The Binding of Free and Sulfated Androstenone in the Plasma of the Boar

SIMPLE SUMMARY: Boar taint is characterized by an off-odor or off-flavor in heated pork products that is caused by the accumulation of androstenone in the fat. We have previously demonstrated that androstenone is transported to the fat bound by the plasma protein albumin; however, it is unclear if androstenone sulfate, which is more abundant in the circulation, is transported in the same manner and if the transport of androstenone in the plasma influences the degree of accumulation in the fat. In this article, we determined that androstenone sulfate bound minimally in the plasma of the boar and suggested that this may leave it readily available to enter peripheral tissues, such as the fat where it may enzymatically return free androstenone. Additionally, we demonstrated that the binding of androstenone in the plasma varies significantly between boars with high and low concentrations of androstenone in the fat. This suggests that the binding of androstenone to albumin in the plasma affects the transport and distribution of androstenone within the boar. ABSTRACT: Androstenone circulates in the plasma bound to albumin before accumulating in the fat, resulting in the development of boar taint. Androstenone sulfate is more abundant in the circulation than free androstenone; however, it is unclear how androstenone sulfate is transported in the plasma and if steroid transport affects the development of boar taint. Therefore, the purpose of this study was to characterize the binding of androstenone sulfate in boar plasma and determine if variability in steroid binding affects the accumulation of androstenone in the fat. [(3)H]-androstenone sulfate was incubated with plasma and the steroid binding was quantified using gel filtration chromatography. Inter-animal variability was assessed by quantifying androstenone binding specificity in plasma obtained from boars that had high or low fat androstenone concentrations at slaughter. Androstenone sulfate bound minimally in the plasma and to isolated albumin, which suggests that it is transported primarily in solution. The specific binding of androstenone quantified in plasma and isolated albumin from low fat androstenone animals was significantly higher (p = 0.01) than in high fat androstenone boars. These results indicate that the binding of androstenone to albumin varies amongst individual animals and affects the transport of androstenone in the plasma and accumulation in the fat of the boar.