Enthalpy-entropy compensation in calcium binding to acid-base forms of glycine tyrosine dipeptides from hydrolysis of α-lactalbumin
[Display omitted] •GlyTyr binds calcium stronger for the pH condition of the intestine than TyrGly.•Calcium binding to acid/base forms of GlyTyr and TyrGly dipeptides is at neutral pH strongly exothermic.•Density Functional Theory suggests calcium binding to occur at carboxylates and amides.•Enthalp...
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| Veröffentlicht in: | Food research international 2021-11, Vol.149, p.110714-110714, Article 110714 |
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| creator | Jiang, Yuan Liu, Xiao-Chen Ahrné, Lilia M. Skibsted, Leif H. |
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•GlyTyr binds calcium stronger for the pH condition of the intestine than TyrGly.•Calcium binding to acid/base forms of GlyTyr and TyrGly dipeptides is at neutral pH strongly exothermic.•Density Functional Theory suggests calcium binding to occur at carboxylates and amides.•Enthalpy–entropy compensation controls calcium binding to GlyTyr and TyrGly acid/base forms.•Calcium binding to GlyTyr and TyrGly decreases radical scavenging and antioxidative activity.
Calcium binding to peptides formed by hydrolysis of whey proteins during digestion is important for calcium uptake in the intestines and affects the antioxidant function of the peptides. For the two dipeptides, Gly-Tyr and Tyr-Gly, potential hydrolysis products of α-lactalbumin, calcium binding to the three forms of each dipeptide in acid-base equilibrium at intestinal pH was determined electrochemically and compared to binding to tyrosine for aqueous 0.16 M NaCl for 5 |
| doi_str_mv | 10.1016/j.foodres.2021.110714 |
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| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2579088592</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S096399692100613X</els_id><sourcerecordid>2579088592</sourcerecordid><originalsourceid>FETCH-LOGICAL-c389t-9e62498f674ef733649e2b6cd5eec8ca527f5e63b8836dd73fbfe0906803e75a3</originalsourceid><addsrcrecordid>eNqFkLFuFDEYhC0EEkfgEZBc0uxhr2-9doVQFAJSpDRQW177d_KfvPZi-5C254V4EZ6JPS59qpliZqT5CHnP2Z4zLj8e9yFnX6Due9bzPeds5IcXZMfVKLrNDi_JjmkpOq2lfk3e1HpkjMlh1Dvy-ya1RxuXtYPUSl5W6vK8QKq2YU4UE3U2OjzNdMLkMT3Qlql16LvJVqAhl7nSHOhDXB0moG0tuZ6NxwWWhh4qDSXP9HH1Jce14v_43z9dtK7ZOJ1mTG_Jq2BjhXdPekV-fLn5fv21u7u__Xb9-a5zQunWaZD9QasgxwOEUQh50NBP0vkBwClnh34MA0gxKSWk96MIUwCmmVRMwDhYcUU-XHaXkn-eoDYzY3UQo02QT9X0GxKm1KD7LTpcom77UwsEsxScbVkNZ-ZM3RzNE3Vzpm4u1Lfep0sPth-_EIqpDiE58FjANeMzPrPwD2VlkjM</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2579088592</pqid></control><display><type>article</type><title>Enthalpy-entropy compensation in calcium binding to acid-base forms of glycine tyrosine dipeptides from hydrolysis of α-lactalbumin</title><source>Elsevier ScienceDirect Journals</source><creator>Jiang, Yuan ; Liu, Xiao-Chen ; Ahrné, Lilia M. ; Skibsted, Leif H.</creator><creatorcontrib>Jiang, Yuan ; Liu, Xiao-Chen ; Ahrné, Lilia M. ; Skibsted, Leif H.</creatorcontrib><description>[Display omitted]
•GlyTyr binds calcium stronger for the pH condition of the intestine than TyrGly.•Calcium binding to acid/base forms of GlyTyr and TyrGly dipeptides is at neutral pH strongly exothermic.•Density Functional Theory suggests calcium binding to occur at carboxylates and amides.•Enthalpy–entropy compensation controls calcium binding to GlyTyr and TyrGly acid/base forms.•Calcium binding to GlyTyr and TyrGly decreases radical scavenging and antioxidative activity.
