Comparative Study on Biochemical Properties and Antioxidative Activity of Cuttlefish (Sepia officinalis)‎ Protein Hydrolysates Produced by Alcalase and Bacillus licheniformis NH1 Proteases

الملخص EN

Antioxidative activities and biochemical properties of protein hydrolysates prepared from cuttlefish (Sepia officinalis) using Alcalase 2.4 L and Bacillus licheniformis NH1 proteases with different degrees of hydrolysis (DH) were determined.

For the biochemical properties, hydrolysis by both enzymes increased protein solubility to above 75% over a wide pH range.

The antioxidant activities of cuttlefish protein hydrolysates (CPHs) increase with increasing DH.

In addition, all CPHs exhibited antioxidative activity in a concentration-dependent manner.

NH1-CPHs generally showed greater antioxidative activity than Alcalase protein hydrolysates (P<0.05) as indicated by the higher 1,1-diphenyl-1-picryhydrazyl (DPPH) radical scavenging activity and ferrous chelating activity.

Both Alcalase and NH1 protein hydrolysates were able to retard lipid peroxidation and β-carotene-linoleic acid oxidation.

Alcalase-CPH (DH = 12.5%) and NH1-CPH (DH = 15%) contained 75.36% and 80.11% protein, respectively, with histidine and arginine as the major amino acids, followed by glutamic acid/glutamine, serine, lysine, and leucine.

In addition, CPHs have a high percentage of essential amino acids made up 48.85% and 50.04%.

Cuttlefish muscle protein hydrolysates had a high nutritional value and could be used as supplement to poorly balanced dietary proteins.