed electric field treatment has lower impact on milk functionality than heating.
Thermodynamics of milk components (milk fat, xanthine oxidase, caseins and whey proteins) in pulsed electric field (PEF)-treated milk were compared with thermally treated milk (63°C for 30min and 73°C for 15s). PEF treatments were applied at 20 or 26kVcm−1 for 34μs with or without pre-heating of milk (55°C for 24s), using bipolar square wave pulses in a continuous mode of operation. PEF treatments did not affect the final temperatures of fat melting (Tmelting) or xanthine oxidase denaturation (Tdenaturation), whereas thermal treatments increased both the Tmelting of milk fat and the Tdenaturation for xanthine oxidase by 2–3°C. Xanthine oxidase denaturation was ∼13% less after PEF treatments compared with the thermal treatments. The enthalpy change (ΔH of denaturation) of whey proteins decreased in the treated-milk, and denaturation increased with the treatment intensity. New endothermic peaks in the calorimetric thermograms of treated milk revealed the formation of complexes due to interactions between MFGM (milk fat globule membrane) proteins and skim milk proteins. Evidence for the adsorption of complexes onto the MFGM surface was obtained from the increase in surface hydrophobicity of proteins, revealing the presence of unfolded hydrophobic regions. |
doi_str_mv | 10.1016/j.foodchem.2016.03.076 |
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Thermodynamics of milk components (milk fat, xanthine oxidase, caseins and whey proteins) in pulsed electric field (PEF)-treated milk were compared with thermally treated milk (63°C for 30min and 73°C for 15s). PEF treatments were applied at 20 or 26kVcm−1 for 34μs with or without pre-heating of milk (55°C for 24s), using bipolar square wave pulses in a continuous mode of operation. PEF treatments did not affect the final temperatures of fat melting (Tmelting) or xanthine oxidase denaturation (Tdenaturation), whereas thermal treatments increased both the Tmelting of milk fat and the Tdenaturation for xanthine oxidase by 2–3°C. Xanthine oxidase denaturation was ∼13% less after PEF treatments compared with the thermal treatments. The enthalpy change (ΔH of denaturation) of whey proteins decreased in the treated-milk, and denaturation increased with the treatment intensity. New endothermic peaks in the calorimetric thermograms of treated milk revealed the formation of complexes due to interactions between MFGM (milk fat globule membrane) proteins and skim milk proteins. Evidence for the adsorption of complexes onto the MFGM surface was obtained from the increase in surface hydrophobicity of proteins, revealing the presence of unfolded hydrophobic regions.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2016.03.076</identifier><identifier>PMID: 27080877</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Animals ; Calorimetry, Differential Scanning - methods ; Caseins - analysis ; Caseins - chemistry ; Cattle ; Differential scanning calorimetry ; Fat melting ; Glycolipids - chemistry ; Glycoproteins - chemistry ; Protein denaturation ; Pulsed electric field ; Surface hydrophobicity ; Whey Proteins - chemistry ; Xanthine Oxidase - analysis ; Xanthine Oxidase - chemistry</subject><ispartof>Food chemistry, 2016-09, Vol.207, p.34-42</ispartof><rights>2016 Elsevier Ltd</rights><rights>Copyright © 2016 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-8f3c4cd9d2a4370981b07f5ec231ded63fd5c665478e6e44d515b20f796318593</citedby><cites>FETCH-LOGICAL-c504t-8f3c4cd9d2a4370981b07f5ec231ded63fd5c665478e6e44d515b20f796318593</cites><orcidid>0000-0001-5094-5123</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.2016.03.076$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27080877$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sharma, Pankaj</creatorcontrib><creatorcontrib>Oey, Indrawati</creatorcontrib><creatorcontrib>Everett, David W.</creatorcontrib><title>Thermal properties of milk fat, xanthine oxidase, caseins and whey proteins in pulsed electric field-treated bovine whole milk</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>•Pulsed electric field treatment did not alter fat melting temperature.•Electric field treatment induced less protein denaturation than thermal treatment.•Protein surface hydrophobicity increased with the intensity of the electric field.•Pulsed electric field treatment has lower impact on milk functionality than heating.
