Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis
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Fecha
2017-09-06
Autores
Machado Sierra, Elwi
Rangel Pereira, Mariana
Carvalho Maester, Thaís
Soares Gomes-Pepe, Elisangela
Rodas Mendoza, Elkin
Macedo Lemos, Elkin
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Editor
Springer
Resumen
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 °C and was strongly
activated by Co2+ and Mn2+. Under these reaction conditions, the enzyme displayed Km and kcat
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.
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Palabras clave
Mesorhizobium, Aminopeptidase, Microbial Biofilms, Sodium Chloride, Osmosis, Biotechnology, Water-Electrolyte Balance, Organic solvent product