The aim of this study was to develop models based on Linear Discriminant Analysis (LDA), Classification and Regression Trees (C&RT), and Artificial Neural Network (ANN) for the prediction of the botanical origin of honeys using their physicochemical parameters as well as their antioxidative...

A well balanced diet of modern population includes an increased consumption of products from goat’s milk, which has composition different from the commonly used cow milk. Goat’s milk is characterized by better digestibility, higher...

The aim of this study was to examine the thermal denaturation properties of proteins from fresh and frozen pond mussels Anodonta woodiana by differential scanning calorimetry (DSC). The A. woodiana (Lea, 1834) mussels were collected from the bottom of a lake located in West Poland. Three parts of the mussel: adductor muscle (AM), foot muscle (FO) and part of internal organs (IO), were taken for analysis. The DSC technique was used to characterize the stability of the protein system, and SDS-PAGE was applied for the separation and identification of proteins. Thermal analysis in all parts of the mussel revealed two main endothermic transitions: the first at 60–61 °C and the second at 69–70 °C. Denaturation transition occurred in the temperature range from 42 to 76 °C. The highest enthalpy of denaturation was observed for FO and was 15.75 J g⁻¹ (per 1 g of protein) and 14.01 J g⁻¹ for AM. The lower-temperature peak, related to myosin and paramyosin, accounted for approximately 70–80 % of the total area of transition. Electrophoretic analysis (SDS-PAGE) confirmed that the paramyosin, with a mass of approx. 98–107 kDa, constituted the largest percentage, i.e., 24 % in AM and 17 % in IO and FO. Two other main myofibrillar proteins were also present in significant amounts: myosin with a molecular mass of 230–245 kDa (12–14 %) and actin with a mass of 47 kDa (18–20 %). In this study, the effect of freezing on protein stability was also investigated. The results of DSC analyses revealed that the process of freezing did not have a significant influence on the first and second peak temperature. Significant differences in enthalpy between fresh and frozen samples were observed only for AM, for which the total enthalpy (ΔH) decreased by 33 %. This study provided insight into the biochemistry of A. woodiana meat and offers an area of scientific novelty. Recognizing quality properties of meat tissue from freshwater Chinese pond mussels collected from selected water ecosystems seems to be important with respect to the potential possibility of using it for feed, pet food or even in food products.