Effect of added enzymes and quinoa flour on dough characteristics and sensory quality of a gluten free bakery product

The study is aimed at developing a new cereal-based product, with increased nutritional quality, by using quinoa flour. The effect of the use of transglutaminase (TGase) and proteolytic enzymes on the microstructure, properties and in vitro digestion of gluten-free bakery products based on quinoa flour was evaluated. Microstructural results evaluated by means of Scanning Electron Microscopy (SEM) showed that the quinoa starch granules are rather small (0.4–2 μm) and the presence of TGase induced significantly changes in dough and baked samples microstructures. The overall acceptability of the breads was improved by TGase addition. The results achieved showed that these enzymes have different effects on the bread characteristics and may improve properties of formulations, setting the basis for development of baked quinoa products

Occurrence of quantitative genetic polymorphism at the caprine beta-CN locus, as determined by a proteomic approach

Genetic screening of caseins in caprine milk samples enabled the identification of two novel b-casein (b- CN) phenotypes, C2 and F1, expressed at lower levels (3.3 and 2.7 g L_1 per allele, respectively) than reference b-CN C (4.7 g L_1 per allele), and another lacking in aS-complex. The b-CN C2 and F1 primary structures, determined by MS analysis, corresponded to b-CN C and F, respectively. The reasonable hypothesis supporting the low expression of both variants considers the C2 and F1 alleles as deriving from b-CN C1 and b-CN A1 precursors, respectively, and characterised by a genic transition C/T negatively affecting the mRNA stability. Further, phosphorylation of Thr41 responsible for the 7P b-CN component was determined by a proteomic approach for the first time. Caprine milk containing low levels of antigenic aS1-, aS2- and b-CN can be used for infant formula production and drinking milk for people with cows' milk protein allergy

Thermal markers arising from changes in the protein component of milk

Classification of heat load applied to milk requires the detection of parameters appropriately related to the intensity of the heat treatment. Current analytical methods based on heat-induced changes in the protein component of milk have been directed either to determine the amount of protein-derived products arised from heat treatments or to evaluate the extent of thermal denaturation of milk proteins. Lately, a new analytical strategy has been developed according to the occurrence of three major whey proteins, namely bovine serum albumin (BSA), beta-lactoglobulin (blg) and alfa-lactalbumin (ala), normally soluble at pH 4.6 in raw milk, in the pH 4.6 insoluble protein fraction recovered from heattreated milk. The results have shown that pH 4.6 insoluble BSA, blg and ala, as detected by ELISA in milk, can be regarded as thermal markers suited for either dairy process control or regulation purposes