α-淀粉酶活性在个体之间不同,并且受饮食行为和唾液成分的影响,但是关于α-淀粉酶活性与唾液成分之间关系的信息有限。这项研究调查了唾液蛋白对α-淀粉酶活性的影响,它们的各种相关性,粘蛋白(MUC5B和MUC7)和乳铁蛋白对α-淀粉酶酶动力学的影响,以及使用具有耗散的石英晶体微天平(QCM-D)技术和分子对接的这些相互作用的机理。结果表明,α-淀粉酶活性与MUC5B浓度呈显著正相关(R2=0.42,p<0.05),MUC7(R2=0.35,p<0.05),和乳铁蛋白(R2=0.35,p<0.05)。一项体外研究表明,通过降低α-淀粉酶的米氏常数(Km),粘蛋白和乳铁蛋白可以显着提高α-淀粉酶的活性。此外,QCM-D和分子对接的结果表明,粘蛋白和乳铁蛋白可以与α-淀粉酶相互作用,通过疏水相互作用形成稳定的α-淀粉酶-粘蛋白和α-淀粉酶-乳铁蛋白复合物,静电相互作用,范德华部队,和氢键。总之,这些结果表明,唾液α-淀粉酶的活性不仅取决于α-淀粉酶的含量,但也可以通过粘蛋白/乳铁蛋白与α-淀粉酶的相互作用来增强。
α-Amylase activity differs between individuals and is influenced by dietary behavior and salivary constituents, but limited information is available on the relationship between α-amylase activity and saliva components. This study investigated the impact of salivary proteins on α-amylase activity, their various correlations, the effect of mucin (MUC5B and MUC7) and lactoferrin on the enzymatic kinetics of α-amylase, and the mechanisms of these interactions using the quartz crystal microbalance with dissipation (QCM-D) technique and molecular docking. The results showed that α-amylase activity was significantly correlated with the concentrations of MUC5B (R2 = 0.42, p < 0.05), MUC7 (R2 = 0.35, p < 0.05), and lactoferrin (R2 = 0.35, p < 0.05). An in vitro study demonstrated that α-amylase activity could be significantly increased by mucins and lactoferrin by decreasing the Michaelis constant (Km) of α-amylase. Moreover, the results from the QCM-D and molecule docking suggested that mucin and lactoferrin could interact with α-amylase to form stable α-amylase-mucin and α-amylase-lactoferrin complexes through hydrophobic interactions, electrostatic interactions, Van der Waals forces, and hydrogen bonds. In conclusion, these findings indicated that the salivary α-amylase activity depended not only on the α-amylase content, but also could be enhanced by the interactions of mucin/lactoferrin with α-amylase.