Raw data used to generate Table 1.

This research examines the enzymatic modification of lysozyme, a glycosidic hydrolase that has restricted effectiveness against Gram-negative bacteria, in order to produce bioactive peptide fractions with improved antibacterial and physicochemical characteristics. Utilizing chicken egg lysozyme, modifications were performed in controlled settings with proteolytic enzymes, mainly pepsin, and experiments with a pepsin-trypsin ratio. The modification methods sought to improve the hydrophobic nature of lysozyme’s surface, create oligomeric and peptide forms, and decrease immunogenicity. Findings showed that raising pepsin concentration enhanced the creation of peptide fractions, increasing surface hydrophobicity while reducing hydrolytic and antioxidant activities. Increased hydrophobicity and reduced enzyme activity were linked to enhanced antibacterial effectiveness, particularly against Gram-negative bacteria, a characteristic absent in natural lysozyme. Additionally, the research noted a decrease in immunoreactivity as pepsin concentrations increased, achieving the lowest antibody response in optimized formulations. This enzymatic method offers an economical way to create lysozyme derivatives that hold considerable promise for wider applications, particularly in scenarios where lower immunoreactivity and a prolonged antibacterial spectrum are needed.

本研究针对溶菌酶（lysozyme）——一种对革兰氏阴性菌（Gram-negative bacteria）抗菌效果受限的糖苷水解酶（glycosidic hydrolase）——开展酶法改性研究，以期制备兼具更优抗菌与理化特性的生物活性肽组分。本研究以鸡蛋清溶菌酶为原料，在可控条件下采用以胃蛋白酶（pepsin）为主的蛋白水解酶进行改性，并开展了胃蛋白酶与胰蛋白酶（trypsin）配比相关实验。该改性策略旨在提升溶菌酶表面疏水性、构建寡聚体与肽类形式，并降低其免疫原性。研究结果显示，提高胃蛋白酶浓度可促进肽组分的生成，在提升溶菌酶表面疏水性的同时，降低了其水解活性与抗氧化活性。表面疏水性增强与酶活性降低，与更优异的抗菌效能相关，尤其是针对天然溶菌酶无法有效作用的革兰氏阴性菌。此外，研究发现随着胃蛋白酶浓度升高，免疫反应性随之降低，在优化配方中可实现最低的抗体应答水平。该酶法改性手段为制备溶菌酶衍生物提供了一种经济高效的途径，这类衍生物在需要低免疫原性与更广抗菌谱的场景中展现出可观的应用前景。