Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
Manganese is an essential trace element for humans, animals, and plants, but excessive amounts of manganese can cause serious harm to organisms. The biological manganese oxidation process mainly oxidizes Mn(II) through the secretion of unique manganese oxidase by manganese-oxidizing bacteria. The T1 Cu site of multicopper oxidase is the main site for substrate oxidation, and its role is to transfer electrons to TNC, where dioxygen reduction occurs. In this study, methionine (Met) No. 444 interacting with the T1Cu-coordinating amino acid in the multicopper oxidase CopA from Brevibacillus panacihumi MK-8 was mutated to phenylalanine (Phe) and leucine (Leu) by the enzyme. Based on the analysis of enzymatic properties and the structural model, the mutant protein M444F with 4.58 times the catalytic efficiency of the original protein CopA and the mutant protein M444L with 1.67 times the catalytic efficiency of the original protein CopA were obtained. The study showed that the manganese removal rate of the manganese-oxidizing engineered bacterium Rosetta-pET-copA cultured for 7 days was 88.87%, which was 10.77% higher than that of the original engineered bacterium. Overall, this study provides a possibility for the application of genetic engineering in the field of biological manganese removal.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s10532-024-10102-4 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Biofilm lifestyle across different lineages of ammonia-oxidizing archaea.
ISME J
September 2025
Department of Functional and Evolutionary Ecology, Archaea Biology and Ecogenomics Unit, University of Vienna, Djerassiplatz 1, 1030 Vienna, Austria.
Although ammonia-oxidizing archaea (AOA) are globally distributed in nature, growth in biofilms has been relatively little explored. Here we investigated six representatives of three different terrestrial and marine clades of AOA in a longitudinal and quantitative study for their ability to form biofilm, and studied gene expression patterns of three representatives. Although all strains grew on a solid surface, soil strains of the genera Nitrosocosmicus and Nitrososphaera exhibited the highest capacity for biofilm formation.
View Article and Find Full Text PDFA Deeper Insight into the Thermostability of a Novel Laccase Designed by Data-Driven Mining and Rational Engineering.
J Agric Food Chem
September 2025
School of Food & Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu Province 212013, China.
Laccases, as multicopper oxidases, play a pivotal role in lignin degradation and hold broad industrial promise in biorefineries, bioremediation, textiles, and pulp and paper processing. However, their use is limited by poor stability under harsh operational conditions. Here, we designed a novel thermostable laccase (WCotA) from by combining data-driven mining with rational engineering.
View Article and Find Full Text PDFKey roles in copper efflux and protein homeostasis of the intrinsically disordered region of a bacterial outer membrane channel.
J Biol Chem
September 2025
Research Unit in Biology of Microorganisms (URBM), Department of Biology, Namur Research Institute for Life Sciences (NARILIS), University of Namur, Namur, Belgium.
Metals like copper (Cu), zinc, and nickel exhibit dual nature, necessitating a tight regulation of their cellular homeostasis to meet physiological demands while preventing toxicity. In bacteria, metal homeostasis involves inner membrane (IM) P-type ATPases and ABC transporters, envelope-spanning tripartite efflux pumps, and outer membrane (OM) pore-forming proteins. Four decades ago, the OM β-barrel protein PcoB was shown to provide an additional layer of Cu resistance in an Escherichia coli strain isolated from the gut of swine fed with Cu supplements.
View Article and Find Full Text PDFDevelopment of SpyTag/SpyCatcher-driven thermostable cyclic laccase and its application in lignin and dye degradation and polymerization of phenolic compounds.
Sci China Life Sci
August 2025
International Joint Laboratory on Synthetic Biology and Biomass Biorefinery, Biofuels Institute, School of Emergency Management, School of the Environment and Safety Engineering, Jiangsu University, Zhenjiang, 212013, China.
Laccases, belonging to the superfamily of multicopper oxidases, can perform electron oxidation on a broad range of substrates, releasing only water as a by-product. Although instability and aggregation significantly constrain the industrial use of these eco-friendly biocatalysts, it is a daunting challenge for current engineering strategies to elevate these crucial enzymatic characteristics simultaneously. Here, we developed a cyclizing laccase (CyLacc) using SpyTag/SpyCatcher technology, which endows the enzyme with high thermostability and high solubility.
View Article and Find Full Text PDFPseudarthrobacter raffinosi sp. nov. and Pseudarthrobacter cellobiosi sp. nov. Two Heavy-Metal-Tolerant and Psychrotolerant Bacteria Isolated from Glaciers.
Curr Microbiol
August 2025
State Key Laboratory of Microbial Diversity and Innovative Utilization, Institute of Microbiology, Chinese Academy of Sciences, NO. 1 West Beichen, Chaoyang District, Beijing, 100101, People's Republic of China.
In a study on bacterial diversity on glacier surfaces in China, five bacterial strains (HLT1-5, HLT3-5, MDT3-26, MDT3-9, and MDT3-28) were isolated from soil samples collected from the surfaces of Hailuogou glacier and Midui glacier. Phylogenetic analysis based on 16S rRNA gene sequences placed these strains close to Pseudarthrobacter humi RMG13, Pseudarthrobacter psychrotolerans YJ56, and Pseudarthrobacter sulfonivorans ALL, with sequence similarity ranging from 98.98 to 100%.
View Article and Find Full Text PDF