Effects of trypsin-induced limited hydrolysis on the structural, functional, and bioactive properties of sericin.

The effects of trypsin-induced hydrolysis on the structural, functional, and antioxidant properties of sericin were studied. The structural properties of sericin and its hydrolysates were characterized by using SDS-PAGE, SEC-HPLC, surface hydrophobicity, and circular dichroism. Antioxidative properties were evaluated based on quenching capacity against hydroxyl, DPPH, and ABTS, and metal (Fe, Cu) chelating activity. The enzymatic hydrolysis raised the flexibility, changed emulsifying and foaming properties, and improved the solubility and antioxidant activity of sericin. Meanwhile, the hydrolysis led to a decline in gelation capacity, oil holding capacity, and water holding capacity. Sericin and its hydrolysates exhibited excellent function with regard to oil holding, emulsifying, and foaming. Sericin and its hydrolysates had clear effects on the growth of both and strains.