Ageritin from poplar mushrooms: scale-up purification and cytotoxicity towards undifferentiated and differentiated SH-SY5Y cells.

Ageritin is the first reported ribotoxin-like protein from basidiomycetes fungi. It can induce ribosomal integrity damage and translation block, and interferes with mitochondrial redox activity of some glioma and neuroblastoma cell lines. Herein, Ageritin has been investigated as a valuable neurotoxin towards either undifferentiated or retinoic acid (RA)-differentiated SH-SY5Y neuroblastoma cells showing a selective cell toxicity against undifferentiated cells. MTT and sulforhodamine B (SRB) assays highlighted that Ageritin markedly decreases the mitochondrial redox activity and viability of undifferentiated cells, meanwhile inducing evident morphological changes eliciting neuronal-like appearance in these cells. Data from lactate dehydrogenase release assay, cytofluorimetric analysis and caspase-3 enzymatic activity measurement suggest that Ageritin promotes cell death through a caspase-dependent apoptotic pathway. The Z-VAD-FMK caspase inhibitor was able to prevent this apoptotic pathway activation. Based on the interesting behaviour of Ageritin vs. SH-SY5Y cells, the development of a scale-up procedure to obtain the purified protein in larger amounts (yield 2.5 mg per 100 g) has been optimized.

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.

Valle Agricola lentil, an unknown lentil (Lens culinaris Medik.) seed from Southern Italy as a novel antioxidant and prebiotic source.

In order to promote 'Valle Agricola' lentil, an autochthonous lentil of the Campania Region, a thorough investigation of its biochemical and nutritional properties has been carried out. The macronutrient content (proteins, carbohydrates and lipids), free and total amino acids, and unsaturated fatty acids were determined. The antioxidant capability of raw 'Valle Agricola' lentils, as well as of boiled ones, was estimated in terms of their total phenol content (TPC), ORAC value, and free radical scavenging capacities using DPPH and ABTS assays. The data obtained evidenced that the boiling process slightly decreased Valle Agricola lentil's antioxidant power. Furthermore, when trypsin and chymotrypsin inhibitory activities were measured, a large decrease of the levels of anti-nutritional factors was estimated. In order to have a phytochemical overview of this autochthonous lentil seed, LC-ESI-MS/MS analysis was applied to raw and boiled lentil extracts. Flavonol glycosides and free flavanols, as well as typical seed prebiotic saccharides, were the most representative constituents.

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.