• Fisheries and Aquatic Sciences
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• v.18 no.1
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• pp.13-20
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• 2015

Calculated chemical scores (computed in relation to the FAO/WHO reference protein) for salmon liver protein hydrolysates indicated that all amino acids (other than methionine and threonine) were present in adequate or excess quantities; thus, the raw liver material is a good source of essential amino acids. The hydrophobic amino acids contents in hydrolysates prepared from Oncorhynchus keta and O. gorbuscha were 38.4 and 39.1%, respectively. The proportion of released peptides exceeding 500 kDa was reduced when hydrolysates were treated with the commercial enzyme Alcalase, although proportions in the following MW ranges were elevated: 100-500 kDa and <50 kDa. The optimal conditions for enzymatic hydrolysis were as follows: pH 7.0, $50^{\circ}C$, and a reaction time of 1 h. Of the different proteases tested, Alcalase was the most efficient for production of salmon liver hydrolysate with the highest 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity. The hydrolysates prepared from salmon liver had a balanced amino acid composition. The liver protein hydrolysates contained low molecular weight peptides, some of which may be bio-active; this bio-active potential should be investigated. Inhibition of the DPPH radical increased with increased degree of hydrolysis (DH), regardless of protease type. DPPH radical scavenging abilities, antithrombotic effects and ${\alpha}$-glucosidase enzyme inhibition effects of O. keta liver hydrolysate increased in a dose-dependent manner. Thus, salmon liver hydrolysate may be useful in functional food applications and as a source of novel products.

• Journal of the Korean Society of Food Science and Nutrition
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• v.42 no.11
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• pp.1759-1766
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• 2013

In this study, the optimal conditions for salmon hydrolysate using squid liver and compositional properties of hydrolysate were investigated. The optimal conditions were $55^{\circ}C$, pH 5.5 and 0.66~0.67% (w/w) in the ratio of squid liver to acidic and thermal treated salmon muscle. The free amino acid of hydrolysate from the acidic treated salmon muscle was higher than that of hydrolysate from the thermal treated salmon muscle, while the total amino acid and mineral were high in the acidic treated salmon muscle. Furthermore, cadmium of hydrolysate from the thermal denatured salmon muscle was below 2 ppm, and has an acceptable level as potential ingredient. The distribution of peptide molecular weight was 40.0% for 1.0~9.5 kDa, 6.7% for 0.5 kDa, and 47.4% of others in hydrolysate from the thermal treated salmon muscle. Both hydrolysates did not show any toxicity against the HepG2 cell line for up to $200{\mu}g/mL$.