Cheese-whey is a valuable byproduct of the dairy industry, rich in various nutritional components such as minerals, lactose, and proteins. Whey proteins, often used in concentrate form, are widely applied in the food industry due to their diverse chemical, physical, and techno-functional properties. This study aimed to investigate the physicochemical composition and biochemical characteristics of camel and bovine whey after partial demineralization at a laboratory scale. Camel whey exhibited lower pH values compared to bovine whey, while showing comparable levels of total solids, ash, and lactose, but significantly higher protein content. Analysis of both types of whey, before and after dialysis filtration, demonstrated partial demineralization, a significant reduction in lactose content, and a decrease in β-lactoglobulin levels in bovine whey. These findings suggest that demineralized camel and bovine whey hold significant potential for applications in the agricultural and food industries.

The overexpression of wheat Bx7 subunit (Bx7OE) encoded by the Glu-B1al allele is originated from a duplication event of the Bx7 gene, and has a positive effect on gluten strength. Thus, it is an important genetic resource for wheat quality improvement. In this study, the Bx7OE subunit from a large number of bread wheat and related species was characterized by sodium dodecyl sulphate–polyacrylamide gel electrophoresis, reversed-phase high-performance liquid chromatography (RP-HPLC) and Sequence-Tagged sites (STS) markers. Only 31 bread wheat varieties were found to carry Bx7OE. RP-HPLC quantification analysis revealed that the mean proportion of the Bx7OE subunit to the total amount of high-molecular-weight glutenin subunits among the 31 bread wheat varieties was 41.8%, which is much higher than that of varieties with the normal Bx7 subunit (generally at 30%). Flour quality analysis of seven representative varieties with Bx7OE and three with the normal Bx7 subunit showed that the varieties with Bx7OE generally displayed better gluten strength than those with the normal Bx7 subunit. STS markers demonstrated that, in addition to the 31 bread wheat varieties with Bx7OE, no PCR products were obtained from the related Triticum and Aegilops species. This suggests that the retroelement-mediated recombination event at the Glu-B1 locus could have occurred more recently, later than the formation of hexaploid wheat. The Bx7OE subunit is mainly distributed in some bread wheat varieties from American countries with a low frequency, which is of particular importance for the quality improvement of wheat gluten.

Sensitive methods that are currently used to monitor proteolysis by plasmin in milk are limited due to their high cost and lack of standardisation for quality assurance in the various dairy laboratories. In this study, four methods, trinitrobenzene sulphonic acid (TNBS), reverse phase high pressure liquid chromatography (RP-HPLC), gel electrophoresis and fluorescamine, were selected to assess their suitability for the detection of proteolysis in milk by plasmin. Commercial UHT milk was incubated with plasmin at 37°C for one week. Clarification was achieved by isoelectric precipitation (pH 4·6 soluble extracts) or 6% (final concentration) trichloroacetic acid (TCA). The pH 4·6 and 6% TCA soluble extracts of milk showed high correlations (R2 > 0·93) by the TNBS, fluorescamine and RP-HPLC methods, confirming increased proteolysis during storage. For gel electrophoresis, extensive proteolysis was confirmed by the disappearance of α- and β-casein bands on the seventh day, which was more evident in the highest plasmin concentration. This was accompanied by the appearance of α- and β-casein proteolysis products with higher intensities than on previous days, implying that more products had been formed as a result of casein breakdown. The fluorescamine method had a lower detection limit compared with the other methods, whereas gel electrophoresis was the best qualitative method for monitoring β-casein proteolysis products. Although HPLC was the most sensitive, the TNBS method is recommended for use in routine laboratory analysis on the basis of its accuracy, reliability and simplicity.