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  • Title: Inactivation of Soybean Bowman-Birk Inhibitor by Stevioside: Interaction Studies and Application to Soymilk.
    Author: Liu C, Luo L, Wu Y, Yang X, Dong J, Luo F, Zou Y, Shen Y, Lin Q.
    Journal: J Agric Food Chem; 2019 Feb 27; 67(8):2255-2264. PubMed ID: 30729785.
    Abstract:
    In this work, the interaction of the soybean Bowman-Birk inhibitor (BBI) with stevioside (STE) was studied by stopped-flow-fluorescence and molecular docking. STE's inactivation of protease-inhibitor activities in soymilk and the influence of STE addition on the sensory character of soymilk were also evaluated. The results indicate that STE binds BBI with a binding constant ( Ka) of 3.38 × 105 L mol-1 to form a 1:1 complex. The docking study reveals that two hydrogen bonds are formed between the side-chain of Lys16 (reactive site 1) of BBI and the glucose-ring hydroxyl groups of STE, which may block BBI from contacting trypsin and thus deactivate the trypsin-inhibitor activity (TIA) of BBI. Moreover, the residual TIA in soymilk could also be inactivated by STE. A mixture of 159 mg/L STE and 60 g/L sucrose could be used for sweetening soymilk without affecting the sensory characteristics when compared to a reference product sweetened with 9% sucrose.
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