Deposition in broiler muscle
The efficacy of 4 different selenium sources on the deposition of selenium in broiler muscle tissue were compared in an in vivo trial at KU Leuven, Faculty of Engineering Technology (Geel, Belgium). Results are presented in Figure 1. In this trial male broilers were fed one of five treatment starter diets. All treatments had 4 pens with 5 animals per pen.
- Treatment 1 was supplemented with 0.2 mg/kg total Se from sodium selenite (55).
Treatment 2 and 3 were supplemented with LSeMet (Excential Selenium4000, Orffa Additives BV. The Netherlands) at a dosing of 0.2 and 0.16 mg/kg total selenium, providing 0.2 mg/kg Se and 0.16 mg/kg Se in the form of L-SeMet respectively.
Treatment 4 was supplemented with 0.2 mg/kg total Se in the form of hydroxy-selenomethionine (OH-SeMet), which provides respectively 0.0 mg/kg total Se in the form of L-SeMet to the diet. Treatment 5 was supplemented with 0.2 mg/kg total Se in the form of a Se-yeast, which resulted in a supplementation of 0.058 mg Se in the form of L-SeMet/kg (only 29% of the total Se was present in the form of L-SeMet; EU legislation requires a minimum of 63%).
In treatment 3 the dosage of 0.16 mg/kg Se in the form of L-SeMet was chosen, as it was hypothesised that the relative utilisation of OH-SeMet (treatment 4) should reach approximately 80% compared to LSeMet.
Sample analysis
Representative samples of the left breast of 3 broilers per pen were taken on d 14 and analysed for Se content by ICP-MS at the university of Ghent, Belgium. Results show a Se content in broiler muscle for treatment 1 (55) of 93 μg/kg Se. The SeYeast showed 101 μg/kg Se. Treatment 2 and 3 (Exc. Seleni um4000) showed the highest Se content in muscle with 263 μg/kg Se and 225 μg/kg Se, respectively. Treatment 4 showed a comparable Se content as treatment 3, OH-SeMet, and 16% lower than treatment 2, Exc. selenium4000 at 0.2 ppm Se. Exc. selenium4000 at 0.2 ppm Se was the only compound able to maintain the selenium status observed at thestart. The observed lower efficacy (-16%) of
OH-Se-Met compared to Exc. Selenium4000 confirms previous findings by Rovers et al. 2016 (abstract WPC). In this earlier trial, 3 different commercially available Se products were incorporated (Figure 2).
Treatment 1 was supplemented with 0.2 mg/kg total Se from sodium selenite (SS). • Treatment 2 was supplemented with L-SeMet (Excential Selenium4000, Orffa Additives BV, The Netherlands) at a dosing of 0.2 mg/kg total selenium. • Treatment 3 was supplemented with 0.2 mg/kg total Se in the form of OH-SeMet. Representative samples of the breast were taken on d7 and analysed for Se content by ICP-MS at the university of Ghent, Belgium. Also here the OH-SeMet treatment showed a lower Se deposition then the Exc. Selenium4000 treatment. The difference in deposition was 15%.
Relative utilisation of L-methionine and its hydroxy analogue
EFSA (European Food Safety Authority) states that the relative utilisation of the hydroxy analogue of L-Met (OH-Met) is lower than L-Met. Table 1 gives an overview of the data brought forward by EFSA (ref 2012). Values are expressed as percentages of the growth efficacy (molar or isosulphurous basis) of the Lisomer, which is in all cases presumed to present 100% oral utilisation. The data shows that the relative utilisation of OH-Met tor all tested animal species is lower than L-Met. For pig and poultry this is down to 80%. The explanation tor this observation lies among others in the conversion of OH-Met to L-Met inside the body. OH-Met is a DL racemic mixture consisting of an L isomer and a D isomer. After adsorption in the upper gastrointestinal tract by simple diffusion or through a low affinity lactic acid carrier mechanism, the con version of DL-OH-Met takes place by enzymatic conversions. The L isomer of OH-Met will be converted to a ketomethionine intermediate called keto-methylthiobutanoic acid (KMB) by L-hydroxy acid oxidase (LHAOX) in peroxisomes found primarily in liver and kidney cells. The D isomer of OH-Met is converted to KMB as well but via D-hydroxy acid dehydrogenase (D-HADH) present in mitochondria of all cells. Eventually, KMB undergoes transamination to form LMet. This complicated 2-way/2-step conversion is likely to be the cause of the lower relative utilisation. L-Met, by contrast, is simply built into proteins as such, no conversion is needed.
