FOOD CHEMISTRY
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2025
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IF 9.8
Qiaoli Yang,Yaping Wang
This research developed an electrochemical biosensor based on T4 bacteriophages assembled with beta-galactosidase (β-gal) for Escherichia coli K12 ( E. coli K12) detection. The β-gal Soc fusion proteins were affinity-assembled on the Hoc − Soc − T4 phage capsid, exhibiting superior substrate affinity and enhanced stability compared to the free enzyme. The antibodies were immobilized on the multiwalled carbon nanotube/gold nanoparticle modified electrode, and then the engineered β-gal T4 was bonded the bacterial cells captured by the antibodies, constructing the electrochemical biosensor. The biosensor can detect E. coli K12 as low as 6 CFU/mL within 90 mins utilizing catalytic events of β-gal T4. The biosensor exhibited high specificity, distinguishing live target bacteria from non-target bacteria or dead target bacteria, which is attributed to its dual recognition mechanism involving antibody and β-gal T4. The biosensing platform can be extended to other bacteria by customizing phage-enzyme combinations, enabling bacterial detection in food, environment and other fields.
研究领域:
微生物学
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生物传感技术
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分子生物学
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DOI
PubMed
高影响因子
CURRENT MICROBIOLOGY
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2025
·Vol. 82
·期 6
·1-10
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IF 2.6
Zhang Pei,Yang Huanggen,Ahmad Malik Taj,Zheng Qi,Nie Guochao,Ahmad Ayesha,Raza Muslim,Raza Saleem
Biofilm formation presents significant challenges in healthcare, food processing, and water treatment, contributing to antibiotic resistance and persistent infections. Effective strategies to combat biofilm-associated infections are urgently needed. This study introduces a novel approach to biofilm removal by bio-functionalizing T4 bacteriophage with modified Fe 3 O 4 nanoparticles (NPs) and Nisin, an antibacterial peptide, to form the Fe 3 O 4 -Phage-T4 + Nisin complex. The aim is to enhance antimicrobial efficacy and biofilm eradication. The Fe 3 O 4 -Phage-T4 + Nisin complex was synthesized by conjugating T4 bacteriophage with modified Fe 3 O 4 NPs and Nisin. The antimicrobial and antibiofilm activity of the complex was evaluated against multidrug-resistant Pseudomonas aeruginosa strains ( PA01 and PA14 ) using biofilm inhibition and eradication assays. Stability and efficacy were further tested across a pH range of 5 to 8. The Fe₃O₄-Phage-T4 + Nisin complex exhibited superior biofilm removal compared to its individual components. The integration of Nisin broadened the antibacterial spectrum, targeting both Gram-positive and Gram-negative bacteria , while the modified Fe₃O₄ NPs enhanced phage penetration and bacterial cell disruption. The complex demonstrated significant biofilm inhibition and eradication, addressing the challenge of biofilm-related antibiotic tolerance, which often necessitates high antibiotic doses. Additionally, it maintained stability and efficacy across varying pH conditions.
研究领域:
微生物学
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生物技术
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医药科学
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DOI
PubMed
高影响因子
CHEMICAL ENGINEERING JOURNAL
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2024
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IF 13.3
Xiao-Lin Hou,Lin-Fang Tan,Xiao-Ting Xie,Bin Zhang,Qiong Wang,Kai Cheng,Jin-Xuan Fan,Tian-Cai Liu,Bo Liu
The peroxisome is an important organelle for H 2 O 2 metabolism and O 2 redistribution in organisms. Drawing inspiration from this biochemical pathway, a T4-Ce6-Cat-Lox (TCCL) simpler biomimetic peroxisome was constructed using the T4 phage’s Soc and Hoc sites to enhance photodynamic therapy (PDT). The cascading catalytic system of lactate oxidase (Lox) and catalase (Cat) was displayed on the phage architecture through in vitro phage display technology. 720 Lox molecules and 95 Cat molecules displayed on the T4 phage can be precisely controlled by the feed concentration. The enzymatic reaction of Lox, triggered by lactic acid in the tumor microenvironment, generated H 2 O 2 at the Soc site. Subsequently, the H 2 O 2 was decomposed into O 2 by Cat at the Hoc site. By manipulating the cascading catalytic system ratio of Lox and Cat to 7.5:1, the ROS generation efficiency of Ce6 was as high as 99.2 %, and the tumor inhibition rate reached 91.25 %. More importantly, the TCCL was constructed by natural T4 nanocarrier, exhibiting good biocompatibility and low immunogenicity in vivo . This study explored the construction of a simplified biomimetic peroxisome using the T4 phage display technology and provided a promising strategy for cascading catalytic system construction.
