Access to health care, nutrition and dietary habits among school-age children living in socio-economic inequality contexts: results from the "ForGood: Sport is Well-Being" programme.

Social frailty is a warring phenomenon in Europe, negatively impacting children's health and nutrition. We present the results of a social programme facilitating access to physical activities for vulnerable children in Italy. 311 school-age children enrolled in the programme between 2015 and 2017 were assessed for health and lifestyle, anthropometric and nutritional status. Data were compared by origin (Italians vs. immigrants) and then immigrants were split into sub-groups: first- and second-generation. Poor socio-economic status exposed children to a lack of access to health services, and drove imbalanced eating behaviour. 20.8% of children were not registered with the National Health Services (immigrants p < .0001); 22% were not fully vaccinated (no differences between groups). A double burden of malnutrition coexisted: overweight was higher for Italians, underweight and poor linear growth for immigrants. Nearly 40% of children had a poor Mediterranean Diet adequacy (KIDMED index). Our findings show that when social programmes, besides their main scope of inclusion and integration, holistically approach their beneficiaries, they can play an important role in monitoring lifestyle conditions and facilitating access to primary health care.

Expression and purification of the recombinant mustard trypsin inhibitor 2 (MTI2) in Escherichia coli.

The mustard trypsin inhibitor 2, MTI2, was expressed in Escherichia coli. A specific procedure for its production and purification is described. The recombinant protein was recovered by protein extraction from the insoluble fraction, then renatured and purified by ion exchange and gel filtration chromatography. Finally, the inhibitory activity against trypsin was also determined.

Use of reverse micelles for the simultaneous extraction of oil, proteins, and glucosinolates from cruciferous oilseeds.

Cruciferous oilseeds are important sources of oil, proteins, and glucosinolates (GLs), potentially available when biorefinery processes are used. The proposed extraction technology is based on the use of reverse micelles (RMs) made with cetyltrimethylammonium bromide (CTAB) dispersed in organic solvent. The physicochemical properties of this extraction system and the good water solubility of many high value compounds, such as GLs and some proteins, permit the simultaneous extraction of oil, and these products from cruciferous oilseed meals. This procedure is based on three main steps: (i) seed conditioning; (ii) solid-liquid extraction by RM solution; and (iii) back-transfer of the RM solution for recovery of the extracted compounds. The method makes it possible to simultaneously extract almost the same amount of oil as with pure organic solvents used in the current extraction plants and more than 90% of soluble proteins and GLs. It is a promising biorefinery technology alternative to traditional oil extraction processes.

Benzodioxole derivatives as negative effectors of plant proteases.

Previous work demonstrated that a commercial formulation of piperonyl butoxide (PBO) did inhibit the activity of some plant proteolytic enzymes. In this paper, the effect of pure PBO and nine pure PBO homologues (PBOH) appropriately synthesized toward bromelain and papain was studied in hydrocarbon solution using the bis(2-ethylhexyl)sodium sulfosuccinate (AOT) reverse micellar system. This study establishes that the majority of these compounds show, in vitro, interesting protease inhibition activities. The benzodioxole and dihydrobenzofuran structures, in particular, 5-[2-(2-butoxyethoxy)ethoxymethyl]-benzo[1,3]dioxole (EN 1-40) and 6-[2-(2-butoxyethoxy)ethoxymethyl]-5-propyl-2,3-dihydrobenzofuran (EN 16-5), respectively, appear to be responsible for protease inhibition. Measures of octanol/water partition coefficients on PBO and PBOH have demonstrated that water solubility plays a fundamental role in the expression of protease inhibition activity.

Isolation and biochemical characterization of a basic myrosinase from ripe Crambe abyssinica seeds, highly specific for epi-progoitrin.

On the basis of previous studies on the mechanism-based inhibition, activation, and active site structure of myrosinase(s) isolated from Sinapis alba and other cruciferous seeds, crambe myrosinase shows uncommon properties and behavior. For this reason homogeneous crambe myrosinase was isolated and investigated to establish the most important physicochemical features, including kinetic properties determined with the epimers progoitrin (R) and epi-progoitrin (S) as substrates, with and without ascorbate as an activator. The results of this study demonstrate that crambe myrosinase is highly specific for epi-progoitrin due to a better stabilization of the enzyme-substrate complex. This stabilization is caused by additional hydrogen bonding that only epi-progoitrin can set up between its hydroxyl group and a suitable residue in the hydrophobic pocket where the "docking" of the glucosinolates side chain takes place.