Calcium binding to peptides formed by hydrolysis of whey proteins during digestion is important for calcium uptake in the intestines and affects the antioxidant function of the peptides. For the two dipeptides, Gly-Tyr and Tyr-Gly, potential hydrolysis products of α-lactalbumin, calcium binding to the three forms of each dipeptide in acid-base equilibrium at intestinal pH was determined electrochemically and compared to binding to tyrosine for aqueous 0.16 M NaCl for 5 < pH < 9 at 15 °C, 25 °C, and 37 °C. At milk pH at 25 °C, binding of calcium to the zwitterion of GlyTyr dominates, with an association constant Kass2 = 22 M−1 with ΔH0 = −46 kJ·mol−1, while binding to the mononegative TyrGly dominates for TyrGly with Kass3 = 32 M−1 and ΔH0 = −38 kJ·mol−1. At intestinal conditions, pH = 7 and 37 °C, binding of calcium has similar affinity for GlyTyr and TyrGly, while at higher pH and lower temperature, GlyTyr binds stronger. Density Functional Theory calculations confirmed a stronger binding to the zwitterion of GlyTyr than of TyrGly and an increasing affinity with increasing pH for both. Calcium binding to the acid/base forms of the dipeptides is at neutral pH strongly exothermic with ΔH0 becoming less negative at higher pH, and a linear enthalpy–entropy compensation (r2 = 0.99) results in comparable binding important for calcium bioavailability along the changing distribution among acid-base forms. Calcium binding decreases radical scavenging rate and antioxidative activity of both dipeptides.</description><identifier>ISSN: 0963-9969</identifier><identifier>EISSN: 1873-7145</identifier><identifier>DOI: 10.1016/j.foodres.2021.110714</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Calcium binding ; Calcium bioavailability ; Density Functional Theory ; Dipeptide ; Enthalpy–entropy compensation</subject><ispartof>Food research international, 2021-11, Vol.149, p.110714-110714, Article 110714</ispartof><rights>2021 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-9e62498f674ef733649e2b6cd5eec8ca527f5e63b8836dd73fbfe0906803e75a3</citedby><cites>FETCH-LOGICAL-c389t-9e62498f674ef733649e2b6cd5eec8ca527f5e63b8836dd73fbfe0906803e75a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S096399692100613X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids></links><search><creatorcontrib>Jiang, Yuan</creatorcontrib><creatorcontrib>Liu, Xiao-Chen</creatorcontrib><creatorcontrib>Ahrné, Lilia M.</creatorcontrib><creatorcontrib>Skibsted, Leif H.</creatorcontrib><title>Enthalpy-entropy compensation in calcium binding to acid-base forms of glycine tyrosine dipeptides from hydrolysis of α-lactalbumin</title><title>Food research international</title><description>[Display omitted]
•GlyTyr binds calcium stronger for the pH condition of the intestine than TyrGly.•Calcium binding to acid/base forms of GlyTyr and TyrGly dipeptides is at neutral pH strongly exothermic.•Density Functional Theory suggests calcium binding to occur at carboxylates and amides.•Enthalpy–entropy compensation controls calcium binding to GlyTyr and TyrGly acid/base forms.•Calcium binding to GlyTyr and TyrGly decreases radical scavenging and antioxidative activity.
Calcium binding to peptides formed by hydrolysis of whey proteins during digestion is important for calcium uptake in the intestines and affects the antioxidant function of the peptides. For the two dipeptides, Gly-Tyr and Tyr-Gly, potential hydrolysis products of α-lactalbumin, calcium binding to the three forms of each dipeptide in acid-base equilibrium at intestinal pH was determined electrochemically and compared to binding to tyrosine for aqueous 0.16 M NaCl for 5 < pH < 9 at 15 °C, 25 °C, and 37 °C. At milk pH at 25 °C, binding of calcium to the zwitterion of GlyTyr dominates, with an association constant Kass2 = 22 M−1 with ΔH0 = −46 kJ·mol−1, while binding to the mononegative TyrGly dominates for TyrGly with Kass3 = 32 M−1 and ΔH0 = −38 kJ·mol−1. At intestinal conditions, pH = 7 and 37 °C, binding of calcium has similar affinity for GlyTyr and TyrGly, while at higher pH and lower temperature, GlyTyr binds stronger. Density Functional Theory calculations confirmed a stronger binding to the zwitterion of GlyTyr than of TyrGly and an increasing affinity with increasing pH for both. Calcium binding to the acid/base forms of the dipeptides is at neutral pH strongly exothermic with ΔH0 becoming less negative at higher pH, and a linear enthalpy–entropy compensation (r2 = 0.99) results in comparable binding important for calcium bioavailability along the changing distribution among acid-base forms. Calcium binding decreases radical scavenging rate and antioxidative activity of both dipeptides.