Food Quality and Safety Management, Poznan University of Life Science, Poznan, Poland.
PLoS One. 2019 Feb 28;14(2):e0213021. doi: 10.1371/journal.pone.0213021. eCollection 2019.
Lysozyme is a type of enzymatic protein found in a wide range of organisms. Among the many applications of lysozyme, the antibacterial activity features caused by the hydrolysis of 1-4 glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine of gram-positive bacteria are beneficial in the food industry, medicine, trade, and pharmacology. Studies have indicated that specific modifications of lysozyme cause oligomerization of the enzyme, and the resulting dimer, which also undergoes changes in physicochemical properties, shows greater total antibacterial activity. Among these modifications, thermo-chemical methods are one of the most important groups. In this study, the microwave method of the enzyme heating with the associated process of enzyme oxidation was used as a novel thermo-chemical method to induce lysozyme oligomerization. The research shows that using this new method can produce enzymatic preparations composed of approximately 58.9% oligomers, including 33.5% dimer and 25.4% trimer under a hydrogen peroxide concentration of 4% and pH of 8. The maximum percentage of lysozyme dimer of 39.4% was obtained at pH 6.0 with the addition of 2% oxidant. In addition, as a result of the modification process, the hydrolytic activity and surface hydrophobicity of the enzyme were changed.
溶菌酶是一种存在于多种生物中的酶蛋白。在溶菌酶的众多应用中，其水解阳性细菌中 N-乙酰胞壁酸和 N-乙酰葡萄糖胺之间 1-4 糖苷键所产生的抗菌活性特征在食品工业、医药、贸易和药理学中具有益处。研究表明，溶菌酶的特定修饰会导致酶的寡聚化，而形成的二聚体，其理化性质也会发生变化，表现出更大的总抗菌活性。在这些修饰中，热化学方法是最重要的方法之一。在这项研究中，使用酶氧化相关过程的微波酶加热方法作为一种新的热化学方法来诱导溶菌酶的寡聚化。研究表明，使用这种新方法可以在 4%过氧化氢浓度和 8.0 pH 下产生约 58.9%寡聚物的酶制剂，其中包括 33.5%二聚体和 25.4%三聚体。在 pH 6.0 下添加 2%氧化剂时，获得了最大的 39.4%溶菌酶二聚体百分比。此外，由于修饰过程，酶的水解活性和表面疏水性发生了变化。
