ARTICLE pubs.acs.org/JAFC
Analysis of the Effect of Temperature Changes Combined with Different Alkaline pH on the β-Lactoglobulin Trypsin Hydrolysis Pattern Using MALDI-TOF-MS/MS Seronei Chelulei Cheison,*,‡,† Janina Brand,† Elena Leeb,† and Ulrich Kulozik§ †
Zentralinstitut f€ur Ern€ahrungs- und Lebensmittelforschung (ZIEL)-Junior Research Group: Bioactive Peptides and Protein Technology, Technische Universit€at M€unchen, Weihenstephaner Berg 1, D-85354 Freising, Germany ‡ School of Public Health and Community Development, Maseno University, Private Bag, Kisumu, Kenya § Chair for Food Process Engineering and Dairy Technology Department, ZIEL Technology Section, Technische Universit€at M€unchen, Weihenstephaner Berg 1, D-85354 Freising, Germany ABSTRACT: Temperature and pH influence the conformation of the whey protein β-lactoglobulin (β-Lg) monomer, dimer, and octamer formation, its denaturation, and solubility. Most hydrolyses have been reported at trypsin (EC 3.4.21.4) optimum conditions (pH 7.8 and 37 °C), while the hydrolysate mass spectrometry was largely limited to peptides with
