J. Dias et al., Nutritional control of lipid deposition in rainbow trout and European seabass: Effect of dietary protein energy ratio, CYBIUM, 23(1), 1999, pp. 127-137
The effects of dietary digestible protein (DP) to digestible energy (DE) ra
tio on lipid deposition, activity of selected liver lipogenic enzymes and m
uscle susceptibility to lipid peroxydation were studied in rainbow trout (O
ncorhynchus mykiss) and European seabass (Dicentrarchus labrax). The experi
mental diets were formulated to contain one of two crude protein levels (43
et 52% of dry matter (DM) for seabass and 38 et 45% DM for trout) and DP/D
E ratios ranged from 17 to 26 mg/kJ. During the growth trials, each diet wa
s hand fed to visual satiation, to triplicate groups of fish. Rainbow trout
were grown in freshwater at a constant water temperature of 18 degrees C o
ver 12 weeks. Seabass were grown in seawater (salinity: 35 parts per thousa
nd; temperature: 18 degrees C) over an identical period. For rainbow trout
the best results in terms of growth performance, feed efficiency and protei
n utilisation were achieved at a DP/DE ratio 17-19 mg/kJ. For seabass, the
optimal DP/DE ratio appears to be 19-20 mg/kJ. Whole body composition of ra
inbow trout at the end of the experiment shows that an increase on dietary
lipids led to an increase in fat content of fish. In seabass, the whole bod
y composition was not much affected by experimental treatments. Trout fed h
igh-energy diets showed highest lipid content in the muscle and particularl
y in viscera. In seabass a similar tendance is observed but the liver seems
to be the main site of lipid storage. Muscle homogenates from trout and se
abass fed high-fat diets showed a higher susceptibility to lipid peroxidati
on than fish fed low-fat diets. Activities of liver glucose-6-phosphate deh
ydrogenase (G6PD), malic enzyme (ME) and fatty acid synthethase (FAS) were
reduced with increasing fat intake. Activities of G6PD, ME and FAS were inc
reased with increasing starch intake. G6PD was found to be the main NADPH-g
enerating enzyme.