Abstract
The aim of this study was to investigate the bioactivity and functional properties of silver catfish (Pangasius sp.) muscle protein hydrolysate (SCMH) at different molecular size (3, 5 and 10 kDa) via ultrafiltration membrane. Bioactivity measures included angiotensin-converting enzyme (ACE) inhibitory activity and antioxidant activity (DPPH radical-scavenging activity, reducing power and Fe2+ chelating effects). The functional properties examined included emulsifying, foaming and solubility. There were significant differences (p < 0.05) in ACE inhibitory activity among the SCMH fractions, with the <3 kDa SCMH fraction showing the highest ACE inhibitory activity (87.68%). There were significant differences (p < 0.05) in DPPH radical-scavenging activities, reducing power and Fe2+ chelating effects among the different SCMH fractions. Fraction <3 kDa showed the highest DPPH radical-scavenging activities and reducing power, while fraction <10 kDa showed the highest chelating effect among all fractions (p < 0.05). In addition, there were no significant difference (p > 0.05) among all SCMH fractions in the emulsifying activity index. However, there were significant differences in terms of emulsifying stability index and foaming capacity properties (p < 0.05). Moreover, there was a significant difference (p > 0.05) among the SCMH fractions in terms of solubility. In conclusion, variations in the molecular size of the SCMH fractions showed a variety of potential applications for silver catfish protein hydrolysates in functional foods, as it possessed high bioactivity and good functional properties.
Published Version
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