Abstract
Bacterial esterases are highly versatile enzymes, currently widely used in detergents, biosurfactants, bioemulsifiers and as biocatalysts in paper and food industries. Present work describes heterologous expression, purification, and biophysical and biochemical characterization of a halotolerant esterase from Bacillus licheniformis (BlEstA). BlEstA preferentially cleaves pNP-octanoate and both activity and stability of the enzyme increased in the presence of 2 M NaCl, and also with several organic solvents (ethanol, methanol and DMSO). Furthermore, BlEstA has considerable emulsifying properties, particularly with olive oil as substrate. Our studies also show that the enzyme is monomeric in solution and its small-angle X-ray scattering low-resolution molecular envelope fits well its high-resolution homology model.
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Acknowledgements
This research was supported by Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) via grant 2015/13684-0 and by Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) via grants 303988/2016-9 and 440977/2016-9. This research used resources of the Brazilian Synchrotron Light Laboratory (LNLS), an open national facility operated by the Brazilian Centre for Research in Energy and Materials (CNPEM) for the Brazilian Ministry for Science, Technology, Innovations, and Communications (MCTIC). The beamline staffs are acknowledged for assistance during the experiments. We also would like to thank Prof. Dr. Ana Paula Ulian de Araujo and Raissa Ferreira Gutierrez, who helped to carry out CD measurements.
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Leite, A.E.T., Briganti, L., de Araújo, E.A. et al. Low-resolution molecular shape, biochemical characterization and emulsification properties of a halotolerant esterase from Bacillus licheniformis. Eur Biophys J 49, 435–447 (2020). https://doi.org/10.1007/s00249-020-01448-7
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DOI: https://doi.org/10.1007/s00249-020-01448-7