The objectives of this study were to investigate the amino acid composition and thermal properties of silkworm larvae protein isolate (SLPI) and to evaluate the in vitro angiotensin-converting enzyme (ACE) inhibitory and antioxidant activities of its hydrolysate prepared with gastrointestinal enzymes. The results showed that, SLPI was a high quality protein source with a well-balanced composition of essential amino acids, which was especially rich in glutamic acid (13.79 g/100 g protein), aspartic acid (10.44 g/100 g protein), leucine (8.68 g/100 g protein), lysine (8.01 g/100 g protein) and arginine (6.59 g/100 g protein). In additon, three endothermic denaturation transitions were observed in DSC thermograms of SLPI. The maximum transition peak occurred in the third thermal transition, which denaturation temperature (T d ), peak temperature of denaturation (T p ) and enthalpy change (ΔH) were 76.95°C, 80.42°C and 783.75 J/g, respectively. SLPI hydrolysate exhibited strong ACE-inhibitory activity (IC 50 =8.3 μg/ml) and relatively higher 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity (IC 50 =57.91 μg/ml) and ferrous ions chelating capacity (IC 50 =2.03 mg/ml). Moreover, the hydrolysate showed notable reducing power. It was concluded that, SLPI might be considered as a multifunctional ingredients for functional foods with protein supplements, ACE-inhibitory and antioxidant activity.
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Qiongying et al. (2011) studied this question.