| iopolymers were prepared by cross-linking whey protein isolate (WPI) and soybean 11S globulin (11S) using transglutaminase (TG). Solubility, emulsification, hydrophobicity and foaming properties of the biopolymers were examined. Differential scanning calorimetry (DSC) was used to determine thermal properties of proteins and biopolymers. Partial purification of biopolymers was carried out using Sepharose 4B column. The extent of polymerization was determined by electrophoresis and HPLC. Ultraviolet (UV) and fluorescence spectra were used to analyze structural changes of biopolymers.;SDS-PAGE showed bands corresponding to high-molecular-weight components (MW ;Heterogeneity of biopolymers was determined by cross-linking acetylated-11S acidic subunits (Ac-11S) of soy protein with ;Protein films were produced from WPI, 11S and a mixture of these two proteins (1:1, wt/wt) using TG catalysis. Solubility of TG cross-linked films was lower than that of control films at pH 3.0, 4.0, 6.0 and 8.0. Solubility of control films in 6.6 M urea and in 10% SDS was higher than that of TG cross-linked films. Hydrolysis of control and TG cross-linked films by trypsin and... |
