Analysis of manganese oxidase and its encoding gene in Lysinibacillus strain MK-1

Tang, Wenwei; Liu, Yunying; Gong, Jiemin; Chen, Shichao; Zeng, Xin

doi:10.1016/j.psep.2019.04.002

Cited by 15 publications

(8 citation statements)

References 45 publications

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“…To determine a possible phylogenetic relationship between manganese-oxidizing multicopper oxidases (MO-mco) and non-manganese oxidizing multicopper oxidases (non-MO-mco), we created a dataset sequences of multicopper oxidases with experimental evidence of Mn 2+ oxidation [ 47 – 49 , 53 , 134 , 135 ] and multicopper oxidases with experimental evidence of non-Mn 2+ oxidation activity [ 47 , 54 ] and included our sequences. They were aligned using MUSCLE [ 136 ] in MEGA v7.0.25.…”

Section: Methodsmentioning

confidence: 99%

Genome analysis of Pseudomonas sp. OF001 and Rubrivivax sp. A210 suggests multicopper oxidases catalyze manganese oxidation required for cylindrospermopsin transformation

et al. 2021

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Background Cylindrospermopsin is a highly persistent cyanobacterial secondary metabolite toxic to humans and other living organisms. Strain OF001 and A210 are manganese-oxidizing bacteria (MOB) able to transform cylindrospermopsin during the oxidation of Mn2+. So far, the enzymes involved in manganese oxidation in strain OF001 and A210 are unknown. Therefore, we analyze the genomes of two cylindrospermopsin-transforming MOB, Pseudomonas sp. OF001 and Rubrivivax sp. A210, to identify enzymes that could catalyze the oxidation of Mn2+. We also investigated specific metabolic features related to pollutant degradation and explored the metabolic potential of these two MOB with respect to the role they may play in biotechnological applications and/or in the environment. Results Strain OF001 encodes two multicopper oxidases and one haem peroxidase potentially involved in Mn2+ oxidation, with a high similarity to manganese-oxidizing enzymes described for Pseudomonas putida GB-1 (80, 83 and 42% respectively). Strain A210 encodes one multicopper oxidase potentially involved in Mn2+ oxidation, with a high similarity (59%) to the manganese-oxidizing multicopper oxidase in Leptothrix discophora SS-1. Strain OF001 and A210 have genes that might confer them the ability to remove aromatic compounds via the catechol meta- and ortho-cleavage pathway, respectively. Based on the genomic content, both strains may grow over a wide range of O2 concentrations, including microaerophilic conditions, fix nitrogen, and reduce nitrate and sulfate in an assimilatory fashion. Moreover, the strain A210 encodes genes which may convey the ability to reduce nitrate in a dissimilatory manner, and fix carbon via the Calvin cycle. Both MOB encode CRISPR-Cas systems, several predicted genomic islands, and phage proteins, which likely contribute to their genome plasticity. Conclusions The genomes of Pseudomonas sp. OF001 and Rubrivivax sp. A210 encode sequences with high similarity to already described MCOs which may catalyze manganese oxidation required for cylindrospermopsin transformation. Furthermore, the analysis of the general metabolism of two MOB strains may contribute to a better understanding of the niches of cylindrospermopsin-removing MOB in natural habitats and their implementation in biotechnological applications to treat water.

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Section: Methodsmentioning

confidence: 99%

Genome analysis of Pseudomonas sp. OF001 and Rubrivivax sp. A210 suggests multicopper oxidases catalyze manganese oxidation required for cylindrospermopsin transformation

et al. 2021

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“…Several genes have been identified as being involved in the coding of MCOs for Mn 2+ oxidation, including mofA in L. discophora SS-1, genes in the ccm operon of P. putida MnB1, mnxA, B, C, D, E, F, and G in P. putida SG-1; cumA in P. putida GB-1 [5]; moxA in Pedomicrobium sp. ACM 3067; mokA in Lysinibacillus strain MK-1; cotA in Bacillus pumilus WH4 [17]; cueO amplified from Escherichia coli [50]; and copA in B. panacihumi MK-8 [51]. Therefore, primers based on these functional proteins can be used to identify MnOB with the same protein gene, but further classification of MnOB still requires the assistance of 16S rRNA gene sequencing.…”

