Combining Alcalase hydrolysis and transglutaminase-cross-linking improved bitterness and techno-functional properties of hypoallergenic soybean protein hydrolysates through structural modifications

Abstract

Alcalase hydrolysis of soybean proteins was shown effective in degrading epitopes, but with a significant loss of tastes and functional properties. In this study, the combined use of controlled Alcalase hydrolysis and transglutaminase (TGase)-cross-linking was used to produce hypoallergenic soybean protein hydrolysates (SPHs) with improved flavor and techno-functional properties. Through establishing the kinetic model of heterogeneous enzymatic processes, SPHs with different degrees of hydrolysis (2.5–10.0%) were obtained and polymerized by TGase to yield products with various peptide components. Results showed that post-hydrolysis cross-linking rearranged the (poly)peptides in SPHs via glutaminyl modifications. Following TGase-treatments, due to the masking of bitter-active peptides and free amino acids, the bitterness of SPHs was significantly reduced with a slight improvement in the overall flavor. Furthermore, TGase–cross-linking rescued multiple techno-functionalities of SPHs, particularly their emulsifying and foaming properties. Using sera from soybean-allergic individuals, it was evidenced that TGase-addition did not generate neoallergens and the residual allergenicity of SPHs was not distinctly affected. The final products maintained 44–71% reduction in the IgE-binding levels in comparison to the unhydrolyzed protein. Combining limited Alcalase hydrolysis with TGase–cross-linking provides a feasible way to produce hypoallergenic soybean ingredients with desired flavor and functional attributes.