Rs Katersky

Growth and protein synthesis of barramundi, Lates calcarifer, fed lupin as a partial protein replacement.

Protein synthesis is an essential growth process in all animals. Little information is available on post-prandial protein synthesis and even less where different protein sources are compared. Protein synthesis was measured at 4 and 24 h after feeding juvenile barramundi in order to determine the effect of using lupin as a partial protein replacement for fish meal on the post-prandial protein metabolism. Juvenile barramundi (4.3+/-0.6 g) were held in a recirculation system (27 degrees C, salinity 10 per thousand and 24 h light) for 15 days. Fish were fed one of two isonitrogenous isoenergetic diets (40% crude protein, 16% lipid and 18.5 GE MJ kg(-1)). One diet was formulated with 100% fish meal as the protein source while the other had 45% of the protein replaced with lupin ingredients (lupin kernel meal (Lupinus angustifolius) and lupin protein concentrate). All fish were fed a ration of 6%.d(-1) and feed intake was not significantly different between the two diets. Specific growth rate (SGR) and growth efficiency (in relation to protein (PPV) and energy (PEV)) were 6.5+/-0.14%.d(-1), 43.8+/-2.72% and 38.31+/-1.56%, respectively, and were not significantly different between the two diets. There was no significant difference in protein synthesis between the two diets at 4 and 24 h after feeding, however protein synthesis was significantly higher 4 h after feeding than at 24 h (p=0.02). Neither growth performance nor protein metabolism was altered by replacing 45% of the protein with lupin protein and indicated this to be a suitable protein source for barramundi feeds.

The effect of temperature on post-prandial protein synthesis in juvenile barramundi, Lates calcarifer

The experiment aimed to measure post-prandial protein synthesis at three different temperatures. Juvenile barramundi (10.81+/-3.46 g) were held at 21, 27 and 33 degrees C and fed to satiation daily. Samples were taken over a 24h period at 0 (24h after the previous meal) and then at 4, 8, 12 and 24h after feeding to measure protein synthesis in the white muscle, liver and remaining carcass. Protein synthesis at 27 and 33 degrees C peaked 4h after feeding in all tissues and returned to pre-feeding rates by 12h. At 21 degrees C protein synthesis remained constant over 24h in all tissues. While the concentration of RNA remained stable over the 24h cycle and across temperatures, the ribosomal activity increased after feeding. This meant k(RNA), not the absolute amount of RNA, was the driving force underlying the post-prandial increase in protein synthesis. However, relative differences in protein synthesis between tissues were attributed to differences in RNA concentration. There was a significant positive relationship between white muscle and whole body protein synthesis. This was the first study to show an interaction between temperature and the time after feeding on protein synthesis for an ectotherm, and that a post-prandial peak in protein synthesis only occurred under optimum temperature conditions.