Airborne ultrasonic application on hot air-drying of pork liver. Intensification of moisture transport and impact on protein solubility.

Nowadays, there is increasing interest in developing strategies for the efficient and sustainable use of animal by-products, such as pork liver. In order to stabilize the product, a prior dehydration stage may be required due to its high perishability. The water removal process of pork liver is energy costly and time consuming, which justifies its intensification using novel technologies. In this sense, the aim of this study was to assess the effect of the airborne application of power ultrasound on the hot air-drying of pork liver. For that purpose, drying experiments were carried out at 30, 40, 50, 60 and 70 °C on pork liver cylinders at 2 m·s-1 with (US) and without ultrasonic application (AIR). The drying process was modeled from the diffusion theory and, in the dried pork liver, the protein solubility was analyzed in order to determine the effect of drying on the protein quality. The ultrasound application increased the drying rate, shortening the drying time by up to 40% at 30 °C. The effect of power ultrasound at high temperatures (60 and 70 °C) was of lesser magnitude. Drying at 70 °C involved a noticeable reduction in the protein solubility for dried liver, while the impact of ultrasound application on the solubility was not significant (p > 0.05).

Heat-induced gelation mechanism of blood plasma modulated by cysteine.

This work aims to determine changes at molecular level of plasma proteins provoked by adding cysteine (Cys, 0.025% to 0.35% w/v) as a reducing agent and their relationship with the heat-induced gel properties obtained when subsequently the solutions were submitted to a thermal treatment. Results show that adding Cys to plasma solutions at concentrations ≥0.15% actually entails modifications in the secondary structure of their main proteins, that is, serum albumin-α-helix rich-and globulin fraction-ß-sheet rich. Basically, a reduction of the intensity of the infrared (IR) bands assigned to both structures takes place concomitant to an increase of extended structures that seem to act as intermediates for the subsequent protein aggregation process through nonnative intermolecular ß-sheets. Cleavage of disulfide bonds is also evidenced at Cys concentrations ≥0.15% by nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with the effects being directly proportional to Cys concentration. However, beneficial effects on gel hardness are gradually obtained at Cys concentrations ≤0.15%, that is, when the effects at molecular level are at most just budding, while not more improvements on this textural parameter are obtained at higher Cys concentrations. By contrast, water retention capacity is gradually diminishing as Cys concentration increases, but with a significant reduction only obtained at the highest tested concentration. These results suggest a negative effect of Cys on gel microstructure at high concentrations, which probably can be attributed to protein aggregation taking place at room temperature.

Foaming and emulsifying properties of porcine red cell protein concentrate.

This work focuses on studying the effects of pH (7.0 and 4.5) and protein concentration on the foaming and emulsifying properties of fresh (F) and spray-dried (SD) porcine red cell protein (RCP) concentrates in order to evaluate the proper use of this blood protein as a functional food ingredient. Also, protein solubility is measured through the pH range from 3.0 to 8.0. In each case, all concentrates show a high solubility, although this is significantly affected by pH. Spray drying slightly reduces the solubility at mild acid and neutral conditions. The foaming capacity is found to be dependent on pH as well as on the drying treatment. SD-RCP concentrates show better foaming capacity than F-RCP. The minimum protein concentration required to attain the highest foaming capacity is found under acid pH for the spray-dried concentrates. Although F-RCP shows low foam stability at acid and neutral pH, spray drying and protein content enhance the stability of foams. Emulsifying properties show dependence on pH as well as on protein content. Furthermore, spray drying affects the emulsifying properties but in different ways, depending on pH and protein concentration.

Color stabilization of porcine hemoglobin during spray-drying and powder storage by combining chelating and reducing agents.

This work focuses on the effects of adding a chelating agent - such as nicotinic acid (NA, 2% w/v) or nicotinamide (Nam, 2.5% w/v) - along with glucose as a reducing agent (G, 10% w/v) to fresh porcine hemoglobin in order to stabilize its red color during spray-drying and powder storage at room temperature. Correlations between the CIELAB color parameters and the relative percentages of the different hemoglobin derivatives (liganded and deliganded ferrohemoglobin, and methemoglobin) were analyzed. The results indicate that, although little effects could be observed for any of the combined treatments on fresh hemoglobin, they were effective against pigment autoxidation during dehydration and subsequent storage. From the results, it can also be concluded that glucose was the main contributor to the color stabilization of the hemoglobin powder, probably due to its high water retention capacity.

Functional and quality characteristics of the red blood cell fraction from biopreserved porcine blood as influenced by high pressure processing.

The effects of high hydrostatic pressure (HHP) processing, at 400MPa for 15min at 20°C, on the microbiological and functional characteristics of the red blood cell (RBC) fraction obtained from porcine blood, previously preserved by means of lactic acid bacteria (LAB) was studied. Biopreservation was achieved by incubation of inulin-enriched blood inoculated with a LAB strain (Enterococcus raffinosus PS99) for 72h at 5°C. Results showed that incubation of blood with added E. raffinosus followed by HHP treatment reduced the levels of contaminant coliforms, proteolytic, hemolytic bacteria, and Pseudomonas spp. on RCB. Color parameters, protein solubility, foaming and emulsifying properties, as well as texture and water holding capacity of heat-induced gels from RBC were not seriously damaged by the combined treatments. This is a new approach to process and preserve animal blood fractions for the development of functional and/or nutritional food ingredients with added value.