Raw Peptide sequences

White lupin (Lupinus albus) is a food source with high protein content and is an important alternative for increasing its use as a functional food in improving health and sustainable nutrition. The aim of this study is to investigate the effects of different cooking methods on allergenic proteins and to evaluate the bioaccessibility of proteins by applying different cooking methods to local lupin seeds grown in our country. Different cooking techniques (boiling, microwave, fermentation, enzyme treatment) were applied to local white lupin seeds. Samples were subjected to proteolytic treatment using in vitro gastrointestinal system procedure and standard proteases. LC-MS/MS (Liquid Chromatography-Mass Spectrometry) was used and in silico analyses were performed to reach the peptide sequences of the proteins. Enzymatic and fermentation processes generated more peptides and allergenic matches after in vitro digestion compared to boiling and microwave treatments. No peptide was detected in only one cooking method. These findings indicate that enzyme and fermentation processes may play a decisive role in the emergence of some unique peptides in both samples. The observation of more matches in the samples subjected to the in vitro gastrointestinal system model in the AllergenOnline match and the fewer matches in the AllerTOP match suggest that these models processed the digestion process give results closer to allergenic peptides that may occur in real biological environments. This study reveal the allergenic potential changes of lupin proteins depending on the processing methods and provides the basis for functional food development studies. This dataset contains the peptide sequences and LC-MS/MS analysis data supporting the research article titled Impact of Thermal and Biotechnological Processing on the Bioaccessibility and Allergenic Peptide Profile of White Lupin (Lupinus albus).