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            <title xml:lang="en">Mineral modulation of thermal aggregation and gelation of whey proteins: from $\beta$-lactoglobulin model system to whey protein isolate</title>
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                <forename type="first">Florence</forename>
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            <idno type="halRefHtml">&lt;i&gt;Le Lait&lt;/i&gt;, 2003, 83 (5), pp.353-364. &lt;a target="_blank" href="https://dx.doi.org/10.1051/lait:2003021"&gt;&amp;#x27E8;10.1051/lait:2003021&amp;#x27E9;&lt;/a&gt;</idno>
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                <title xml:lang="en">Mineral modulation of thermal aggregation and gelation of whey proteins: from $\beta$-lactoglobulin model system to whey protein isolate</title>
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                    <forename type="first">Florence</forename>
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                    <surname>Famelart</surname>
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                  <persName>
                    <forename type="first">Jean-Louis</forename>
                    <surname>Maubois</surname>
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                  <idno type="halauthorid">765546-0</idno>
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                <author role="aut">
                  <persName>
                    <forename type="first">Said</forename>
                    <surname>Bouhallab</surname>
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                  <email type="md5">453131a699232b907c089befecc22fe5</email>
                  <email type="domain">inrae.fr</email>
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                <title level="j">Le Lait</title>
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                  <date type="datePub">2003</date>
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                <term xml:lang="fr">agrégation</term>
                <term xml:lang="fr">gélification</term>
                <term xml:lang="fr">calcium</term>
                <term xml:lang="fr">sodium</term>
                <term xml:lang="fr">gelation&lt;br&gt;---&lt;br&gt;Protéine de lactosérum</term>
                <term xml:lang="fr">aggregation</term>
                <term xml:lang="fr">Whey protein</term>
              </keywords>
              <classCode scheme="halDomain" n="sdv.aen">Life Sciences [q-bio]/Food and Nutrition</classCode>
              <classCode scheme="halDomain" n="sdv.ida">Life Sciences [q-bio]/Food engineering</classCode>
              <classCode scheme="vocinrae-old" n="produit laitier">produit laitier</classCode>
              <classCode scheme="vocinrae-old" n="calcium">calcium</classCode>
              <classCode scheme="vocinrae-old" n="gelation thermique">gelation thermique</classCode>
              <classCode scheme="vocinrae-old" n="technologie laitière">technologie laitière</classCode>
              <classCode scheme="vocinrae-old" n="agrégation">agrégation</classCode>
              <classCode scheme="vocinrae-old" n="pont disulfure">pont disulfure</classCode>
              <classCode scheme="vocinrae-old" n="protéine de lactosérum">protéine de lactosérum</classCode>
              <classCode scheme="vocinrae-old" n="sodium">sodium</classCode>
              <classCode scheme="halTypology" n="ART">Journal articles</classCode>
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              <p>Solutions of 100 g$\cdot$kg$^{-1}$ of $\beta$-lactoglobulin ($\beta$-Lg), $\beta$-Lg + $\alpha$-lactalbumin ($\alpha$-La), $\beta$-Lg + $\alpha$-La + bovine serum albumin (BSA) or whey protein isolate (WPI) were heated at 75 °C, pH 6.8 in water and in the presence of either 100 mmol$\cdot$L$^{-1}$ NaCl or 10 mmol$\cdot$L$^{-1}$ CaCl$_2$. The subsequent polymerisation-aggregation processes in solution before gelation and the physical properties of the formed gels were determined. The disappearance of native-like proteins, formation of $\beta$-Lg covalent dimer and the nature of the interactions involved in the formed aggregates were addressed. Whatever the protein system, both NaCl and CaCl$_2$ increased gel strength and decreased gelation time. At gelling time, relatively small aggregates, formed by the contribution of the total initial amount of proteins, were observed in samples without added salts. In contrast, with NaCl or CaCl$_2$, only part of the initial amount of proteins was aggregated before gel time. Very large aggregates were formed in the presence of calcium. Under these two mineral conditions, as well as in samples without added salt, covalent disulphide bonds were seen to be the major forces involved in the aggregation process at gel time.</p>
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              <p>Modulation de l'agrégation et de la gélification des protéines de lactosérum par les minéraux : de la $\beta$-lactoglobuline pure à l'isolat de protéines sériques. Des gels de différentes solutions de protéines ($\beta$-lactoglobuline ($\beta$-Lg), $\beta$-Lg + $\alpha$-lactalbumine ($\alpha$-La), $\beta$-Lg + $\alpha$-La + sérum albumine bovine (BSA), isolat de protéines sériques) à 100 g$\cdot$kg$^{-1}$ étaient formés à pH 6.8 dans l'eau ou dans 100 mmol$\cdot$L$^{-1}$ NaCl ou 10 mmol$\cdot$L$^{-1}$ CaCl$_2$. Les propriétés physiques des gels ainsi que les réactions d'agrégation des protéines (disparition des protéines natives, formation de dimères covalents de $\beta$-Lg et nature des liaisons entre protéines agrégées) ont été étudiées. Le NaCl et le CaCl$_2$ augmentent la force des gels et diminuent les temps de gel (tg). Au tg, sans ajout de sels, les agrégats formés, de petites tailles, impliquent la totalité des protéines présentes en solution. En revanche, en présence de NaCl ou de CaCl$_2$, seule une partie des protéines est impliquée dans la formation des agrégats au tg. La taille des agrégats formés est plus élevée en présence de CaCl$_2$. Dans toutes les conditions, les ponts disulfures interprotéiques semblent être les liaisons majoritairement impliquées dans la formation des agrégats au tg.</p>
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