Study on the induced polymeric protein aggregation and immunoreactivity in biscuits enriched with peanut flour.

This work deals with the study on the protein extractability of biscuits incurring different percentages of roasted peanut flour. The presence of two different flours influenced the rate of protein aggregation and protein extractability, according to the percentage of roasted peanut flour added to the formulation and assessing these features by testing the use of two buffers. Results showed that gluten network arrangement of biscuits was influenced by the flours mixture besides the baking, with possible different protein organizations.

Effect of the Addition of Freeze-Dried Grape Pomace on Fresh Tagliatelle Gluten Network and Relationship to Sensory and Chemical Quality.

The incorporation of 5 and 10% freeze-dried grape pomace powder (GPP) in fresh tagliatelle pasta preparation was evaluated for its effect on chemical composition, gluten protein structure, and sensory properties. The addition of the freeze-dried GPP led to a significant increase ( < 0.05) in polyphenol content in the raw and cooked fortified pasta samples with respect to 100% semolina pasta, although the phenolic content decreased after the cooking process.

A proteomic study of "Coppa Piacentina": A typical Italian dry-cured Salami.

Coppa Piacentina is considered a peculiar dry cured salami, since it is manufactured by the entire neck muscles stuffed and matured in natural casings, the same as dry cured ham and fermented dry cured sausages. In this work the proteolysis of external and internal portions was investigated by a proteomic approach and by amino acids analysis. Samples of "Coppa Piacentina" were analyzed at 0 days and after 5 and 8 months of ripening through mono- and two-dimensional gel electrophoresis.

Protein aggregation in cooked pork products: New details on the supramolecular organization.

The molecular weight distribution of protein aggregates from raw meat and cooked pork products was assessed by size exclusion-high performance liquid chromatography (SE-HPLC). Electrophoretic analysis under reducing conditions showed that the high molecular weight SE-HPLC peak (peak 1) of the cooked products contained protein aggregates in addition to high molecular weight muscle proteins, while the second peak (peak 2) still contained aggregates and <50 kDa proteins. The protein aggregates composition was investigated by HPLC-tandem mass spectrometry.