Seaweeds are an excellent source of bioactive compounds, and therefore the use of sustainable and food compatible extraction methods such as enzyme-assisted (EAE) and ultrasound-assisted extraction were applied on Sargassum muticum, Osmundea pinnatifida, and Codium tomentosum. Extracts were evaluated for proximate characterization and biological properties. Higher extraction yields were observed for C. tomentosum EAE (48-62%; p < 0.05 for Cellulase and Viscozyme), followed by O. pinnatifida (49-55%; p < 0.05 except Alcalase) and S. muticum (26-31%; p < 0.05). S. muticum extracts presented the highest nitrogen (25 ± 2 mg/glyoph extract) and total phenolics (261 ± 37 μgcatechol equiv/glyoph extract) contents, whereas higher sugars (78 ± 14 mgglucose equiv/glyoph extract) including sulfated polysaccharide (44 ± 8 mgNa2SO4 acid/glyoph extract) contents characterized O. pinnatifida extracts. A higher effect on hydroxyl-radical scavenging activity (35-50%) was observed for all extracts, whereas S. muticum Alcalase and C. tomentosum Cellulase extracts exhibited higher prebiotic activity than fructooligosaccharides. O. pinnatifida and C. tomentosum EAE showed inhibitory potential against α-glucosidase (38-49%).

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a b s t r a c tWhey protein concentrate (WPC) was subjected to enzymatic hydrolysis by proteases from the flowers of Cynara cardunculus, and the resulting angiotensin-converting enzyme (ACE)-inhibitory effect was monitored. The whole WPC hydrolysate exhibited an IC 50 value of 52.9 ± 2.9 g/mL, whereas the associated peptide fraction with molecular weight below 3 kDa scored 23.6 ± 1.1 g/mL. The latter fraction was submitted to RP-HPLC, and 6 fractions were resolved that exhibited ACE-inhibitory effects. Among the various peptides found, a total of 14 were identified via sequencing with an ion-trap mass spectrometer. Eleven of these peptides were synthesized de novo -to validate their ACE-inhibitory effect, and also to ascertain their stability when exposed to simulated gastrointestinal digestion. Among them, three novel, highly potent peptides were found, corresponding to ␣-lactalbumin f(16-26) -with the sequence KGYGGVSLPEW, ␣-lactalbumin f(97-104) with DKVGINYW, and ␤-lactoglobulin f(33-42) with DAQS-APLRVY; their IC 50 values were as low as 0.80 ± 0.1, 25.2 ± 1.0 and 13.0 ± 1.0 g/mL, respectively. None of them remained stable in the presence of gastrointestinal enzymes: they were partially, or even totally hydrolyzed to smaller peptides -yet the observed ACE-inhibitory effects were not severely affected for two of those peptides.

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Lactoferrin has for long captured the interest of many researchers as a natural compound with a wide variety of uses. Lactoferrin is a monomeric, iron-binding 80 kDa glycoprotein, and appears to be the subfraction of whey with the best documented antiviral, antimicrobial, anticancer and immune modulating/enhancing effects. It belongs to the family of transferrin proteins, and serves to control iron levels in body fluids by sequestering and solubilizing ferric iron. In the present research effort, production of lactoferrin derivatives (starting from a purified commercial extract), encompassing full stabilization of its three-dimensional structure, has been attempted via nanoencapsulation within lipid nanovesicles, integrating a multiple water-in-oil-in-water emulsion. Long-term storage of the multiple nanoemulsions produced did not lead to leaching of protein, thus proving the effectiveness of the encapsulation procedure. Furthermore, lactoferrin nanovesicle derivatives prepared under optimal conditions were successfully employed at lab-scale antimicrobial trials.