Abstract
In this study, transglutaminase (TGase) was introduced into soybean protein isolate (SPI) and its major fractions, 7S and 11S globulins combined proteins (CP), and the effects of TGase on the physicochemical properties of SPI and CP films were explored in pH values of 5.0, 6.0, 7.0, and 8.0. The results suggested that TGase facilitated the conversion of β-turn and random coil to β-sheet structure in protein films, resulting in a more ordered and table protein network. Homogeneous and dense microscopic films were observed and resulted in a reduction of over 20% in the water vapor permeability (WVP) for both TGase-modified SPI and CP films. However, the effect of enzymatic action also greatly depends on the regulation of protein conformation by pH environment. The tensile strength of CP films prepared at pH 6.0 modified by TGase increased by more than 26% (from 6.21 MPa to 7.87 MPa), and the elongation of all film samples prepared at pH 7.0 and 8.0 modified by TGase increased by more than 76% (from 16.25%–19.24% to 33.92%–36.35%). Consequently, it is proposed that the mechanism of TGase-catalyzed film formation of soybean protein is related to the catalytic affinity of TGase for different subunits and the type of crosslinks formed. This aims to provide a valuable theoretical reference for the rational application of crosslinkers in protein-based products.
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