No abstract

A low-value sea fish Saurida elongata was hydrolyzed using papain. Proximate composition analysis of the fish protein hydrolysate showed that the hydrolysate contained 84.7% crude protein, 7.1% ash and 3.5% fat. The determination of amino acid content by o-phthaldialdehyde pre-column derivatization reversed-phase high-performance liquid chromatography (RP-HPLC) showed that the hydrolysate contained 20 different amino acids, and the total percentage of eight essential amino acids was as high as 41.5% of the total amino acids, which meant that the hydrolysate could provide a good nitrogen source for human consumption. Peptides were separated by RP-HPLC using a C-18 column into more than 14 fractions. Molecular weight distribution of peptides was determined by size-exclusion HPLC, which indicated that the size of 74.8% of the peptides ranged from 1.0 to 5.0 kDa. Most importantly, the enzymatic hydrolysate from S elongata was shown to contain significant in vivo anti-anaemia activity on experimental anaemia models induced by blood loss or cyclophosphamide damage to hematogenic mechanism. To the best of our knowledge, this was the first time that the description of hydrolysis of S elongata and the indication of anti-anaemia activity in the hydrolysate have been reported.