Parmigiano–Reggiano (PR) is a worldwide known Italian, long ripened, hard cheese. Its inclusion in the list of cheeses bearing the protected designation of origin (PDO, EU regulation 510/2006) poses restrictions to its geographic area of production and its technological characteristics. To innovate the Parmigiano–Reggiano (PR) cheese manufacturing chain from the health and nutritional point of view, the output of defatted PR is addressed. Two defatting procedures (Soxhlet, and supercritical CO₂ extraction) were tested, and the obtained products were compared in the composition of their nitrogen fraction, responsible for their nutritional, organoleptic, and bioactive functions. Free amino acids were quantified, and other nitrogen compounds (peptides, proteins, and non-proteolytic aminoacyl derivatives) were identified in the extracts and the mixtures obtained after simulated gastrointestinal digestion. Moreover, antioxidant and angiotensin converting enzyme (ACE) inhibition capacities of the digests were tested. Results obtained from the molecular and biofunctional characterization of the nitrogen fraction, show that both the defatted products keep the same nutritional properties of the whole cheese.

Non-specific lipid transfer proteins (nsLTP) were shown to be among the most significant allergens, in particular in several fruits belonging to the Rosaceae family. The molecular features of LTPs, such as the presence of eight cysteine residues forming four disulfide bridges, confer a compact structure, decreasing the probability of degradation due to cooking or digestion, thereby increasing the chance of systemic absorption and severe allergic reactions. Few studies on LTP-induced allergies regarding almond (Prunus dulcis L) are available in the literature. In the present work, we describe for the first time the extraction and purification of an almond LTP, achieving its full characterisation by using liquid chromatography and exact mass spectrometry; the full sequence was identified by means of LC-ESI-Orbitrap-MS applying a bottom-up approach. The characterised protein consists of 92 amino acids and has a calculated exact MW of 9579.0. The presence of four disulfide bridges was confirmed after reduction, as shown by a mass increment of 8 Da. Finally, its potential allergenicity was confirmed via an in silico approach. The results presented here demonstrate the enormous potential of advanced MS techniques for obtaining high-quality structural and functional data of allergenic proteins in a short time.

R,S-(±)-Dimethyl(1-methyl-2-oxo-2-phenylethyl)sulphonium bromide (3a), obtained from 1-phenylpropanone by bromination with t-buty bromide–dimethyl sulphoxide and further reaction with dimethyl sulphide, undergoes spontaneous resolution of its two enantiomers upon crystallization, as demonstrated by a single crystal X-ray analysis and assignment of absolute configuration (R).

A current hot topic in the field of environmental protection and development of valuable new products is represented by the recovery of food waste from the meat sector. The present study focused on the recovery of bovine hides by means of a sustainable method. Enzymatic hydrolysis was selected as a potential green methodology for use in the production of protein hydrolysates to be applied on an industrial scale. For this purpose, the enzymatic hydrolysis of bovine hides with Alcalase was investigated following a multiscale approach: lab-scale, medium-scale and semi-industrial pilot plant. Alcalase proved to be highly efficient due to its ability to degrade collagen, the main protein of hides. Under optimized conditions, the hydrolysis of hides at laband medium-scales resulted in approx. 85% protein solubilisation after 6 hours, with a consistent release of free amino acids and a degree of hydrolysis of 17-19%. However, in the pilot plant, solubilisation decreased due to difficulties in mixing bovine hides in the reactor, which was compensated with a longer reaction time to achieve virtually total protein solubilisation (∼98%). The present data therefore demonstrate the applicability of the process at semi-industrial scale in protein recovery with a reduced amount of waste by-products.

The reasons behind the increasing prevalence of celiac disease (CD) worldwide are still not fully understood. This study adopted a multilevel approach (in vitro, ex vivo, in vivo) to assess the potential of gluten from different wheat varieties in triggering CD. Peptides triggering CD were identified and quantified in mixtures generated from simulated gastrointestinal digestion of wheat varieties (n = 82). Multivariate statistics enabled the discrimination of varieties generating low impact on CD (e.g., Saragolla) and high impact (e.g., Cappelli). Enrolled subjects (n = 46) were: 19 healthy subjects included in the control group; 27 celiac patients enrolled for the in vivo phase. Celiacs were divided into a gluten-free diet group (CD-GFD), and a GFD with Saragolla-based pasta group (CD-Sar). The diet was followed for 3 months. Data were compared between CD-Sar and CD-GFD before and after the experimental diet, demonstrating a limited ability of Saragolla to trigger immunity, although not comparable to a GFD. Ex vivo studies showed that Saragolla and Cappelli activated immune responses, although with great variability among patients. The diverse potential of durum wheat varieties in triggering CD immune response was demonstrated. Saragolla is not indicated for celiacs, yet it has a limited potential to trigger adverse immune response.