No abstract

The present study in rats was aimed at determining the specific day of pregnancy on which maternal body fat accumulation starts and which tissues are involved. Most of the body weight increase at day 12 of gestation corresponded to conceptus-free maternal weight which progressively increased until the 19th day of gestation after which maternal weight stabilized and the rate of conceptus weight gain became maximal. Maternal carcass fat content progressively increased until day 18 of gestation, increased very markedly on day 19, stabilized between day 19 and 20 and then decreased on day 21. These changes were the opposite of the course of the specific-gravity values. The fresh weight of lumbar fat-pads and mesenteric adipose tissue reflected the changes in carcass fat content throughout gestation. Periuterine adipose-tissue mass declined on day 12 of gestation to be recuperated later, subcutaneous adipose tissue increased on day 12 to decline progressively thereafter and interscapular brown adipose tissue remained stable until day 20 and increased on day 21. With only a few exceptions, the lipid concentration in all these adipose tissues remained stable throughout gestation. Mammary glands and liver weights increased intensely from day 12 and, whereas the lipid concentration in the former was stable, in the latter it decreased on day 12 and increased on days 18 and 19. These results show that in the rat (a) maternal carcass fat accumulation during gestation is not paralleled by the size of the different fat-storing tissues and (b) mammary-gland fat accumulation also contributes to maternal fat storage.

Selective thermal precipitation followed by a mechanical separation step is a well described method for fractionation of the main whey proteins, α-lactalbumin (α-la) and β-lactoglobulin (β-lg). By choosing appropriate environmental conditions the thermal precipitation of either α-la or β-lg can be induced. Whereas β-lg irreversibly aggregates, the precipitated α-la can be resolubilized by a subsequent adjustment of the solution’s pH and the ionic composition. This study reports on the analytical characterization of resolubilized α-la compared to its native counterpart as a reference in order to assess whether the resolubilized α-la can be considered close to ‘native’. Turbidity and quantification by RP-HPLC of the resolubilized α-la solutions were used as a measure of solubility in aqueous environment. RP-HPLC was also applied to determine the elution time as a measure for protein’s hydrophobicity. DSC measurement was performed to determine the denaturation peak temperature of resolubilized α-la. FTIR spectroscopy provided insights in the secondary structure. The refolding of α-la achieved best results using pH 8.0 and a 3-fold stoichiometric amount of Ca2+ per α-la molecule. The results showed that the mechanism of aggregation induced by gentle thermal treatment under acidic conditions with subsequent mechanical separation is reversible to a certain extent, however, the exact native conformation was not restored.