Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis
| Autor: | Eliana Gertrudes de Macedo Lemos, Mariana Rangel Pereira, Elkin Fernando Rodas Mendoza, Elisangela Soares Gomes-Pepe, Elwi Guillermo Machado Sierra, Thaís Carvalho Maester |
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| Přispěvatelé: | Universidade Estadual Paulista (Unesp), Inst Res Bioenergy IPBEN, Univ Simon Bolivar |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Osmosis Aminopeptidase Quantitative Structure-Activity Relationship lcsh:Medicine Bacterial growth Sodium Chloride medicine.disease_cause Aminopeptidases Article Microbiology Evolution Molecular 03 medical and health sciences Enzyme activator medicine Enzyme kinetics Amino Acid Sequence lcsh:Science Escherichia coli Microbial Biofilms Multidisciplinary biology Chemistry lcsh:R Mesorhizobium Biofilm Genomics Sequence Analysis DNA Water-Electrolyte Balance biology.organism_classification Organic solvent product Recombinant Proteins Enzyme Activation Solutions 030104 developmental biology Biofilms Halotolerance lcsh:Q Protein Multimerization Genome Bacterial Biotechnology |
| Zdroj: | Web of Science Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017) Scientific Reports Vol. 7, No. 10684 (2017) Repositorio Digital USB Universidad Simón Bolívar instacron:Universidad Simón Bolívar |
| DOI: | 10.1038/s41598-017-10932-8 |
| Popis: | Made available in DSpace on 2018-11-26T17:40:31Z (GMT). No. of bitstreams: 0 Previous issue date: 2017-09-06 Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) The aminopeptidase gene from Mesorhizobium SEMIA3007 was cloned and overexpressed in Escherichia coli. The enzyme called MesoAmp exhibited optimum activity at pH 8.5 and 45 degrees C and was strongly activated by Co2+ and Mn2+. Under these reaction conditions, the enzyme displayed K-m and k(cat) values of 0.2364 +/- 0.018 mM and 712.1 +/- 88.12 s(-1), respectively. Additionally, the enzyme showed remarkable stability in organic solvents and was active at high concentrations of NaCl, suggesting that the enzyme might be suitable for use in biotechnology. MesoAmp is responsible for 40% of the organism's aminopeptidase activity. However, the enzyme's absence does not affect bacterial growth in synthetic broth, although it interfered with biofilm synthesis and osmoregulation. To the best of our knowledge, this report describes the first detailed characterization of aminopeptidase from Mesorhizobium and suggests its importance in biofilm formation and osmotic stress tolerance. In summary, this work lays the foundation for potential biotechnological applications and/or the development of environmentally friendly technologies and describes the first solvent- and halo-tolerant aminopeptidases identified from the Mesorhizobium genus and its importance in bacterial metabolism. Sao Paulo State Univ, Dept Technol, Jaboticabal, SP, Brazil Inst Res Bioenergy IPBEN, Jaboticabal, SP, Brazil Univ Simon Bolivar, Barranquilla, Colombia Av Prof Paulo Donato Castellane S-N, BR-14884900 Jaboticabal, SP, Brazil Sao Paulo State Univ, Dept Technol, Jaboticabal, SP, Brazil |
| Databáze: | OpenAIRE |
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