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针对生物膜的降解酶之间明显缺乏协同作用。

An apparent lack of synergy between degradative enzymes against biofilms.

作者信息

Ellis Jeremy R, Rowley Paul A

机构信息

University of Idaho, Department of Biological Sciences, Moscow, ID 83844, USA.

Johns Hopkins University, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

出版信息

bioRxiv. 2023 Oct 5:2023.10.05.561034. doi: 10.1101/2023.10.05.561034.

DOI:10.1101/2023.10.05.561034
PMID:37873330
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10592981/
Abstract

The use of enzymes represents an approach to combat bacterial infections by degrading extracellular biomolecules to disperse biofilms. Commercial enzyme preparations, including cellulase, amylase, pectinase, zymolyase, and pepsin, exhibit concentration-dependent dispersion of biofilms. Here, we report that low concentrations of these enzymes generally lack synergy when combined or added together sequentially to biofilms. Only the addition of a protease (pepsin) followed by a commercial mixture of degradative enzymes from (zymolyase 20T), demonstrated synergy and was effective at dispersing biofilms. A more purified mixture of enzymes (zymolyase 100T) showed improved dispersal of biofilms compared to zymolyase 20T but lacked synergy with pepsin. This study emphasizes the complexity of enzymatic biofilm dispersal and the need for tailored approaches based on the properties of degradative enzymes and biofilm composition.

摘要

使用酶是一种通过降解细胞外生物分子来分散生物膜从而对抗细菌感染的方法。商业酶制剂,包括纤维素酶、淀粉酶、果胶酶、酵母裂解酶和胃蛋白酶,表现出生物膜浓度依赖性分散。在此,我们报告,当这些酶以组合或顺序添加到生物膜中时,低浓度通常缺乏协同作用。只有先添加蛋白酶(胃蛋白酶),然后添加来自酵母的商业降解酶混合物(酵母裂解酶20T),才表现出协同作用并能有效分散生物膜。与酵母裂解酶20T相比,更纯化的酶混合物(酵母裂解酶100T)显示出更好的生物膜分散效果,但与胃蛋白酶缺乏协同作用。本研究强调了酶促生物膜分散的复杂性以及基于降解酶特性和生物膜组成采取定制方法的必要性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6d66/10592981/56f15383384b/nihpp-2023.10.05.561034v1-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6d66/10592981/1aabb0e708c6/nihpp-2023.10.05.561034v1-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6d66/10592981/4c4cf8dd0638/nihpp-2023.10.05.561034v1-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6d66/10592981/56f15383384b/nihpp-2023.10.05.561034v1-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6d66/10592981/1aabb0e708c6/nihpp-2023.10.05.561034v1-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6d66/10592981/4c4cf8dd0638/nihpp-2023.10.05.561034v1-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6d66/10592981/56f15383384b/nihpp-2023.10.05.561034v1-f0003.jpg

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本文引用的文献

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The Pseudomonas aeruginosa Biofilm Matrix Protein CdrA Has Similarities to Other Fibrillar Adhesin Proteins.铜绿假单胞菌生物膜基质蛋白 CdrA 与其他纤维状粘附蛋白具有相似性。
J Bacteriol. 2023 May 25;205(5):e0001923. doi: 10.1128/jb.00019-23. Epub 2023 Apr 26.
2
Fungal Glycoside Hydrolases Display Unique Specificities for Polysaccharides and Biofilms.真菌糖苷水解酶对多糖和生物膜具有独特的特异性。
Microorganisms. 2023 Jan 23;11(2):293. doi: 10.3390/microorganisms11020293.
3
Evaluation of antibiofilm potential of four-domain α-amylase from Streptomyces griseus against exopolysaccharides (EPS) of bacterial pathogens using Danio rerio.
利用斑马鱼评价灰色链霉菌四域 α-淀粉酶抗细菌病原体胞外多糖(EPS)的生物膜潜力。
Arch Microbiol. 2022 Apr 5;204(5):243. doi: 10.1007/s00203-022-02847-4.
4
In vitro activities of cellulase and ceftazidime, alone and in combination against Pseudomonas aeruginosa biofilms.纤维素酶和头孢他啶单独及联合对铜绿假单胞菌生物膜的体外活性。
BMC Microbiol. 2021 Dec 16;21(1):347. doi: 10.1186/s12866-021-02411-y.
5
Efficient Biofilms Eradication by Enzymatic-Cocktail of Pancreatic Protease Type-I and Bacterial α-Amylase.通过I型胰蛋白酶和细菌α-淀粉酶的酶混合物有效根除生物膜
Polymers (Basel). 2020 Dec 17;12(12):3032. doi: 10.3390/polym12123032.
6
Differential Efficacy of Glycoside Hydrolases to Disperse Biofilms.糖苷水解酶对生物膜的分散作用的差异效果
Front Cell Infect Microbiol. 2020 Jul 24;10:379. doi: 10.3389/fcimb.2020.00379. eCollection 2020.
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A novel multi-enzyme preparation produced from Aspergillus niger using biodegradable waste: a possible option to combat heterogeneous biofilms.一种利用可生物降解废物由黑曲霉生产的新型多酶制剂:对抗异质生物膜的一种可能选择。
AMB Express. 2020 Feb 21;10(1):36. doi: 10.1186/s13568-020-00970-3.
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Langmuir. 2020 Feb 18;36(6):1585-1595. doi: 10.1021/acs.langmuir.9b02188. Epub 2020 Feb 7.
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Sci Rep. 2019 Nov 8;9(1):16284. doi: 10.1038/s41598-019-52726-0.
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Nat Phys. 2019 Apr 26;15(3):251-256. doi: 10.1038/s41567-018-0356-9. Epub 2018 Nov 26.