Low-resolution molecular shape, biochemical characterization and emulsification properties of a halotolerant esterase fr
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ORIGINAL ARTICLE
Low‑resolution molecular shape, biochemical characterization and emulsification properties of a halotolerant esterase from Bacillus licheniformis Ana Elisa T. Leite1 · Lorenzo Briganti1 · Evandro Ares de Araújo1 · Vanessa de Oliveira Arnoldi Pellegrini1 · Cesar Moyses Camilo1 · Igor Polikarpov1 Received: 5 December 2019 / Revised: 28 June 2020 / Accepted: 8 July 2020 © European Biophysical Societies’ Association 2020
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. Keywords Esterases · Bacillus licheniformis · Biochemical characterization · Small-angle X-ray scattering
Introduction Modern biotechnology is unthinkable without applications of enzymes. Currently, over 200 different enzymes, including carboxylic ester hydrolases, are used in industrial applications (Sharma 2011) for manufacturing a wide range of industrial products, in diverse areas such as (bio)chemical synthesis, pharmaceutical industry, food, feed and detergent additives (Adrio 2013). The commercial use of lipases and esterases has a wide variety of different applications including synthesis of biopolymer and biodiesel, production of pharmaceuticals, agrochemicals, cosmetics and flavors, having billion dollars value (Joseph, Ramteke and Thomas 2008). Carboxylic ester hydrolases (triacylglycerol acyl hydrolases EC 3.1.1.3) is a group of enzymes that frequently act at Electronic supplementary material The online version of this article (https://doi.org/10.1007/s00249-020-01448-7) contains supplementary material, which is available to authorized users. * Igor Polikarpov [email protected] 1
the lipid-water interface, catalyzing the disruption of triglyceride chains via hydrolysis of ester bonds. These reactions cause release of fatty acids and organic alcohols (Nthangeni 2001; KhyamiHorani 1996; Barros 2010). The enzymes can be further divided into lipases and esterases, which are present in diverse organisms, such as plants, yeasts, fungi and bacteria (Kumar 2005; Sharma 2001). Carboxylic ester hydrolases are widely applied in flavor and fragrancies production, drug synthesis, transesterification and hydrolysis of fats and oils and also in biosensor manufacturing (Pandey 1999; Wakelin 1997). Within the recent years, lipases have also been used as b
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