Exploring the antimicrobial potential of hybrid endolysin L4-GS-C111 for the control of Bacillus cereus in food systems

IF 5.9 1区农林科学 Q1 FOOD SCIENCE & TECHNOLOGY

Food Bioscience Pub Date : 2026-04-01 Epub Date: 2026-02-11 DOI:10.1016/j.fbio.2026.108470

Siyoung Yoo , Nanjoo Park , Junsik Hwang , Min-Duk Seo , Hyunjin Yoon

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Abstract

Bacillus cereus is a major foodborne pathogen with limited effective control strategies. To enhance antibacterial efficacy against B. cereus, hybrid endolysins were engineered by fusing the enzymatically active domain (EAD) of LysB4 with those of CD27L and PHICD111_20024, amidase-type endolysins derived from Clostridioides difficile phages. All recombinant proteins were successfully expressed in Escherichia coli and retained their bacteriolytic activity. Among the four hybrid constructs, L4-GS-C111 and C111-GS-L4 exhibited stronger bactericidal activity against Bacillus species than that of their parental forms. Structural modeling predicted that the active sites of each endolysin were accessible in both L4-GS-C111 and C111-GS-L4, suggesting enhanced activity. Both constructs maintained stable lytic activity across a wide pH range (4.5–9.5) and varying NaCl concentrations (0–150 mM), outperforming LysB4_EAD under various changes in pH and salinity. L4-GS-C111 successfully inactivated B. cereus in soymilk with pH 6.5 and 15 mM NaCl, achieving a 4 log decrease within 12 h at 40 μM. L4-GS-C111 also effectively disrupted preformed B. cereus biofilms, as confirmed by confocal microscopy, but barely displayed any cytotoxicity toward Caco-2 cells. These results demonstrate that L4-GS-C111 exerts bactericidal activity against B. cereus in diverse environments, supporting its potential as a biocontrol agent for improving food safety.

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探讨杂交内溶素L4-GS-C111对食品中蜡样芽孢杆菌的抑菌潜力

蜡样芽孢杆菌是一种主要的食源性致病菌，有效的防治策略有限。为了提高对蜡样芽孢杆菌的抑菌效果，将LysB4的酶活性结构域（EAD）与艰难梭菌噬菌体衍生的酶活性结构域（CD27L）和PHICD111_20024的酶活性结构域（EAD）融合，构建了杂交内溶素。所有重组蛋白均在大肠杆菌中成功表达，并保持其溶菌活性。在4个杂交组合中，L4-GS-C111和C111-GS-L4对芽孢杆菌的杀菌活性较亲本菌株强。结构模型预测，L4-GS-C111和C111-GS-L4中每个内溶素的活性位点都可以到达，表明活性增强。两种构建体在较宽的pH范围（4.5-9.5）和不同的NaCl浓度（0-150 mM）下都保持稳定的裂解活性，在不同的pH和盐度变化下都优于LysB4_EAD。L4-GS-C111在pH为6.5、NaCl为15 mM的条件下成功灭活了豆浆中的蜡样芽孢杆菌，在40 μM条件下，12 h内灭活了4倍对数。共聚焦显微镜证实，L4-GS-C111也能有效地破坏预先形成的蜡样芽孢杆菌生物膜，但对Caco-2细胞几乎没有细胞毒性。这些结果表明，L4-GS-C111在不同环境下对蜡样芽孢杆菌具有杀菌活性，支持其作为提高食品安全的生物防治剂的潜力。

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来源期刊

Food Bioscience Biochemistry, Genetics and Molecular Biology-Biochemistry

CiteScore

6.40

自引率

5.80%

发文量

671

审稿时长

27 days

期刊介绍： Food Bioscience is a peer-reviewed journal that aims to provide a forum for recent developments in the field of bio-related food research. The journal focuses on both fundamental and applied research worldwide, with special attention to ethnic and cultural aspects of food bioresearch.