Effect of water activity, temperature and pH on solid state lactosylation of β-lactoglobulin

Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration

“…The minor peaks found on both sides of the main peak were also seen by Toro-Sierra et al (2013) and Cheison et al (2012) who purified α-La from whey protein isolates. Heat treatment during milk and whey processing promote protein lactosylation causing the molecule to be more hydrophilic and elute earlier in RP-HPLC (Thomsen et al 2012;Lund et al 2005). Accordingly, the small peaks before the main peak for α-La are expected to contain mono-lactosylated α-La.…”

Comparative study on the effects of nystose and fructofuranosyl nystose in the glycation reaction on the antigenicity and conformation of β-lactoglobulin

“…(Jimenez-Castano, Villamiel, Martin-Alvarez, Olano, & Lopez-Fandino, 2005;Thomsen et al, 2012). Furthermore, the nature of the saccharides used for glycation showed profound influence on the structural changes of b-LG.…”

Dissociation and reduction of covalent β-lactoglobulin–quinone adducts by dithiothreitol, tris(2-carboxyethyl)phosphine, or sodium sulfite

“…The formation of such covalent adducts 28 between b-lactoglobulin (b-LG) and the quinone of 4-methylcatechol, 4-methylbenzoquinone (4MBQ), 29 and subsequent reduction by dithiothreitol (DTT), tris(2-carboxyethyl)phosphine (TCEP), or sodium sul- 30 fite was investigated by mass spectrometry. The results showed that 19.0 ± 8.8% of b-LG reacted with 31 4MBQ when present in equimolar ratio at 20°C (pH 8.0) to yield the protein-phenol adduct (b-LG-Q).…”