Isolation of a New Agar Degrading Bacterium, Maribacter sp. SH-1 and Characterization of its Agarase

Lee, Chang-Eun; Lee, Sol-Ji; Lee, Dong‐Geun; Lee, Sang-Hyeon

doi:10.4014/mbl.1511.11007

Cited by 2 publications

(1 citation statement)

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“…To date, the majority of published work on the genus Maribacter has been related to the description of new species, the deposition of genomic sequences or their interactions with macroalgae, but with only a small number of Maribacter spp. enzymes being specifically characterized, primarily for their ability to degrade polysaccharides (Lee et al., 2016 ; Lu et al., 2022 ). To our knowledge, there are no reports describing other types of enzymes from Maribacter species, for example, those with activity towards ester and polyester substrates.…”

Section: Resultsmentioning

confidence: 99%

Identification and expression of MarCE, a marine carboxylesterase with synthetic ester‐degrading activity

Carr,

Göttsch,

de Oliveira

et al. 2024

Microbial Biotechnology

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Carboxylic ester hydrolases with the capacity to degrade polyesters are currently highly sought after for their potential use in the biological degradation of PET and other chemically synthesized polymers. Here, we describe MarCE, a carboxylesterase family protein identified via genome mining of a Maribacter sp. isolate from the marine sponge Stelligera stuposa. Based on phylogenetic analysis, MarCE and its closest relatives belong to marine‐associated genera from the Cytophaga–Flavobacterium–Bacteroides taxonomic group and appear evolutionarily distinct to any homologous carboxylesterases that have been studied to date in terms of structure or function. Molecular docking revealed putative binding of BHET, a short‐chain PET derivative, onto the predicted MarCE three‐dimensional structure. The synthetic ester‐degrading activity of MarCE was subsequently confirmed by MarCE‐mediated hydrolysis of 2 mM BHET substrate, indicated by the release of its breakdown products MHET and TPA, which were measured, respectively, as 1.28 and 0.12 mM following 2‐h incubation at 30°C. The findings of this study provide further insight into marine carboxylic ester hydrolases, which have the potential to display unique functional plasticity resulting from their adaptation to complex and fluctuating marine environmentsw.

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Section: Resultsmentioning

confidence: 99%