小麦蛋白酶解物的分离及其体外抗菌作用的研究

Separation and Antimicrobial Activity of Hydrolysates from Wheat Protein

采用碱性蛋白酶水解小麦面筋蛋白制备抗菌肽,再依次采用超滤处理、Sephadex G-25凝胶层析和反相高效液相色谱,从小麦面筋蛋白酶解产物中分离抗菌肽,并研究其体外抑菌作用。结果表明,经过超滤处理后,相对分子量在5 kDa以下的酶解物抑菌活性较好,随后其经过SephadexG-25凝胶层析得到4种组分,抑菌试验表明,其中相对分子量为2 036 Da的峰Ⅱ组分的抑菌效果最好,对大肠杆菌的抑菌率为20.6%,对金黄色葡萄球菌的抑菌率为20.1%。峰Ⅱ组分经过反相高效液相色谱鉴定,得到4个多肽组分。

In this paper, wheat gluten protein is hydrolyzed by Alcalase protease, wheat gluten protein hydrolysates is processed by nltrafihration, Sephadex G-25 gel chromatography and phase high performance liquid ehromatograpby is reversed, and the inhibition in vitro is studied. The results show that after uhrafihration, the molecular weight of hydrolysates in 5 kDa show a good antibacterial activity, followed by Sephadex G-25 gel chromatography, it is classified into four components, antimicrobial test shows that peak II has the highest antibacterial ability, which molecular weight of 2 036 Do, the inhibition rate of E. coli is 20.6%, S. aureus is 20.1%, Peak II components is identified by RP-HPLC to four polypeptide components.