SDS-PAGE showed an irreducible aggregation of mulberry polyphenols with proteins. 
SDS-PAGE
Fluorescence spectroscopy and FT-IR analysis manifested that mulberry polyphenols promoted the unfolding of protein structure and the transformation of α-helix to β-turn structure. 
Fluorescence spectroscopy
Fluorescence spectroscopy and FT-IR analysis manifested that mulberry polyphenols promoted the unfolding of protein structure and the transformation of α-helix to β-turn structure. 
FT-IR analysis
Scanning electron microscopy (SEM) observed that oxidation with polyphenols facilitated the cross-linking and aggregation of MP more tightly. 
Scanning electron microscopy (SEM)