Abstract
This study evaluated the effects of different concentrations of green lentil acetone extract (GLA) (250, 500, 750, and 1000 μg/mL) and protein of green lentil (PGL) (1, 2, 3, and 4 g/100 g MP) on the functional attributes of myofibrillar protein (MP). GLA extract and PGL significantly affected the structure of MP by decreasing the carbonyl and sulfhydryl contents. Intrinsic fluorescence quenching studies showed that static quenching was involved in MP-GLA extract and MP-PGL complexes. Compared to the control (MP), the addition of GLA extract and PGL decreased the surface hydrophobicity, which correlated with the decrease in protein solubility. The MP-GLA and MP-PGL had lower cooking losses and slightly higher water-holding capacities P < 0.05 . FTIR spectroscopy demonstrated changes in MP secondary structure with the addition of GLA extract and PGL. GLA extract and PGL also decreased the thermal stability of MP and showed significant synergism in enhancing the radical scavenging activity of MP. Taken together, the results indicated that a high concentration of GLA extract (1000 μg/mL) and PGL (4 g/100 g MP) improved the functional properties of MP, and GLA extract was the most effective.
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