Section: Mnob Recognitionmentioning

confidence: 99%

“…However, there are currently no specifications for the design or operation of bioprocesses that can be referenced as a guide, which could result in a number of operational issues, such as excessive energy use. Moreover, in addition to groundwater purification, because the cycle in Figure 1 is regulated by numerous environmental factors [17], organic compounds such as antibiotics [18] and dyes [19] can be absorbed and degraded by biogenic MnO x (bioMnO x ). It possesses advantages over chemical approaches for the treatment of contaminated water since it is a natural biosorbent and oxidant.…”

Section: Introductionmentioning

confidence: 99%

A Review of Manganese-Oxidizing Bacteria (MnOB): Applications, Future Concerns, and Challenges

Cai

Yang

Qiu

et al. 2023

IJERPH

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Groundwater serving as a drinking water resource usually contains manganese ions (Mn2+) that exceed drinking standards. Based on the Mn biogeochemical cycle at the hydrosphere scale, bioprocesses consisting of aeration, biofiltration, and disinfection are well known as a cost-effective and environmentally friendly ecotechnology for removing Mn2+. The design of aeration and biofiltration units, which are critical components, is significantly influenced by coexisting iron and ammonia in groundwater; however, there is no unified standard for optimizing bioprocess operation. In addition to the groundwater purification, it was also found that manganese-oxidizing bacteria (MnOB)-derived biogenic Mn oxides (bioMnOx), a by-product, have a low crystallinity and a relatively high specific surface area; the MnOB supplied with Mn2+ can be developed for contaminated water remediation. As a result, according to previous studies, this paper summarized and provided operational suggestions for the removal of Mn2+ from groundwater. This review also anticipated challenges and future concerns, as well as opportunities for bioMnOx applications. These could improve our understanding of the MnOB group and its practical applications.

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“…In recent years, the over-exploitation of Mn ores and its widespread use in the steel industry have resulted in large discharges of Mn into surface waters, causing significant environmental pollution ( Huang et al, 2020 ; Wu et al, 2022 ). Soluble Mn(II) is the main form of Mn and is toxic, making its treatment crucial in Mn-polluted wastewater ( Tang et al, 2019 ). The concentration of Mn(II) in electrolytic manganese wastewater has been reported to reach 35.7 mM, with some even reaching a peak value of 268 mM, which is much higher than the World Health Organization’s standard Mn content for drinking water (<0.002 mM) ( Xu et al, 2014 ; Tang et al, 2019 ).…”

Section: Introductionmentioning

confidence: 99%

Efficient Mn(II) removal mechanism by Serratia marcescens QZB-1 at high manganese concentration

et al. 2023

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Manganese (Mn(II)) pollution has recently increased and requires efficient remediation. In this study, Serratia marcescens QZB-1, isolated from acidic red soil, exhibited high tolerance against Mn(II) (up to 364 mM). Strain QZB-1 removed a total of 98.4% of 18 mM Mn(II), with an adsorption rate of 71.4% and oxidation rate of 28.6% after incubation for 48 h. The strain synthesized more protein (PN) to absorb Mn(II) when stimulated with Mn(II). The pH value of the cultural medium continuously increased during the Mn(II) removal process. The product crystal composition (mainly MnO2 and MnCO3), Mn-O functional group, and element-level fluctuations confirmed Mn oxidation. Overall, strain QZB-1 efficiently removed high concentration of Mn(II) mainly via adsorption and showed great potential for manganese wastewater removal.

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Analysis of manganese oxidase and its encoding gene in Lysinibacillus strain MK-1

Cited by 15 publications

References 45 publications

Genome analysis of Pseudomonas sp. OF001 and Rubrivivax sp. A210 suggests multicopper oxidases catalyze manganese oxidation required for cylindrospermopsin transformation

Genome analysis of Pseudomonas sp. OF001 and Rubrivivax sp. A210 suggests multicopper oxidases catalyze manganese oxidation required for cylindrospermopsin transformation

A Review of Manganese-Oxidizing Bacteria (MnOB): Applications, Future Concerns, and Challenges

Efficient Mn(II) removal mechanism by Serratia marcescens QZB-1 at high manganese concentration

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