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Proteins apart from their basic functions may be the precursors of peptides with opioid, antihypertensive, immunomodulating, dipeptidyl peptidase inhibitors, antiamnestic, antithrombotic and other activities. Biopeptides as components of food with desired features become an interesting issue for scientific research. The bioinformatic-aided analysis of the distribution of biologically active fragments and bonds, which are predicted to be susceptible to the action of endopeptidases of known specificity, hydropathy index and prediction of secondary structures has been carried out. The results indicated that wheat gliadins were the most susceptible for bioactive peptides release. These peptides showed antihypertensive, inhibitor of dipeptidyl peptidase opioid and antioxidative effect, and were released by chymotrypsin, elastase, ficin and pepsin. The bioactive fragments predicted to be released by proteolytic enzymes as well as surroundings of such fragments were hydrophilic. The most frequently occurring structure of bioactive peptides from plant proteins was random coil. These findings suggested that the distribution of bioactive fragments could favour their release by proteinases.
Abstract
The thermal analytical study of most hydrophobic and hydrophilic D/L amino acids reveals significant hydropathy index correlation between the presence of water and crystalline amino acids. The TG derivative mass profiles for arginine and lysine (hydrophilic acids) at various time intervals of atmospheric exposure, show two distinct peaks, one between 50 and 60°C (unbound water), and one close to 100°C (bound-like water). The DSC heat-cool profiles for lysine and arginine confirmed the presence of these multiple waters with two heats of vaporization. The absence of these patterns from the TG and DSC for cysteine and phenylalanine (hydrophobic acids) further supports the conclusions.
