Urtica dioica (Stinging Nettle): A Neglected Plant With Emerging Growth Promoter/Immunostimulant Properties for Farmed Fish.

Urtica dioica (stinging nettle), is a perennial plant belonging to the family of Urticaceae, genus Urtica. Despite the use of nettle in folk veterinary medicine is well documented, U. dioica is today an underestimated and frequently neglected plant, considered by the contemporary agriculture as a weed to be eliminated. This mini review focus on very recent studies on dietary administration of U. dioica, both as a single herb or in combination with other herbs, to enhance growth and stimulate farmed fish immunity, thus enabling the fish to be more resistant against bacterial infections. Such an emerging feature, together with cost-effectiveness, adequate availability, and easy processing of nettle, could make this herb an excellent, inexpensive and widely used dietary supplement on intensive fish farms.

Nutritional values and metabolic profile with and without boiled treatment of 'Gallo Matese' beans (Phaseolus vulgaris L.), a landrace from Southern Italy.

BACKGROUND: 'Gallo Matese' beans are known as a typical legume of Southern Italy and continue to be consumed as a traditional food preserving the diversity of this region. Nonetheless, no information about the nutritional values of this legume is available. The objective of the present investigation was to determine the nutritional value and metabolic profile of 'Gallo Matese' beans. Results. 'Gallo Matese' beans contain high levels of proteins (22.64 g/100 g) and essential amino acids  (8.3 g/100 g). Furthermore, differentunsaturated fatty acidscontributetothetotalamountoflipids (0.97 g/100 g); among them, the essential PUFA α-linolenic (0.48 g/100 g) and linoleic (0.39 g/100 g) acids are the most abundant. The total phenol content was revealed and ABTS and ORAC-fluorescein methods were applied to determine the radical scavenging capabilities of the extract with and without boiled treatment. Finally, a de- crease in trypsin and chymotrypsin inhibitory activities was estimated before and after the boiling procedure. Conclusion. The data obtained show that 'Gallo Matese' beans are a functional food with healthy qualities. Overall, these results are useful to promote their cultivation and consumption, thus preserving Italian beans biodiversity due to consumer interest in choosing a healthy diet, such as the Mediterran. METHODS: nd. 'Gallo Matese' beans are known as a typical legume of Southern Italy and continue to be consumed as a traditional food preserving the diversity of this region. Nonetheless, no information about the nutritional values of this legume is available. The objective of the present investigation was to determine the nutritional value and metabolic profile of 'Gallo Matese' beans. RESULTS: 'Gallo Matese' beans contain high levels of proteins (22.64 g/100 g) and essential amino acids  (8.3 g/100 g). Furthermore, differentunsaturated fatty acidscontributetothetotalamountoflipids (0.97 g/100 g); among them, the essential PUFA α-linolenic (0.48 g/100 g) and linoleic (0.39 g/100 g) acids are the most abundant. The total phenol content was revealed and ABTS and ORAC-fluorescein methods were applied to determine the radical scavenging capabilities of the extract with and without boiled treatment. Finally, a de- crease in trypsin and chymotrypsin inhibitory activities was estimated before and after the boiling procedure. CONCLUSIONS: The data obtained show that 'Gallo Matese' beans are a functional food with healthy qualities. Overall, these results are useful to promote their cultivation and consumption, thus preserving Italian beans biodiversity due to consumer interest in choosing a healthy diet, such as the Mediterranean diet.

Purification and characterization of novel cationic peroxidases from Asparagus acutifolius L. with biotechnological applications.

Four novel basic peroxidases, named AaP-1, AaP-2, AaP-3, and AaP-4, were purified from Asparagus acutifolius L. seeds by cation-exchange and gel filtration chromatographies. The four proteins showed a similar electrophoretic mobility of 46 kDa while, by MALDI-TOF MS, different Mr values of 42758.3, 41586.9, 42796.3, and 41595.5 were determined for AaP-1, AaP-2, AaP-3, and AaP-4, respectively. N-terminal sequences of AaPs 1-4 up to residue 20 showed a high percentage of identity with the peroxidase from Glycine max. In addition, AaP-1, AaP-2, AaP-3, and AaP-4 were found to be glycoproteins, containing 21.75, 22.27, 25.62, and 18.31 % of carbohydrates, respectively. Peptide mapping and MALDI-TOF MS analysis of AaPs 1-4 showed that the structural differences between AaP-1 and AaP-2 and AaP-3 and AaPs-4 were mainly due to their glycan content. We also demonstrate that AaPs were able to remove phenolic compounds from olive oil mill wastewaters with a higher catalytic efficiency with respect to horseradish peroxidase, thus representing candidate enzymes for potential biotechnological applications in the environmental field.