Results of physicochemical properties of modified lysozyme with pepsin and trypsin

The data set contains the results of studies on an attempt to obtain bioactive peptide fractions from lysozyme derived from hen egg by enzymatic hydrolysis. The data file contains the results of enzymatic modification of lysozyme carried out in two successive stages. 1. Stage one – hydrolytic modification of lysozyme using pepsin and trypsin. For modification, a 5% aqueous solution of lysozyme at pH 2 was prepared containing a mixture of trypsin and pepsin in the ratios of 1/0, 0.75/0.25, 0.5/0.5, 0.25/0.5, 0/1, respectively. The hydrolysis reactions were carried out in the ratio of lysozyme to the enzyme mixture of 500/1. The reference sample was a lysozyme solution without added enzymes. Samples containing pepsin and trypsin and the reference sample were modified in the analytical reactor BUCHI Syncore® (Switzerland) at 55 °C for 60 minutes, then the reaction was stopped by heating them for 5 minutes at 85 °C and then, after cooling, their pH value was set at 7.0. The second stage - consisted in assessing the effect of peptides and oligomers formed as a result of lysozyme modification on physicochemical properties. For this purpose, for the most advantageous in the first variant of the experiment in the formation of the peptide and oligomeric fraction of the enzyme, i.e. pepsin, subsequent modifications of lysozyme were carried out, this time in the ratio of lysozyme to pepsin: 1/2000, 1/1500, 1/750, 1/500, 1/250, 1/166, 1/125, 1/100. The obtained preparations were frozen and then lyophilized in Labconco-freezedryer (USA). The preparations prepared in this way were subjected to analytical tests, i.e. hydrolytic and antioxidant activity, hydrophobicity, percentage of oligomeric and peptide fractions, molecular weights of the obtained individual peptide fractions and the level of immunoreactivity. The obtained fractions were also visualized using densitometric analysis.