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Journal of Dairy Science Vol. 80 No. 10 2270-2281
© 1997 by American Dairy Science Association ®
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Characterization by Ionization Mass Spectrometry of Lactosyl ß-Lactoglobulin Conjugates Formed During Heat Treatment of Milk and Whey and Identification of One Lactose-Binding Site

J. Leonil 1, D. Molle 1, J. Fauquant 1, J. L. Maubois 1, R. J. Pearce 2, and S. Bouhallab 1

1 Institut National de la Recherche Agronomique, Laboratoire de Recherches de Technologie Laitière, 65 rue de Saint Brieuc, 35042 Rennes, France
2 CSIRO Division of Food Science and Technology, Melbourne, Australia

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 ß-lactoglobulin (ß-LG) was observed that differed from that of the native form by 324. This specific modification of ß-LG occurred in acidified whey as well as in sweet whey and increased with the extent of the heat treatment. Incubation of purified ß-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 ß-LG; ß-casein, used as a control, showed no mass modification. Studies of kinetics showed that a maximum of 35% of the ß-LG was lactosyl-ß-LG conjugate after heat treatment at 70°C for 1 h. This study provides the first direct evidence of specific lactosylation of ß-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 ß-LG (f 46–51) showed the rearrangement reactions occurring during the fragmentation process by electrospray. A mechanism is proposed.

Key Words: mass spectrometry • ßbeta;-lactoglobulin • lactose • binding site

Submitted on July 29, 1996
Accepted on April 16, 1997




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