There is currently considerable interest on the use of animal, plant, and fungal sources in the production of bioactive peptides, as evidenced by the substantial body of research on the topic. Such sources provide cheap and environmentally friendly material as it often includes waste and by-products. Enzymatic hydrolysis is considered an efficient method of obtaining peptides capable of antioxidant activity. Those properties have been proven in terms of radical-scavenging capacity using the DPPH (1,1-diphenyl-2-picrylhydrazyl) and ABTS (2,2-azinobis-(3-ethyl-benzothiazoline-6-sulphonic acid)), hydroxyl and superoxide radical methods. Additionally, the reducing power, ferrous ion-chelating (FIC), ferric reducing antioxidant power (FRAP), and the ability of the protein hydrolysates to inhibit lipid peroxidation have also been explored. The results collected in this review clearly indicate that the substrate properties, as well as the conditions under which the hydrolysis reaction is carried out, affect the final antioxidant potential of the obtained peptides. This is mainly due to the structural properties of the obtained compounds such as size or amino acid sequences.

A significant increase in interest in food-derived peptides obtained mostly through enzymatic reactions has been observed in the past few years. One of the best sources of bioactive peptides are defatted egg yolk proteins, which can potentially find application as high-quality nutritional supplements for infants with cow’s milk protein intolerance and as natural preservatives. The aim of this study was to obtain peptides from defatted egg yolk protein, to study their antioxidant and antimicrobial properties, and to identify peptides with bioactive properties To control the course of the process, MALDI-TOF/MS (matrix-assisted laser desorption/ionization time-of flight/mass spectrometry) spectra were also examined. The peptide mixture obtained through enzyme digestion was tested for its antioxidant properties by measuring the scavenging activity in 2,2-diphenyl-1-picrylhydrazyl radical (DPPH•), 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) radical cation decolorization (ABTS•+), and ferric reducing activity (FRAP) assays. Antimicrobial activity was also studied. The peptide mixture exhibited significant antioxidant activity: DPPH—1776.66 ± 32.99, ABTS—390.43 ± 8.92, and FRAP—16.45 ± 0.19. The inhibition of bacterial growth by two concentrations of the peptide mixture was examined. The best result was obtained in Bacillus cereus, with an inhibition zone of 20.0 ± 1.0 and 10.7 ± 0.6 mm at the concentrations of 50 and 25 mg/mL, respectively. The results of the study suggest that the mixture of egg yolk peptides may exhibit a number of health-promoting properties.

Oilseed-derived proteins have emerged as an excellent alternative to animal sources for the production of bioactive peptides. The bioactivities exhibited by peptides derived from plant proteins encompass a wide range of health-promoting and disease-preventing effects. Peptides demonstrate potential capabilities in managing diseases associated with free radicals and regulating blood pressure. They can also exhibit properties that lower blood sugar levels and modify immune responses. In addition to their bioactivities, plant-derived bioactive peptides also possess various functional properties that contribute to their versatility. An illustration of this potential can be the ability of peptides to significantly improve food preservation and reduce lipid content. Consequently, plant-derived bioactive peptides hold great promise as ingredients to develop functional products. This comprehensive review aims to provide an overview of the research progress made in the elucidation of the biological activities and functional properties of oilseed-derived proteins. The ultimate objective is to enhance the understanding of plant-derived bioactive peptides and provide valuable insights for further research and use in the food and medicine industries.

Rapeseed meal, a byproduct of oil extraction, is increasingly recognised as a valuable source of plant protein and health-promoting peptides. This study aimed to identify key proteins in cold-pressed rapeseed meal and assess their potential to release bioactive peptides through in silico hydrolysis using plant-derived proteases, namely papain, bromelain, and ficin. Proteomic profiling via two-dimensional electrophoresis and MALDI-TOF/TOF mass spectrometry revealed cruciferin as the dominant protein, along with other metabolic and defence-related proteins. In silico digestion of these sequences using the BIOPEP database generated thousands of peptide fragments, of which over 50% were predicted to exhibit bioactivities, including ACE and DPP-IV inhibition, as well as antioxidant, neuroprotective, and anticancer effects. Among the evaluated enzymes, bromelain exhibited the highest efficacy, yielding the greatest quantity and diversity of bioactive peptides. Notably, peptides with antihypertensive and antidiabetic properties were consistently identified across all of the protein and enzyme variants. Although certain rare functions, such as anticancer and antibacterial activities, were observed only in specific hydrolysates, their presence underscores the broader functional potential of peptides derived from rapeseed. These findings highlight the potential of rapeseed meal as a sustainable source of functional ingredients while emphasising the necessity for experimental validation to confirm the predicted bioactivities.