Influence of level of inclusion of Azolla leaf meal on growth performance, meat quality and skeletal muscle p70S6 kinase α abundance in broiler chickens

The interest in biodiesel production from oil-bearing seeds rather than soybean necessitates the scientific validation of other good quality protein sources that could substitute soybean meal in animal diets, particularly, broiler chickens where soybean meal constitutes a large portion of their diet. Therefore, the present study was conducted to investigate the effect of sun-dried Azolla leaf meal(ALM)as an unconventional dietary protein source in broiler chicken diet on growth performance, meat quality, skeletal muscle cell growth and protein synthesis through regulation of ribosomal protein S6 kinase (p70S6 kinase alpha). A total of 120 male Ross 308 broiler chicks were randomly allocated to three dietary treatments. Each treatment had four cages (i.e. replicates) with 10 birds/cage. The control group was fed with a corn-soy-based diet, theAZ5group was supplemented with 5% ALM and theAZ10group was supplemented with 10% ALM for 37 days. A 5-day trial was also conducted to measure the apparent nutrient digestibility. Growth performance parameters were measured weekly. At the end of the experiment, 12 birds from each group (3/cage) were euthanized and used for samplings. Inclusion of ALM tended to improve BW gain (P= 0.06) and increased feed intake (P< 0.01). Additionally, ALM decreased the percentage of breast meat cooking loss linearly (P< 0.01). In addition, ALM at a dose of 5% increased the production of propionate in the cecum (P= 0.01). Activation of breast muscle p70S6 kinase was higher when ALM was included in a dose-dependent manner (P< 0.01). The inclusion of ALM increased breast meat redness (P< 0.01); however, the lightness was within the normal range in all groups. Findings from our study suggest that ALM could be included in a broiler chicken diet up to 5% without any major negative effect on meat quality or performance, and it regulates muscle protein synthesis through activation of mammalian target of rapamycin/6S kinase signaling.