Heat-induced inactivation mechanism of soybean Bowman-Birk inhibitors

Abstract

Due to the complications of the soymilk system, the heat-induced Bowman-Birk inhibitor (BBI) inactivation mechanism is not well known. In this study, two BBI samples with low and high purities were prepared from soymilk. It was confirmed that three groups (A, C, and D) of BBI, which are contained in soybean seeds, were transferred into soymilk during processing. On heating, it was found that 1) the two subdomains of BBI were not equally heat stable, 2) the conformation of BBI gradually changed, 3) some amino acid residues (namely, cystine, serine and lysine) in BBI were degraded, 4) BBI did not tend to form intermolecular cross-links with another BBI, but did slightly with non-BBI proteins. Based on some previous studies, the conformational change of BBI was attributed to β-elimination reactions on the amino acid residues of BBI and the subsequent intramolecular reactions induced by the products yielded by the β-elimination reactions.

Keywords: Bowman-Birk inhibitors; Cystine-rich peptides; Disulfide bond; β-Elimination reaction.