Thermodynamics of milk components (milk fat, xanthine oxidase, caseins and whey proteins) in pulsed electric field (PEF)-treated milk were compared with thermally treated milk (63°C for 30min and 73°C for 15s). PEF treatments were applied at 20 or 26kVcm−1 for 34μs with or without pre-heating of milk (55°C for 24s), using bipolar square wave pulses in a continuous mode of operation. PEF treatments did not affect the final temperatures of fat melting (Tmelting) or xanthine oxidase denaturation (Tdenaturation), whereas thermal treatments increased both the Tmelting of milk fat and the Tdenaturation for xanthine oxidase by 2–3°C. Xanthine oxidase denaturation was ∼13% less after PEF treatments compared with the thermal treatments. The enthalpy change (ΔH of denaturation) of whey proteins decreased in the treated-milk, and denaturation increased with the treatment intensity. New endothermic peaks in the calorimetric thermograms of treated milk revealed the formation of complexes due to interactions between MFGM (milk fat globule membrane) proteins and skim milk proteins. Evidence for the adsorption of complexes onto the MFGM surface was obtained from the increase in surface hydrophobicity of proteins, revealing the presence of unfolded hydrophobic regions.</description><subject>Animals</subject><subject>Calorimetry, Differential Scanning - methods</subject><subject>Caseins - analysis</subject><subject>Caseins - chemistry</subject><subject>Cattle</subject><subject>Differential scanning calorimetry</subject><subject>Fat melting</subject><subject>Glycolipids - chemistry</subject><subject>Glycoproteins - chemistry</subject><subject>Protein denaturation</subject><subject>Pulsed electric field</subject><subject>Surface hydrophobicity</subject><subject>Whey Proteins - chemistry</subject><subject>Xanthine Oxidase - analysis</subject><subject>Xanthine Oxidase - chemistry</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EokvhL1Q-cmjCOI4_9gaqClSqxKWcLa89Vrwk8WJn-3Hht-Pttr32MtaMnndea15Czhi0DJj8sm1DSt4NOLVd7VvgLSj5hqyYVrxRoLq3ZAUcdKNZL0_Ih1K2AFBZ_Z6cdAo0aKVW5N_NgHmyI93ltMO8RCw0BTrF8Q8Ndjmn93ZehjgjTffR24Ln1NUa50Lt7OndgA8H6fI4iTPd7ceCnuKIbsnR0RBx9M2S0S51vEm3h1V3Qxrx0eMjeRdsVXx6ek_J7--XNxc_m-tfP64uvl03TkC_NDpw1zu_9p3tuYK1ZhtQQaDrOPPoJQ9eOClFrzRK7HsvmNh0ENRacqbFmp-Sz8e99a9_91gWM8XicBztjGlfDNMgBIhOda-jSjPRMyZVReURdTmVkjGYXY6TzQ-GgTnEZLbmOSZziMkANzWmKjx78thvJvQvsudcKvD1CGA9ym3EbIqLODv0MdfLGp_iax7_AQPEqAo</recordid><startdate>20160915</startdate><enddate>20160915</enddate><creator>Sharma, Pankaj</creator><creator>Oey, Indrawati</creator><creator>Everett, David W.</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><scope>7U7</scope><scope>C1K</scope><orcidid>https://orcid.org/0000-0001-5094-5123</orcidid></search><sort><creationdate>20160915</creationdate><title>Thermal properties of milk fat, xanthine oxidase, caseins and whey proteins in pulsed electric field-treated bovine whole milk</title><author>Sharma, Pankaj ; Oey, Indrawati ; Everett, David W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-8f3c4cd9d2a4370981b07f5ec231ded63fd5c665478e6e44d515b20f796318593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animals</topic><topic>Calorimetry, Differential Scanning - methods</topic><topic>Caseins - analysis</topic><topic>Caseins - chemistry</topic><topic>Cattle</topic><topic>Differential scanning calorimetry</topic><topic>Fat melting</topic><topic>Glycolipids - chemistry</topic><topic>Glycoproteins - chemistry</topic><topic>Protein denaturation</topic><topic>Pulsed electric field</topic><topic>Surface hydrophobicity</topic><topic>Whey Proteins - chemistry</topic><topic>Xanthine Oxidase - analysis</topic><topic>Xanthine Oxidase - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sharma, Pankaj</creatorcontrib><creatorcontrib>Oey, Indrawati</creatorcontrib><creatorcontrib>Everett, David W.</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><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sharma, Pankaj</au><au>Oey, Indrawati</au><au>Everett, David W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thermal properties of milk fat, xanthine oxidase, caseins and whey proteins in pulsed electric field-treated bovine whole milk</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2016-09-15</date><risdate>2016</risdate><volume>207</volume><spage>34</spage><epage>42</epage><pages>34-42</pages><issn>0308-8146</issn><eissn>1873-7072</eissn><abstract>•Pulsed electric field treatment did not alter fat melting temperature.•Electric field treatment induced less protein denaturation than thermal treatment.•Protein surface hydrophobicity increased with the intensity of the electric field.•Pulsed electric field treatment has lower impact on milk functionality than heating.
Thermodynamics of milk components (milk fat, xanthine oxidase, caseins and whey proteins) in pulsed electric field (PEF)-treated milk were compared with thermally treated milk (63°C for 30min and 73°C for 15s). PEF treatments were applied at 20 or 26kVcm−1 for 34μs with or without pre-heating of milk (55°C for 24s), using bipolar square wave pulses in a continuous mode of operation. PEF treatments did not affect the final temperatures of fat melting (Tmelting) or xanthine oxidase denaturation (Tdenaturation), whereas thermal treatments increased both the Tmelting of milk fat and the Tdenaturation for xanthine oxidase by 2–3°C. Xanthine oxidase denaturation was ∼13% less after PEF treatments compared with the thermal treatments. The enthalpy change (ΔH of denaturation) of whey proteins decreased in the treated-milk, and denaturation increased with the treatment intensity. New endothermic peaks in the calorimetric thermograms of treated milk revealed the formation of complexes due to interactions between MFGM (milk fat globule membrane) proteins and skim milk proteins. Evidence for the adsorption of complexes onto the MFGM surface was obtained from the increase in surface hydrophobicity of proteins, revealing the presence of unfolded hydrophobic regions.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>27080877</pmid><doi>10.1016/j.foodchem.2016.03.076</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0001-5094-5123</orcidid></addata></record> |
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subjects | Animals Calorimetry, Differential Scanning - methods Caseins - analysis Caseins - chemistry Cattle Differential scanning calorimetry Fat melting Glycolipids - chemistry Glycoproteins - chemistry Protein denaturation Pulsed electric field Surface hydrophobicity Whey Proteins - chemistry Xanthine Oxidase - analysis Xanthine Oxidase - chemistry |
title | Thermal properties of milk fat, xanthine oxidase, caseins and whey proteins in pulsed electric field-treated bovine whole milk |
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