RESUMEN
Membrane filtration technologies have shown great potential as a gentle and effective method for concentrating and fractionating proteins for food applications. However, the application of this technology to plant-derived protein streams is in its infancy. In this study, an aqueous rapeseed protein concentrate was obtained with wet milling, and its performance during ultrafiltration with two distinct molecular weight cut-offs (10 and 100 kDa) was tested. All rapeseed proteins were retained during filtration. The addition of pectinase during extraction prior to filtration caused important structural modifications to the extract, resulting in increased permeate fluxes, increased carbohydrate permeation and a reduction in irreversible fouling. Lager pore sizes led to more pronounced fouling. FTIR analysis of the spent membranes showed that proteins and lipids are causing irreversible fouling.
RESUMEN
The contents and profiles of small molecules in a food can provide information about quality-related properties. Processing methods and deterioration during storage, e.g. from bacterial proliferation and degradation, might also lead to changes in the metabolome, which can be determined by mass spectrometry-based metabolomics. By measuring as many metabolites as possible in differently treated pre-cooked chicken fillets in an untargeted approach, we studied individual and combined effects of vacuum packaging (VP), soluble gas stabilisation (SGS), high pressure processing (HPP), and microwave volumetric heating (MW) on the quality and shelf-life of the finished product. The extensive dataset was processed using an optimised workflow of consecutive software tools with stringent statistical analysis to prevent over-interpretation, which is an inherent risk of metabolomics data. Our results showed the predominant influence of VP on storage quality since SGS, HPP, and MW did not have the potential to extent shelf-life.
Asunto(s)
Pollos , Culinaria , Animales , Embalaje de Alimentos , Metabolómica , Control de Calidad , Flujo de TrabajoRESUMEN
Shell-loosening is of importance in facilitating shrimp peeling. In this study, enzyme and high pressure (HP) improved the shell-loosening at different degrees, which were observed as gaps by microscopy. The shell-loosening gap induced by an endoprotease with broad specificity (Endocut-03L, 53⯵m) was much higher than that induced by HP at 100â¯MPa (HP100, 12⯵m), followed by an endoprotease with high specificity (Tail21, 8⯵m), and HP at 600â¯MPa (HP600, 5⯵m). The degree of shell-loosening was found to be correlated to the extent of protein changes that were obtained by 2D gel electrophoresis. Shell-loosening due to HP100 and Endocut-03L was mainly caused by physical and enzymatic degradation of high molecular-weight proteins in shell and epidermis and subsequent loss of degradation products, disrupting the structure of muscle-shell connection. However, HP100 was less effective than Endocut-03L due to its stabilizing effect on the shell collagen, lowering its shell-loosening effect.