An efficient reduced simulation of residual stresses in composite forming processes

An efficient simulation of thermal and mechanical models involved in thermosetting composites forming needs to overcome some numerical difficulties related to: (i) the multi-scale behaviour; (ii) the complex geometries involved needing too many degrees of freedom; (iii) the large time intervals where the solution has to be computed; (iv) the non-linearity of the involved evolution equations; (v) the numerous couplings… In this work, an efficient strategy based on a separated representation is proposed. This method enables to avoid the use of an incremental strategy and can lead to impressive computing time savings especially when the model involves fine meshes and very small time steps. The local non-linear chemical kinetics and its coupling with the global heat balance equation are naturally introduced in the separated representation algorithm. Moreover, the dependence of the thermal conductivity and the specific heat on the temperature and on the reaction advancement degree are also taken into account. Knowing the history of the temperature field, the separated representation is again used to solve the thermo-mechanical problem in order to determine the residual stresses.     

Lactic acid bacteria from fermented table olives

Table olives are one of the main fermented vegetables in the world. Olives can be processed as treated or natural. Both have to be fermented but treated green olives have to undergo an alkaline treatment before they are placed in brine to start their fermentation. It has been generally established that lactic acid bacteria (LAB) are responsible for the fermentation of treated olives. However, LAB and yeasts compete for the fermentation of natural olives. Yeasts play a minor role in some cases, contributing to the flavour and aroma of table olives and in LAB development.     

From contact angle titration to chemical force microscopy: a new route to assess the pH-dependent character of the stratum corneum

Despite of its complex multicomponent organization and its compact architecture, the Stratum corneum (SC) is not completely impermeable to substances directly applied on the skin surface. A huge number of works have been dedicated to the understanding of the mechanisms involved in substance permeation by exploring deeper layers than the SC itself. Surprisingly, there is a poor interest in studies relating to interactions which may occur in the near-surface region (i.e. approximately 1 nm depth) of the SC. In this work, equilibrium proton-transfer reactions have been used as probes to define in a fundamental point of view the nature of the SC interactions with its environment. Such titration curves are investigated on 'in vitro' SC (isolated SC from abdominal skin tissue) and on 'in vivo' volar forearm (a sebum poor area). The results are discussed in term of work of adhesion and surface pKa values. Because SC can 'reconstruct' under heating, influence of the temperature on titration curves is investigated and the role of the different components is discussed. Different sigmoidal transitions were observed. Two common pKa values (pKa(1) = 4 and pKa(2) = 11.5) were clearly identified in both cases and associated to an acid-base character. By playing with the temperature of 'in vitro' SC, the 'accessibility' of polar functions was increased, thus refining the results by revealing an amphoteric character with an acid-to-base transition at pH 3.5 and two acid transitions at pH = 6.5 and pH = 11.5. Adhesion forces between an Atomic Force Microscopy (AFM) tip and a single isolated corneocyte through buffered liquid media were also investigated to better understand the role of the individual corneocytes.     

Are disulphide bonds formed during acid gelation of preheated milk?

The role of thiol/disulphide exchanges during acid gelation of preheated milk was studied with milk samples with or without N‐ethylmaleimide (NEM), a thiol‐blocking agent, and acidified to pH 4 by the addition of glucono‐delta‐lactone at 20 °C. Active or total thiol groups, particle size with light scattering measurements in a dissociating solvent or by SDS‐agarose electrophoresis were determined on acidified milk samples. Diffusing wave spectroscopy and rheology in low strain were applied during acidification of sample, while rheology in large strain was applied on final acid gels. The only effect of the presence of NEM was a reduced firmness of acid gels as measured at large strain and a reduced tendency to form large aggregates at pH<5.5. In conclusions, thiol/disulphide exchanges during acidification of milk played only a minor role in the building of acid gel networks from heated milk.     

MedISys: An early-warning system for the detection of (re-)emerging food- and feed-borne hazards

We evaluated the Medical Information System (MedISys) as an early-warning system for the detection of food- and feed-borne hazards. Nine hazards were selected in the period from January 2007 to March 2009 from the Rapid Alert System for Food and Feed (RASFF) and traced back on MedISys and ProMED-mail. In addition, from January to March 2009, food- and feed-borne (re-)emerging hazards were monitored on MedISys and traced back on ProMED-mail and RASFF. MedISys has demonstrated to be an effective early-warning system for food- and feed-borne hazards. However, further customization is required to improve its sensitivity, in particular by increasing the number of multi-lingual categories related to food and feed items. MedISys tended to detect food- and feed-borne hazards earlier and more frequently than ProMED-mail, but the information from both systems was often complementary.     