研究领域:
生物医学工程
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肿瘤学
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酶工程
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DOI
高影响因子
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
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2025
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IF 3.3
Wu Dan,Khan Sulaiman,Zhang Shujie,Wang Huan,Chen Wei,Wang Shenqi
Enzymes, key catalysts in biochemical reactions, are prone to denaturation under harsh conditions, leading to reduced stability and higher costs. Enzyme immobilization, using carriers like magnetic nanoparticles, metal–organic frameworks, and viruses, is a common solution. T4 bacteriophage, a virulent E. coli phage containing 155 Hoc and 870 Soc proteins, offers a cost-effective and highly stable platform for enzyme immobilization. In this study, Soc-β-galactosidase (Soc-β-gal) was immobilized on the surface of T4 bacteriophage via affinity fixation and further encapsulated with a metal-polyphenol network (MPN) coating. Comparative analysis of the biochemical properties revealed that the immobilized enzyme, β-gal T4, retained over 85% activity after 6 h at 50 °C, while free Soc-β-gal retained only 40.63%. Moreover, β-gal T4@TA-Ti demonstrated superior stability, retaining 92.88% of its activity after 6 h of UV exposure, compared to 10.21% for β-gal T4 and 7.23% for Soc-β-gal. The MPN coating also enhanced resistance to proteolytic degradation, with β-gal T4@TA-Ti retaining 9.48% of its activity after exposure to proteinase K, in contrast to 4.62% for β-gal T4. Overall, these results demonstrate that enzyme immobilization significantly enhances stability, while the MPN coating further improves resistance to extreme pH, ultraviolet radiation, and other environmental stressors, highlighting the potential of this approach for biocatalytic applications.
研究领域:
生物化学
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酶工程
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材料科学
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DOI
PubMed
高影响因子
SENSORS AND ACTUATORS B-CHEMICAL
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2022
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IF 9.221
Jingjing Xu,Qiaoli Yang,Pei Wang,Dan Wu,Xiaohan Yang,Wei Chen,Song Gao,Shenqi Wang
Due to the highly efficient and specific catalysis , enzymes have been extensively applied in various fields. In the development of enzyme-based sensing devices, the immobilization of enzyme is critical for achieving superior performance which is drastically dependent on enzyme stability and activity. In this study, we construct and assemble the beta-galactosidase( β -gal)-Soc fusion proteins onto biologically produced nanoparticle – T4 phage in vitro as a specific sensing probe for the rapid colorimetric detection of Escherichia coli K12. The stability and substrate affinity of β -gal assembled on T4 phage were largely enhanced in comparison with that of free β -gal due to this affinity-based immobilization, and the assay based on this β -gal T4 phage was able to quantify bacteria at concentration of 10 3 cfu mL −1 in drink water within 2 h. This affinity binding based enzyme immobilization strategy employed T4 bacteriophage capsid as the supporting nanoparticle and exhibited enhanced enzyme activity and stability which are highly favored for the future development of sensing applications.
研究领域:
生物技术
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酶学
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微生物学
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纳米技术
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DOI
高影响因子
NANOTECHNOLOGY
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2022
·Vol. 33
·期 16
·165102
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IF 3.953
Weilun Sun,Jingjing Xu,Bo Liu,Yuan-Di Zhao,Ling Yu,Wei Chen
Phage is a promising therapeutic agent for treating antibiotic resistant bacteria. However, in the process of treatment, phage may be cleared by the immune system and cleaved by protease, which could affect the efficacy of phage. In order to solve the above problems, phage encapsulation is usually adopted. In this study, we employed metal phenolic network (MPN) for efficient phage encapsulation which could protect phage from the cleavage of protease, and keep cytotoxicity weak. In the model of skin wound infection, the encapsulated phage could be released in response to pH change to achieve good antibacterial effect. Furthermore, the MPN encapsulation could prolong the T4 phage residence time at the wound. Our findings suggest that MPN can be a promising material for phage encapsulation.
研究领域:
药学
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生物技术
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微生物学
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材料科学
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产品关联
DOI
PubMed
高影响因子
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