Microbial enzymes as powerful natural anti-biofilm candidates
Bacterial biofilms pose significant challenges, from healthcare-associated infections to biofouling in industrial systems, resulting in significant health impacts and financial losses globally. Classic antimicrobial methods often fail to eradicate sessile microbial communities within biofilms, requiring innovative approaches. This review explores the structure, formation, and role of biofilms, highlighting the critical importance of exopolysaccharides in biofilm stability and resistance mechanisms. We emphasize the potential of microbial enzymatic approaches, particularly focusing on glycosidases, proteases, and deoxyribonucleases, which can disrupt biofilm matrices effectively. We also delve into the importance of enzymes such as cellobiose dehydrogenase, which disrupts biofilms by degrading polysaccharides. This enzyme is mainly sourced from Aspergillus niger and Sclerotium rolfsii, with optimized production strategies enhancing its efficacy. Additionally, we explore levan hydrolase, alginate lyase, α-amylase, protease, and lysostaphin as potent antibiofilm agents, discussing their microbial origins and production optimization strategies. These enzymes offer promising avenues for combating biofilm-related challenges in healthcare, environmental, and industrial settings. Ultimately, enzymatic strategies present environmentally friendly solutions with high potential for biofilm management and infection control.
Funding
Open access funding provided by The Science, Technology & Innovation Funding Authority (STDF) in cooperation with The Egyptian Knowledge Bank (EKB)
History
Data Availability Statement
No datasets were generated or analysed during the current study.Comments
The original article is available at https://microbialcellfactories.biomedcentral.com/Published Citation
Al-Madboly LA, Aboulmagd A, El-Salam MA, Kushkevych I, El-Morsi RM. Microbial enzymes as powerful natural anti-biofilm candidates. Microb Cell Fact. 2024;23(1):343.Publication Date
23 December 2024External DOI
PubMed ID
39710670Department/Unit
- School of Pharmacy and Biomolecular Sciences
Publisher
BioMed Central LtdVersion
- Published Version (Version of Record)