New dienelactone hydrolase from microalgae bacterial community-Antibiofilm activity against fish pathogens and potential applications for aquaculture.

Bibliographic Details
Title: New dienelactone hydrolase from microalgae bacterial community-Antibiofilm activity against fish pathogens and potential applications for aquaculture.
Authors: Bergmann, Lutgardis1 (AUTHOR), Balzer Le, Simone2 (AUTHOR), Hageskal, Gunhild2 (AUTHOR), Preuss, Lena1 (AUTHOR), Han, Yuchen1 (AUTHOR), Astafyeva, Yekaterina1 (AUTHOR), Loevenich, Simon2 (AUTHOR), Emmann, Sarah3 (AUTHOR), Perez-Garcia, Pablo3 (AUTHOR), Indenbirken, Daniela4 (AUTHOR), Katzowitsch, Elena5 (AUTHOR), Thümmler, Fritz5 (AUTHOR), Alawi, Malik6 (AUTHOR), Wentzel, Alexander2 (AUTHOR), Streit, Wolfgang R.1 (AUTHOR), Krohn, Ines1 (AUTHOR) ines.krohn@uni-hamburg.de
Source: Scientific Reports. 1/3/2024, Vol. 13 Issue 1, p1-13. 13p.
Subject Terms: *FISH pathogens, *MICROALGAE, *AQUATIC resources, *VIBRIO anguillarum, *EDWARDSIELLA, *AQUACULTURE, *BIOFILMS
Abstract: Biofilms are resistant to many traditional antibiotics, which has led to search for new antimicrobials from different and unique sources. To harness the potential of aquatic microbial resources, we analyzed the meta-omics datasets of microalgae-bacteria communities and mined them for potential antimicrobial and quorum quenching enzymes. One of the most interesting candidates (Dlh3), a dienelactone hydrolase, is a α/β-protein with predicted eight α-helices and eight β-sheets. When it was applied to one of the major fish pathogens, Edwardsiella anguillarum, the biofilm development was reproducibly inhibited by up to 54.5%. The transcriptome dataset in presence of Dlh3 showed an upregulation in functions related to self-defense like active genes for export mechanisms and transport systems. The most interesting point regarding the biotechnological potential for aquaculture applications of Dlh3 are clear evidence of biofilm inhibition and that health and division of a relevant fish cell model (CHSE-214) was not impaired by the enzyme. [ABSTRACT FROM AUTHOR]
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ISSN:20452322
DOI:10.1038/s41598-023-50734-9
Published in:Scientific Reports
Language:English