伴大豆球蛋白酶解肽抑菌活性研究

Antibacterial activity of peptides from hydrolyzed soybean conglycinin

建立伴大豆球蛋白酶解产生抑菌肽的最适条件,对酶解产物进行分离纯化后进一步测定其抑菌活性。采用复合风味蛋白酶水解伴大豆球蛋白,测定不同时间的酶解液对大肠杆菌和金黄色葡萄球菌的抑菌活性。结果显示:2 h水解产生的酶解肽具有抑菌活性,其对大肠杆菌和金黄色葡萄球菌的最小抑菌浓度分别是2.6和3.2 mg/mL。2 h水解液经Sephadex-G15分离纯化,采用平板计数法鉴定各组分。结果显示:CP2组分对大肠杆菌具有显著的抑制作用(P<0.05)。本研究证明伴大豆球蛋白的复合风味蛋白酶酶解肽具有一定的抑菌活性。

The study is aimed to establish the optimum conditions under which conglycinin can be hydrolyzed to produce the peptides, and then to purify the peptide and determine its antibacterial activity. The peptides were prepared by hydrolyzing conglycinin with flavourzyme. The 2h hydrolysates had exhibited good inhibitory activities to Escherichia coli and Staphylococcus aureus. The minimal inhibitory concentra- tions （MICs） against E. coli and S. aureus were 2.6 mg/mL and 3.2 mg/mL, respectively. Components of the 2 h hydrolysates were further separated using Sephadex-G15 gel filtration chromatography. The results of bacterial growth assays showed that CP2 had the maximum growth inhibitory activity to E. coli（P〈0.05）. It suggested that the hydrolysates from conglycinin exhibited significant inhibitory activities to E. coli and S. aureus.