The present invention relates to a method for determining and quantifying β-casein derived proteose peptones and/or β-casein, said method comprising the steps of (i) providing a dairy-based product to be analysed; (ii) subjecting said product using liquid chromatography-mass spectrometry analysis; (iii) determining and/or quantifying said β-casein derived proteose peptones and/or β-casein in said product by detecting compounds of defined m/z values or deconvoluting the mass spectrometry spectra to calculate monoisotopic masses. The present invention also relates to nutritional compositions having a reduced content of β-casein derived proteose peptones and the uses hereof for e.g. treating, preventing and/or ameliorating abdominal pain in an infant.

A method for testing for the presence and quantification of A1-type beta-casein variants or A2-type beta-caseins, in milk and milk derived dairy products, using chymotrypsin digestion followed by LC-MS analysis to determining the concentrations of beta-casein digestion peptides and using the concentrations to calculate the amounts of A1-type beta-casein variants or A2-type beta-casein variants present.

The present invention broadly relates to the field of biotechnology. More particularly, the present invention relates to recombinant vector systems for the production of animal free milk proteins and a process for the production of the animal protein in recombinant host cells.

Methods and systems for detecting allergens using mass spectrometry are provided herein. In some aspects, a sample can be screened for the presence or quantity of ovalbumin, lysozyme, casein (isoform S1 and S2), lactoglobulin, high and low glutens, wheat, rye, oats, barley, mustard, sesame, and various types of nuts including macadamia, pistachio, brazil, walnuts, peanuts and hazelnuts by detecting one or more peptides specific to the allergen of interest using selected MRM transitions.