Affiliations: Dipto. di Scienza degli Alimenti, Univ. Napoli 'Federico II', Parco G., 80055 Portici, Naples, Italy
CRISCEB-Ctro. Ric. I., Seconda Univ. Napoli, Via C., 80138 Naples, Italy
References: Not available.
Identification of a β-lactoglobulin lactosylation site
Thermal treatment of milk leads to non-enzymatic glycosylation of proteins through Maillard reaction. Free NH2 groups of basic amino acids react with the reducing carbonyl group of lactose forming the so-called Amadori products. Electrospray mass spectrometry analysis shows that β-lactoglobulin (β-LG), the major whey protein, undergoes lactosylation under industrial thermal treatment. In order to investigate the specificity of reactive sites for lactose binding the analysis of trypsin hydrolysates of β-LG isolated from different industrial milks was performed. Results demonstrate that Lys-100 is a preferential lactosylation site of β-LG during industrial milk treatment. These results were confirmed by an analysis of the three-dimensional model of the protein which showed that Lys-100 had the highest solvent accessibility and proximity to another amino group making Lys-100 the best candidate to lactosylation. Lys-47, previously identified by other authors, showed a good proximity to another Lys residue, but an intermediate level of exposition to solvent. Copyright (C) 1998 Elsevier Science B.V.
Identification of a β-lactoglobulin lactosylation site
No results.
Identification of a β-lactoglobulin lactosylation site