Lentil Protein and Tannic Acid Interaction Limits <i>in Vitro</i> Peptic Hydrolysis and Alters Peptidomic Profiles of the Proteins
Ruth T. Boachie, Ogadimma D. Okagu, Raliat O. Abioye, Nico Hüttmann, Teresa Oliviero, Edoardo Capuano, Vincenzo Fogliano, Chibuike C. Udenigwe
Abstract
pepsin digestion were investigated. LPTA mixtures containing 1% w/v LP and 0.001-0.5% TA were prepared and characterized in terms of particle size, thermal properties, and secondary and tertiary structures. A 20-fold increase in particle size was observed in LPTA0.5% compared to LP control (without TA), indicating aggregation. Static quenching of tryptophan residues within the protein hydrophobic folds was observed. Increasing TA levels also enhanced protein thermal stability. Over 50% reduction in free amino groups of LPTA 0.5%, relative to LP, was observed after pepsin digestion. Cleavage specificity of pepsin and peptidomic profile of LP were modified by the presence of TA in LPTA 0.5%. This study showed that 0.5% w/v TA induced protein aggregation and reduced LP digestibility by hindering the accessibility of pepsin to the protein network, thus modifying the profile of released peptides.