Phaseolin diversity as a possible strategy to improve the nutritional value of common beans (Phaseolus vulgaris)

This article proposes a new way to improve the protein quality of the common bean (Phaseolus vulgaris). It is based on the natural variability found in the different types of phaseolin, its main storage protein (40–50% of the total protein). Despite the fact that it is deficient in methionine content, phaseolin still represents the main source of that amino acid in the seed. More than 40 genetic variants, differing in subunit number (2–6) and molecular weight (40–54 kDa) have been analyzed. The similarity of the amino acid composition among phaseolins, suggests that a nutritional improvement cannot be expected from that side. Conversely, important variation in phaseolin susceptibility to proteolysis (ranging from 57% to 96% after cooking) has been observed, increasing the theoretical availability of methionine by up to 37%. Therefore, breeding programs based on highly-digestible phaseolin types could lead to the production of beans with higher protein quality.     

Impact of enzyme inactivation conditions during the generation of whey protein hydrolysates on their physicochemical and bioactive properties

The thermal inactivation conditions (75 °C × 35 min, 80 °C × 10 min, 85 °C × 5 min and 90 °C × 5 min) for Protamex? following bovine whey protein concentrate (WPC) hydrolysis was studied with the view to limiting WPC hydrolysate (WPH) aggregation while maintaining bioactivity. A decrease in the amount of large WPH aggregates formed was observed at inactivation temperatures ≤85 °C. However, the WPC appeared to be more hydrolysed on heating at 75 °C × 35 min, as Protamex? was active for longer under these heating conditions. Significantly (P < 0.05), higher WPH antioxidant (oxygen radical absorbance capacity – ORAC) activity was obtained on inactivation at temperatures ≤80 °C. In contrast, the dipeptidyl peptidase IV (DPP‐IV) inhibitory properties of all WPH samples were similar (P > 0.05). A reduction in thermal treatment from 90 °C × 5 min to 85 °C × 5 min was sufficient to decrease the amount of large aggregates formed in the hydrolysate without altering its bioactive properties.     

Apparent chemical composition of nine commercial or semi-commercial whey protein concentrates, isolates and fractions

Summary Analytical results are given for whey powders prepared on a commercial or semi-commercial scale by three companies. Altogether, five preparations enriched in β-lactoglobulin, four whey protein isolates and a fraction enriched in α-lactalbumin were analyzed for protein composition, including %β-lactoglobulin, α-lactalbumin, bovine serum albumin, casein (glyco) macropeptide and the main triglycerides. Protein composition was determined by high pressure gel permeation and reversed phase liquid chromatography and by capillary zone electrophoresis. The extent of modification of the native β-lactoglobulin structure was also measured through the degree of lactosylation and the fraction of accessible free sulphydryl groups. One significant finding was that the calculated recovery of protein following quantitation of the chromatogram or electropherogram was seldom above 90% and occasionally below 60% of that loaded onto the column or capillary, raising doubts as to the reliability of the analytical results. Extrapolation by linear regression to 100% recovery allowed estimates to be made of the true β-lactoglobulin composition of the samples. The nine samples could be placed into three distinct groups with estimated true β-lactoglobulin weight % of 70.9 ± 1.1, 62.0 ± 3.4 and 39.5 ± 4.9. Physico-chemical properties of the group of samples are reported elsewhere (Holt et al ., 1999).     

The heat treatment and the gelation are strong determinants of the kinetics of milk proteins digestion and of the peripheral availability of amino acids

This study aimed to determine the kinetics of milk protein digestion and amino acid absorption after ingestion of four dairy matrices by six minipigs: unheated or heated skim milk and corresponding rennet gels. Digestive contents and plasma samples were collected over a 7 h-period after meal ingestion. Gelation of milk slowed down the outflow of the meal from the stomach and the subsequent absorption of amino acids, and decreased their bioavailability in peripheral blood. The gelled rennet matrices also led to low levels of milk proteins at the duodenum. Caseins and β-lactoglobulin, respectively, were sensitive and resistant to hydrolysis in the stomach with the unheated matrices, but showed similar digestion with the heated matrices, with a heat-induced susceptibility to hydrolysis for β-lactoglobulin. These results suggest a significant influence of the meal microstructure (resulting from heat treatment) and macrostructure (resulting from gelation process) on the different steps of milk proteins digestion.