</description><subject>Calcium binding</subject><subject>Calcium bioavailability</subject><subject>Density Functional Theory</subject><subject>Dipeptide</subject><subject>Enthalpy–entropy compensation</subject><issn>0963-9969</issn><issn>1873-7145</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNqFkLFuFDEYhC0EEkfgEZBc0uxhr2-9doVQFAJSpDRQW177d_KfvPZi-5C254V4EZ6JPS59qpliZqT5CHnP2Z4zLj8e9yFnX6Due9bzPeds5IcXZMfVKLrNDi_JjmkpOq2lfk3e1HpkjMlh1Dvy-ya1RxuXtYPUSl5W6vK8QKq2YU4UE3U2OjzNdMLkMT3Qlql16LvJVqAhl7nSHOhDXB0moG0tuZ6NxwWWhh4qDSXP9HH1Jce14v_43z9dtK7ZOJ1mTG_Jq2BjhXdPekV-fLn5fv21u7u__Xb9-a5zQunWaZD9QasgxwOEUQh50NBP0vkBwClnh34MA0gxKSWk96MIUwCmmVRMwDhYcUU-XHaXkn-eoDYzY3UQo02QT9X0GxKm1KD7LTpcom77UwsEsxScbVkNZ-ZM3RzNE3Vzpm4u1Lfep0sPth-_EIqpDiE58FjANeMzPrPwD2VlkjM</recordid><startdate>202111</startdate><enddate>202111</enddate><creator>Jiang, Yuan</creator><creator>Liu, Xiao-Chen</creator><creator>Ahrné, Lilia M.</creator><creator>Skibsted, Leif H.</creator><general>Elsevier Ltd</general><scope>6I.</scope><scope>AAFTH</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>202111</creationdate><title>Enthalpy-entropy compensation in calcium binding to acid-base forms of glycine tyrosine dipeptides from hydrolysis of α-lactalbumin</title><author>Jiang, Yuan ; Liu, Xiao-Chen ; Ahrné, Lilia M. ; Skibsted, Leif H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-9e62498f674ef733649e2b6cd5eec8ca527f5e63b8836dd73fbfe0906803e75a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Calcium binding</topic><topic>Calcium bioavailability</topic><topic>Density Functional Theory</topic><topic>Dipeptide</topic><topic>Enthalpy–entropy compensation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jiang, Yuan</creatorcontrib><creatorcontrib>Liu, Xiao-Chen</creatorcontrib><creatorcontrib>Ahrné, Lilia M.</creatorcontrib><creatorcontrib>Skibsted, Leif H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Food research international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jiang, Yuan</au><au>Liu, Xiao-Chen</au><au>Ahrné, Lilia M.</au><au>Skibsted, Leif H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enthalpy-entropy compensation in calcium binding to acid-base forms of glycine tyrosine dipeptides from hydrolysis of α-lactalbumin</atitle><jtitle>Food research international</jtitle><date>2021-11</date><risdate>2021</risdate><volume>149</volume><spage>110714</spage><epage>110714</epage><pages>110714-110714</pages><artnum>110714</artnum><issn>0963-9969</issn><eissn>1873-7145</eissn><abstract>[Display omitted]
•GlyTyr binds calcium stronger for the pH condition of the intestine than TyrGly.•Calcium binding to acid/base forms of GlyTyr and TyrGly dipeptides is at neutral pH strongly exothermic.•Density Functional Theory suggests calcium binding to occur at carboxylates and amides.•Enthalpy–entropy compensation controls calcium binding to GlyTyr and TyrGly acid/base forms.•Calcium binding to GlyTyr and TyrGly decreases radical scavenging and antioxidative activity.
Calcium binding to peptides formed by hydrolysis of whey proteins during digestion is important for calcium uptake in the intestines and affects the antioxidant function of the peptides. For the two dipeptides, Gly-Tyr and Tyr-Gly, potential hydrolysis products of α-lactalbumin, calcium binding to the three forms of each dipeptide in acid-base equilibrium at intestinal pH was determined electrochemically and compared to binding to tyrosine for aqueous 0.16 M NaCl for 5 < pH < 9 at 15 °C, 25 °C, and 37 °C. At milk pH at 25 °C, binding of calcium to the zwitterion of GlyTyr dominates, with an association constant Kass2 = 22 M−1 with ΔH0 = −46 kJ·mol−1, while binding to the mononegative TyrGly dominates for TyrGly with Kass3 = 32 M−1 and ΔH0 = −38 kJ·mol−1. At intestinal conditions, pH = 7 and 37 °C, binding of calcium has similar affinity for GlyTyr and TyrGly, while at higher pH and lower temperature, GlyTyr binds stronger. Density Functional Theory calculations confirmed a stronger binding to the zwitterion of GlyTyr than of TyrGly and an increasing affinity with increasing pH for both. Calcium binding to the acid/base forms of the dipeptides is at neutral pH strongly exothermic with ΔH0 becoming less negative at higher pH, and a linear enthalpy–entropy compensation (r2 = 0.99) results in comparable binding important for calcium bioavailability along the changing distribution among acid-base forms. Calcium binding decreases radical scavenging rate and antioxidative activity of both dipeptides.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.foodres.2021.110714</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Calcium binding Calcium bioavailability Density Functional Theory Dipeptide Enthalpy–entropy compensation |
| title | Enthalpy-entropy compensation in calcium binding to acid-base forms of glycine tyrosine dipeptides from hydrolysis of α-lactalbumin |
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