Characterization by ionization mass spectrometry of lactosyl β-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site
Identifieur interne : 006780 ( PascalFrancis/Checkpoint ); précédent : 006779; suivant : 006781Characterization by ionization mass spectrometry of lactosyl β-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site
Auteurs : J. Leonil [France] ; D. Molle [France] ; J. Fauquant [France] ; J. L. Maubois [France] ; R. J. Pearce [Australie] ; S. Bouhallab [France]Source :
- Journal of dairy science [ 0022-0302 ] ; 1997.
Descripteurs français
- Pascal (Inist)
- Wicri :
English descriptors
- KwdEn :
Abstract
The extent of the early stage of the Maillard-type reaction that impaired functional properties of whey proteins was evaluated by electrospray ionization mass spectrometry. Under conditions of mild heat treatment (63°C for 20 s) applied to milk before whey separation at room temperature 23°C ), a modification of the relative molecular mass of β-lactoglobulin ( β-LG) was observed that differed from that of the native form by 324. This specific modification of β-LG occurred in acidified whey as well as in sweet whey and increased with the extent of the heat treatment. Incubation of purified β-LG dissolved in milk ultrafiltration permeate or in lactose solution at 50 to 80°C demonstrated the presence of a lactosyl residue that was covalently bound to β-LG; β-casein, used as a control, showed no mass modification. Studies of kinetics showed that a maximum of 35% of the β-LG was lactosyl-β-LG conjugate after heat treatment at 70°C for 1 h. This study provides the first direct evidence of specific lactosylation of β-LG during the initial stage of the Maillard reaction. One of the first lactose-binding sites was identified as a Lys47 by protease mapping and analysis by means of on-line liquid chromatography combined with mass spectrometry. In addition, collision-activated dissociation performed on the lactosylated peptide β-LG (f 46-51) showed the rearrangement reactions occurring during the fragmentation process by electrospray. A mechanism is proposed.
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Pascal:98-0026219Le document en format XML
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<term>Lactose</term>
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<term>Lactoglobuline</term>
<term>Composé conjugué</term>
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<front><div type="abstract" xml:lang="en">The extent of the early stage of the Maillard-type reaction that impaired functional properties of whey proteins was evaluated by electrospray ionization mass spectrometry. Under conditions of mild heat treatment (63°C for 20 s) applied to milk before whey separation at room temperature 23°C ), a modification of the relative molecular mass of β-lactoglobulin ( β-LG) was observed that differed from that of the native form by 324. This specific modification of β-LG occurred in acidified whey as well as in sweet whey and increased with the extent of the heat treatment. Incubation of purified β-LG dissolved in milk ultrafiltration permeate or in lactose solution at 50 to 80°C demonstrated the presence of a lactosyl residue that was covalently bound to β-LG; β-casein, used as a control, showed no mass modification. Studies of kinetics showed that a maximum of 35% of the β-LG was lactosyl-β-LG conjugate after heat treatment at 70°C for 1 h. This study provides the first direct evidence of specific lactosylation of β-LG during the initial stage of the Maillard reaction. One of the first lactose-binding sites was identified as a Lys<sup>47</sup>
by protease mapping and analysis by means of on-line liquid chromatography combined with mass spectrometry. In addition, collision-activated dissociation performed on the lactosylated peptide β-LG (f 46-51) showed the rearrangement reactions occurring during the fragmentation process by electrospray. A mechanism is proposed.</div>
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</fC03>
<fC03 i1="11" i2="X" l="SPA"><s0>Mecanismo reacción</s0>
<s5>53</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Protéine lactosérum</s0>
<s5>32</s5>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Whey protein</s0>
<s5>32</s5>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Proteína lactosero</s0>
<s5>32</s5>
</fC07>
<fN21><s1>012</s1>
</fN21>
</pA>
</standard>
</inist>
<affiliations><list><country><li>Australie</li>
<li>France</li>
</country>
<region><li>Région Bretagne</li>
<li>Victoria (État)</li>
</region>
<settlement><li>Melbourne</li>
<li>Rennes</li>
</settlement>
</list>
<tree><country name="France"><region name="Région Bretagne"><name sortKey="Leonil, J" sort="Leonil, J" uniqKey="Leonil J" first="J." last="Leonil">J. Leonil</name>
</region>
<name sortKey="Bouhallab, S" sort="Bouhallab, S" uniqKey="Bouhallab S" first="S." last="Bouhallab">S. Bouhallab</name>
<name sortKey="Fauquant, J" sort="Fauquant, J" uniqKey="Fauquant J" first="J." last="Fauquant">J. Fauquant</name>
<name sortKey="Maubois, J L" sort="Maubois, J L" uniqKey="Maubois J" first="J. L." last="Maubois">J. L. Maubois</name>
<name sortKey="Molle, D" sort="Molle, D" uniqKey="Molle D" first="D." last="Molle">D. Molle</name>
</country>
<country name="Australie"><region name="Victoria (État)"><name sortKey="Pearce, R J" sort="Pearce, R J" uniqKey="Pearce R" first="R. J." last="Pearce">R. J. Pearce</name>
</region>
</country>
</tree>
</affiliations>
</record>
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