Protein hydrolysates were prepared from defatted engraved catfish roe using alcalase enzyme by a two-stage serial hydrolysis process. The soluble hydrolysate formed after first stage of hydrolysis was removed (RH-1) and fresh enzyme was added at the same concentration to achieve further hydrolysis (RH-2). Further, compositional, surface-active and antioxidant properties of both hydrolysates were compared. The SDS-PAGE profile showed two distinct bands for RH-1, whereas no bands were visible for RH-2. On the other hand, gel filtration chromatography of the hydrolysates indicated 3-4 distinct fractions. Both the hydrolysates showed similar foam forming abilities, however, RH-1 exhibited poor foam stability. Emulsion properties of RH-1 were superior to that of RH-2. The major fractions eluted through gel filtration column were screened for antioxidant properties. Higher DPPH radical scavenging and metal chelating properties were observed for RH-1 second fragment, whereas FRAP and Fe(2+) reducing power was highest for second fragment of RH-2.
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| http://dx.doi.org/10.1007/s13197-015-1998-6 | DOI Listing |
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