Antioxidant capacity (AOC) against peroxyl radical and 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) radical cation was measured for a series of p-hydroxybenzoic (HB) and p-hydroxycinnamic (HC) acids at different pH. Quantum-chemical computation was performed using Gaussian 3.0 software package to calculate the geometry and energy parameters of the same compounds. Significant correlations were revealed between AOC and a number of calculated parameters. The most significant AOC descriptors for the studied compounds against peroxyl radical were found to be HOMO energy, rigidity (η) and Mulliken charge on the carbon atom in m-position to the phenolic hydroxyl. The most significant descriptor of the antioxidant properties against the ABTS radical cation at рН 7.40 is electron transfer enthalpy from the phenolate ion. The mechanism of AOC realization has been proposed for HB and HC acids against both radicals.

Quantum chemical methods allow screening and prediction of peptide antioxidant activity on the basis of known experimental data. It can be used to design the selective proteolysis of protein sources in order to obtain products with antioxidant activity. Molecular geometry and electronic descriptors of redox-active amino acids, as well as tyrosine and methionine-containing dipeptides, were studied by Density Functional Theory method. The calculated data was used to reveal several descriptors responsible for the antioxidant capacities of the model compounds based on their experimentally obtained antioxidant capacities against ABTS (2,2′-Azino-bis-(3-ethyl-benzothiazoline-6-sulfonate)) and peroxyl radical. A formula to predict antioxidant activity of peptides was proposed.

Bioinformatics was used to design a procedure for industrial enzymatic proteolysis of cheese whey. The specificity rules for commercial enzymes were applied to in silico proteolysis of cheese whey proteins. The pattern of antigens was considered, along with molecular descriptors of bitter taste, antioxidant capacity, and anti-hypertensive activity. The main objective was to obtain hydrolysates with reduced antigenicity and satisfactory sensory properties; an additional goal was to characterize their bioactivity profiles. Protamex/Alcalase mixtures were first used as multienzyme compositions to obtain non-bitter cheese whey hydrolysates. The multifactor optimization performed for degree of hydrolysis, free amino acid content, and residual antigenicity has revealed the optimal Protamex/Alcalase ratio of 3.5:0.5 and the optimal hydrolysis duration of 90 min. The hydrolysate obtained using Protamex/Alcalase 3.5:0.5 mixture had a double antioxidant capacity and a 15 times lower ACE-I inhibition concentration IC50 compared to cheese whey concentrate, and an 11 times lower β-LG residual antigenicity.